Affinage

CD151

CD151 antigen · UniProt P48509

Length
253 aa
Mass
28.3 kDa
Annotated
2026-04-28
100 papers in source corpus 48 papers cited in narrative 48 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CD151 is a palmitoylated tetraspanin that serves as a master organizer of laminin-binding integrins (α3β1, α6β1, α6β4, α7β1), coupling them to signaling platforms, pericellular proteases, and endocytic trafficking machinery to control cell adhesion, migration, and basement membrane integrity. It directly binds these integrins via a QRD(194–196) motif in its large extracellular loop—forming detergent-resistant complexes early in biosynthesis that sustain an activated integrin conformation and potentiate laminin-binding activity—while DHHC2-mediated palmitoylation at N- and C-terminal cysteines governs its lateral assembly into tetraspanin-enriched microdomains, protein stability, and secondary associations with CD9, CD63, growth factor receptors (Met, EGFR/ErbB2), small GTPases (Rac1, Cdc42, Ras), and matrix metalloproteinases (MMP-7, MT1-MMP) (PMID:12356873, PMID:15677332, PMID:18508921, PMID:16200075, PMID:18663148, PMID:20937830, PMID:22843693). Through a cytoplasmic YRSL motif CD151 drives integrin internalization to regulate migration, and via its C-terminal tail and integrin-dependent signaling it modulates FAK, PI3K/Akt, Rac1/RhoA balance, and MAPK cascades in endothelial, epithelial, platelet, and immune cell contexts (PMID:17716972, PMID:17023588, PMID:21832275, PMID:24723389). Loss-of-function mutations in humans and mice cause glomerular basement membrane failure and nephropathy through weakened α3β1-mediated podocyte adhesion, and CD151-null mice additionally exhibit defective pathological angiogenesis, impaired wound healing, and attenuated airway hyperreactivity (PMID:15265795, PMID:22201679, PMID:17023588, PMID:16410781, PMID:27233153).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 1995 High

    Molecular cloning established CD151 (PETA-3) as a new tetraspanin superfamily member, providing the primary sequence framework (four transmembrane domains, large extracellular loop) needed for all subsequent structure–function studies.

    Evidence cDNA cloning from megakaryoblastic leukemia cells with sequence analysis

    PMID:7632941

    Open questions at the time
    • No functional data; no interacting partners identified
  2. 1999 High

    Demonstration that CD151 forms uniquely strong (digitonin-resistant) complexes with α3β1 and α6β1 integrins—unlike all other tetraspanins—established CD151 as the primary tetraspanin partner for laminin-binding integrins and raised the question of how this specificity is encoded.

    Evidence Reciprocal co-immunoprecipitation under digitonin, CHAPS, Brij 97 in multiple cell lines; epitope-blocking analysis

    PMID:10229664 PMID:9931299

    Open questions at the time
    • Binding domain not yet mapped
    • Functional consequences of the association unclear
  3. 2001 High

    Mapping the integrin-binding site to the large extracellular loop—and subsequently to the QRD(194–196) residues—resolved how CD151 achieves direct, high-affinity integrin recognition, and showed this occurs early in biosynthesis with integrin precursors.

    Evidence Chimera/deletion/point mutagenesis of CD151 LEL; co-immunoprecipitation under Triton X-100; biosynthetic pulse-chase

    PMID:11479292 PMID:12356873

    Open questions at the time
    • No atomic structure of the complex
    • How QRD contacts the integrin α-subunit unknown
  4. 2002 High

    Identification of palmitoylation at C11/C15/C242/C243 and the C-terminal tail as functionally separable domains resolved how CD151 simultaneously performs two roles: direct integrin binding (palmitoylation-independent) and lateral assembly into tetraspanin-enriched microdomains/signaling (palmitoylation-dependent).

    Evidence Site-directed mutagenesis; [³H]palmitate labeling; C-terminal deletion/exchange mutants; co-IP and functional Matrigel assays

    PMID:11809818 PMID:11907260

    Open questions at the time
    • Palmitoyl transferase not yet identified
    • Stoichiometry of tetraspanin web assembly unclear
  5. 2002 High

    Extension of the CD151–integrin partnership to α7β1 and demonstration that the integrin-binding epitope is masked in tissues in vivo established that CD151 is the universal tetraspanin partner for all laminin-binding integrins under physiological conditions.

    Evidence Co-immunoprecipitation with α7β1; immunostaining of tissue sections with epitope-mapped antibody TS151r

    PMID:11884516

    Open questions at the time
    • Functional significance of α7β1 partnership not tested in vivo
  6. 2004 High

    CD151-null mice and human loss-of-function patients demonstrated that CD151 is essential for glomerular and tubular basement membrane integrity and platelet outside-in signaling, establishing physiological non-redundancy.

    Evidence Cd151-knockout mice with renal histopathology and EM; human frameshift mutation (G383 insertion) analysis; KO platelet functional assays

    PMID:15226180 PMID:15265795 PMID:17015618

    Open questions at the time
    • Strain-dependent penetrance (FVB vs B6) unexplained
    • Whether renal phenotype is purely α3β1-dependent or involves other integrins
  7. 2005 High

    Reconstitution experiments and FRET imaging showed that CD151 actively sustains an activated integrin conformation that enhances laminin-binding, transforming the view of CD151 from a passive scaffold to an allosteric regulator of integrin activity.

    Evidence Antibody-mediated CD151 dissociation; reconstitution of purified CD151 with α3β1; siRNA; FRET on live cells; adhesion assays

    PMID:15677332

    Open questions at the time
    • Structural basis of conformational stabilization unknown
    • Whether this applies equally to α6β4
  8. 2005 High

    Discovery that CD151 recruits and activates proMMP-7 at the cell surface expanded its role beyond adhesion to pericellular proteolysis, with subsequent work showing MT1-MMP also forms ternary complexes with CD151–α3β1.

    Evidence Yeast two-hybrid; co-IP; ¹²⁵I-proMMP-7 binding; in situ zymography; FRET for MT1-MMP–CD151 in endothelial cells

    PMID:16200075 PMID:18663148

    Open questions at the time
    • How CD151 activates proMMP-7 catalytically is unclear
    • Whether protease recruitment is palmitoylation-dependent
  9. 2006 High

    CD151-null mouse phenotyping in angiogenesis, wound healing, and signaling demonstrated that CD151 couples laminin-binding integrins to PKB/Akt, eNOS, and Rac/Cdc42 activation in a context-specific manner—required for pathological but not developmental angiogenesis.

    Evidence CD151-null mice; Matrigel plug, corneal micropocket, aortic ring assays; wound healing; isolated endothelial cell signaling on laminin

    PMID:16410781 PMID:17023588

    Open questions at the time
    • Why developmental angiogenesis is spared is mechanistically unexplained
    • Compensating tetraspanins not identified
  10. 2007 High

    Identification of the YRSL endocytosis motif in CD151's cytoplasmic tail established a direct mechanism by which CD151 controls integrin internalization and recycling to promote cell migration.

    Evidence YRSL→AASL mutagenesis; endocytosis and co-localization assays; migration on ECM

    PMID:17716972

    Open questions at the time
    • Adaptor protein recognizing YRSL not identified
    • Recycling route (early/late endosome) not defined
  11. 2008 High

    DHHC2 was identified as the specific palmitoyl acyltransferase for CD151, closing the palmitoylation circuit and showing that DHHC2-mediated palmitoylation protects CD151 from lysosomal degradation and enables tetraspanin web assembly.

    Evidence DHHC2 overexpression/knockdown with catalytic-dead mutants; [³H]palmitate labeling; co-IP; lysosomal inhibitor rescue

    PMID:18508921

    Open questions at the time
    • Whether DHHC2 is the sole palmitoyltransferase for CD151 in all cell types
    • Depalmitoylation enzyme unknown
  12. 2008 High

    Discovery that CD151 controls α3 integrin N-glycosylation revealed an unexpected biosynthetic role: CD151 influences the glycan structure of its integrin partner, which in turn affects laminin-binding and migration.

    Evidence CD151 knockdown and N159Q glycosylation mutant rescue; lectin-based glycan profiling; migration on laminin-332

    PMID:18852263

    Open questions at the time
    • Glycosyltransferase(s) affected by CD151 not identified
    • Whether α6 glycosylation is similarly regulated
  13. 2010 High

    Demonstration that CD151 bridges integrins to Met (HGF receptor) and modulates ErbB2/EGFR signaling complexes expanded its role to a platform connecting adhesion receptors with growth factor receptor tyrosine kinases.

    Evidence Co-IP of Met–β4 complexes ± CD151 RNAi; ErbB2 phosphorylation and resistance assays with trastuzumab; FAK/Akt/Erk readouts

    PMID:20197472 PMID:20937830

    Open questions at the time
    • Whether CD151 directly contacts RTKs or acts indirectly through integrins
    • Structural basis of RTK–integrin–CD151 ternary complex
  14. 2011 High

    CD151 was shown to balance Rac1/RhoA GTPase activity in endothelial cells and podocytes, with CD151 loss elevating RhoA and destabilizing cell–cell and cell–matrix adhesion—a unifying mechanism explaining vascular instability and podocyte detachment phenotypes.

    Evidence CD151-null mice and siRNA in HUVECs; RhoA/Rac1 activity assays; pharmacological RhoA inhibition rescue; podocyte-specific conditional KO with hypertension challenge

    PMID:21832275 PMID:22201679

    Open questions at the time
    • GEF/GAP mediating CD151-dependent Rac1/RhoA balance not identified
    • Whether RhoA dysregulation explains strain-dependent renal phenotype
  15. 2012 High

    Ternary complex formation between CD151–integrins and small GTPases (Ras, Rac1, Cdc42) at the membrane, enhanced by laminin adhesion, established CD151 as a scaffold organizing signaling nanoclusters that couple adhesion to motility and MMP expression.

    Evidence Reciprocal co-IP of integrin–CD151–GTPase complexes; GTPase activation assays; comparison across four tetraspanins

    PMID:22843693

    Open questions at the time
    • Direct vs. indirect GTPase binding not resolved
    • Stoichiometry of signaling nanocluster unknown
  16. 2012 High

    Genetic epistasis in tumor models (ErbB2-driven mammary and chemical skin carcinogenesis) demonstrated that CD151 supports PKCα–β4 S1424 phosphorylation, STAT3 activation, and loss of epithelial polarity during tumor initiation, establishing CD151 as a gatekeeper for integrin-dependent oncogenic signaling.

    Evidence CD151-null × MMTV-ErbB2 mice; two-stage chemical carcinogenesis; PKCα–α6β4 co-IP; β4 phosphorylation and STAT3 assays

    PMID:22824799 PMID:22952421

    Open questions at the time
    • Whether CD151's tumor-promoting role is integrin-dependent or partially integrin-independent
    • Therapeutic targetability not tested with CD151-specific agents
  17. 2016 High

    CD151's role was extended beyond integrins to GPCR-driven calcium signaling and PKC membrane translocation in airway smooth muscle, demonstrating tissue-specific functions in contractile responses and allergen-induced airway hyperreactivity.

    Evidence CD151-null mouse allergen challenge; intracellular Ca²⁺ measurements; PKC translocation assays in airway smooth muscle cells

    PMID:27233153

    Open questions at the time
    • Which GPCR specifically requires CD151 not defined
    • Whether smooth muscle function involves integrin partnership
  18. 2019 Medium

    Separation of integrin-dependent and integrin-independent CD151 functions was achieved: CD151 stabilizes hybrid adhesion structures via α3β1 in keratinocytes and supports drug resistance through an integrin-binding-independent mechanism, indicating that intracellular CD151 has autonomous cytoprotective activity.

    Evidence CD151-KO keratinocytes with TIRF microscopy; QRD mutant reconstitution showing equal anti-apoptotic activity as WT in drug resistance assays

    PMID:30778617 PMID:31488507

    Open questions at the time
    • Integrin-independent cytoprotective mechanism not defined at the molecular level
    • Whether intracellular CD151 pool has distinct binding partners
  19. 2024 Medium

    CD151 was identified as a promoter of migrasome formation in hepatocellular carcinoma, with VEGF-enriched migrasomes driving angiogenesis and metastasis, linking CD151's membrane-organizing function to extracellular vesicle biogenesis.

    Evidence CD151 overexpression/knockdown; migrasome imaging; VEGF quantification; in vivo metastasis models

    PMID:38840183

    Open questions at the time
    • Whether migrasome formation requires CD151–integrin association or palmitoylation
    • Migrasome biogenesis mechanism not resolved at the molecular level

Open questions

Synthesis pass · forward-looking unresolved questions
  • Despite extensive functional characterization, no high-resolution structure of a CD151–integrin complex exists, the GEFs/GAPs mediating CD151-dependent Rac1/RhoA balance are unidentified, the adaptor engaging the YRSL trafficking motif is unknown, and the molecular basis of integrin-independent cytoprotective functions remains undefined.
  • No atomic structure of CD151–integrin complex
  • Adaptor protein for YRSL motif unknown
  • Integrin-independent survival mechanism molecularly undefined
  • GEF/GAP linking CD151 to Rho GTPase regulation not identified

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0098772 molecular function regulator activity 3 GO:0008289 lipid binding 2
Localization
GO:0005886 plasma membrane 5 GO:0005794 Golgi apparatus 2 GO:0031410 cytoplasmic vesicle 2
Pathway
R-HSA-162582 Signal Transduction 6 R-HSA-1500931 Cell-Cell communication 4 R-HSA-1474244 Extracellular matrix organization 3 R-HSA-168256 Immune System 2 R-HSA-9609507 Protein localization 2 R-HSA-109582 Hemostasis 1
Partners
CD9ITGA3ITGA6ITGA7ITGB4MMP14MMP7ZDHHC2
Complex memberships
CD151–α3β1 integrin complexCD151–α6β1 integrin complexCD151–α6β4 integrin complexTetraspanin-enriched microdomain (TEM)

Evidence

Reading pass · 48 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1995 CD151 (PETA-3) was cloned and identified as a member of the Tetraspan/Transmembrane 4 superfamily, encoding a 253 amino acid protein with four transmembrane domains and a large extracellular loop containing a single N-linked glycosylation site. cDNA cloning from megakaryoblastic leukemia cell line library, Northern blot, sequence analysis Blood High 7632941
1999 CD151 forms direct, digitonin-resistant complexes specifically with integrin α3β1 and α6β1, distinguishing it from other tetraspanins whose integrin associations are disrupted by digitonin; the anti-CD151 mAb TS151r epitope is blocked upon integrin association, suggesting the integrin-binding site on CD151. Reciprocal immunoprecipitation in multiple cell lines under digitonin, CHAPS, Brij 97 conditions; epitope-blocking analysis The Biochemical Journal High 10229664
1999 CD151 associates with integrins α4β1, α5β1, α6β1, and αIIbβ3 in haemopoietic cell lines; antibody-induced CD151 ligation triggers homotypic cell-cell adhesion dependent on energy and cytoskeletal integrity, without upregulating integrin avidity for ECM ligands. Co-immunoprecipitation with CHAPS detergent; functional adhesion assays with F(ab')2 antibody fragments; blocking mAbs The Biochemical Journal Medium 9931299
2000 CD151 is concentrated in hemidesmosomes in human skin, where it associates with α6β4 integrin; recruitment of CD151 into hemidesmosomes requires the α6 subunit of integrin (via β4 chimera experiments), and CD151 is the only tetraspanin identified in hemidesmosomal structures. Immunoelectron microscopy; immunoprecipitation from transfected K562 cells; β4 chimera transfection into PA-JEB keratinocytes The Journal of Cell Biology High 10811835
2001 The integrin-binding site on CD151 maps to the large extracellular loop (LECL, residues Leu149–Glu213); substitution of 11 amino acids (residues 195–205) or point mutations in conserved CCG and PXXCC cysteine motifs abolish α3β1 interaction; CD151 assembly into the tetraspanin web occurs later and is governed by different structural requirements than integrin binding. CD151/CD9 chimeras and deletion mutants; Triton X-100 co-immunoprecipitation; mutagenesis of CCG motif The Journal of Biological Chemistry High 11479292
2002 Palmitoylation of CD151 occurs at intracellular N-terminal and C-terminal cysteine residues (C11, C15, C242, C243) in Golgi/post-Golgi compartments. Palmitoylation is not required for α3β1 association but is critical for lateral associations with other tetraspanins (CD9, CD63) and for CD151 stability; the palmitoylation-deficient mutant is diffusely distributed and profoundly alters α3 integrin-dependent cell morphology. Site-directed mutagenesis of cysteine residues; [3H]palmitate labeling; co-immunoprecipitation; immunofluorescence; biosynthetic stability assays Molecular Biology of the Cell High 11907260
2002 An extracellular site QRD(194-196) on CD151 is required for strong (Triton X-100-resistant) lateral association with α3β1 and α6β1 integrins; this strong association occurs early in biosynthesis with integrin precursors and is required for CD151-mediated cellular network formation and cell spreading on Matrigel. QRD→INF mutagenesis; co-immunoprecipitation under Triton X-100 vs Brij 96; biosynthetic pulse-chase; functional Matrigel assays in Cos7 and NIH3T3 cells The Journal of Cell Biology High 12356873
2002 The CD151–α6β1 integrin complex functions as a unit in cellular morphogenesis on basement membrane Matrigel; deletion or exchange of the short 8-amino acid C-terminal CD151 tail exerts a dominant-negative effect on α6β1-dependent cell network formation and spreading on laminin-1, without disrupting integrin association or adhesion. C-terminal deletion/exchange mutants transfected into NIH3T3 cells; anti-integrin antibody inhibition assays; Matrigel network formation assay Molecular Biology of the Cell High 11809818
2002 CD151 associates with laminin-binding integrin α7β1 with comparable strength to α3β1 and α6β1; complex formation uses all splice variants of α3, α6, α7 subunits; the TS151r epitope (at the integrin-binding site) is masked in most tissues co-expressing laminin-binding integrins, demonstrating in vivo complex formation. Co-immunoprecipitation; transfection of K562 cells; immunostaining with epitope-mapped antibodies on tissue sections Journal of Cell Science High 11884516
2003 CD151 expression specifically attenuates adhesion-dependent activation of Ras and downstream PKB/Akt and ERK1/2 in rat fibroblasts, while not affecting FAK or Src activation; the cytoplasmic C-terminal portion of CD151 is critical for this negative regulatory activity. CD151 overexpression in rat fibroblasts; Ras activity assays; C-terminal deletion mutants; Western blotting for downstream signaling The Journal of Biological Chemistry Medium 12782641
2004 Loss of CD151 in mice impairs outside-in αIIbβ3 integrin signaling in platelets, resulting in defective platelet aggregation, spreading on fibrinogen, and delayed clot retraction, while inside-out signaling remains intact; constitutive CD151–αIIbβ3 physical association is demonstrated. CD151-null mouse platelets; co-immunoprecipitation/Western blot; platelet aggregation, spreading, clot retraction assays; FITC-fibrinogen binding (inside-out); JON/A antibody; Ca2+ and IP3 measurements Blood High 15226180
2004 CD151 null mice develop massive proteinuria and focal glomerulosclerosis with age due to disorganization of the glomerular basement membrane; podocyte-specific α3 integrin knockout mice recapitulate this phenotype, demonstrating that CD151 strengthens α3β1-mediated adhesion in podocytes. CD151-null mouse generation; podocyte-specific conditional α3 integrin knockout mice; histopathology; electron microscopy; immunostaining The Journal of Cell Biology High 17015618
2004 CD151 null mice show a homozygous single-nucleotide insertion (G383) in human patients causing frameshift/premature stop before the integrin-binding domain, leading to loss of laminin-binding integrin complexes in kidney and skin, establishing CD151 as essential for glomerular and tubular basement membrane assembly. Genetic analysis of MER2-negative patients; immunoprecipitation in patient-derived tissues; histology/electron microscopy of kidney and skin Blood High 15265795
2005 CD151 association with α3β1 integrin potentiates the ligand-binding activity of α3β1 to laminin-10/11 by sustaining an activated integrin conformation; CD151-free integrin shows reduced laminin-binding and reduced activated β1 epitope, which is restored upon CD151 reassociation; FRET imaging confirms dissociation on live cell surfaces. Anti-CD151 mAb 8C3-mediated dissociation of CD151 from purified α3β1; integrin activity assays with reconstituted CD151; siRNA knockdown; FRET imaging on live cells; cell adhesion assays Proceedings of the National Academy of Sciences USA High 15677332
2005 CD151 interacts via its COOH-terminal extracellular loop with the propeptide of proMMP-7 (promatrilysin-1), capturing and activating proMMP-7 on the cell membrane; CD151-dependent pericellular MMP-7 activity was abolished by anti-CD151 or anti-MMP-7 antibodies. Yeast two-hybrid screen; co-immunoprecipitation; [125I]-proMMP-7 binding assay; confocal colocalization; in situ zymography with MMP inhibitors and blocking antibodies Laboratory Investigation High 16200075
2006 Dissociation of the CD151–integrin complex (via TS151r antibody targeting the integrin-binding site) permits rearrangement of the actin cytoskeleton, dismantling of cell-matrix contacts, and cell migration; free (integrin-unbound) CD151 is present at intercellular contacts in migrating hair follicle epithelial cells but absent in resting interfollicular epidermis. Antibody blocking of CD151–integrin interface; actin cytoskeleton imaging; in vivo immunostaining of resting vs. migrating epithelial compartments Experimental Cell Research Medium 16490193
2006 CD151 deletion impairs pathologic angiogenesis (not developmental angiogenesis) in vivo; CD151-null endothelial cells show defective adhesion-dependent activation of PKB/Akt, eNOS, Rac, and Cdc42 on laminin substrate, while ERK, p38, FAK, Src signaling are unaltered; CD151 is required for molecular connections between laminin-binding integrins and ≥5 other proteins. CD151-null mouse; Matrigel plug, corneal micropocket, tumor implantation, aortic ring assays; isolated mouse lung endothelial cells; laminin substrate signaling assays; co-immunoprecipitation Blood High 17023588
2006 CD151 regulates wound healing by supporting keratinocyte migration and basement membrane organization; CD151-null mice show impaired re-epithelialization, disorganized laminin deposition, and blunted upregulation of α6 and β4 integrins at the wound edge. CD151-null mice; wound healing assay; immunostaining for laminin and integrins; spatiotemporal analysis of CD151 expression The Journal of Investigative Dermatology High 16410781
2006 Homophilic CD151–CD151 interactions between cells stimulate integrin-dependent signaling through FAK→Src→p38 MAPK/JNK→c-Jun axis, leading to increased MMP-9 expression and AP-1 transcription; this requires prior activation of associated α3β1/α6β1 integrins. CD151 transfection into CD151-negative melanoma cells; co-immunoprecipitation; kinase inhibitors and siRNA targeting FAK, Src, p38, JNK; AP-1/MMP-9 promoter reporter; homotypic adhesion assays The Journal of Biological Chemistry Medium 16798740
2007 CD151 promotes cell migration via a YRSL (YXXφ) endocytosis motif in its C-terminal cytoplasmic domain; this motif mediates CD151 internalization and co-internalization of associated α3β1, α5β1, and α6β1 integrins into the same vesicular compartments; mutation of YRSL abolishes CD151 internalization and CD151-promoted migration. YRSL→AASL mutagenesis; endocytosis assays; co-localization of CD151 and integrins in vesicles by immunofluorescence; cell migration assays on ECM The Journal of Biological Chemistry High 17716972
2008 DHHC2, a Golgi-resident palmitoyl acyltransferase, specifically palmitoylates CD151 and CD9; DHHC2 physically associates with CD151; DHHC2 knockdown reduces CD151 palmitoylation; DHHC2-mediated palmitoylation promotes CD151–CD9 association, protects CD151 from lysosomal degradation, and shifts cells toward cell-cell contact formation. DHHC2 overexpression/knockdown; catalytically inactive DHHC2 (DH→AA; C→S) mutants; [3H]palmitate labeling; co-immunoprecipitation; lysosomal inhibitor experiments; cell morphology assays Molecular Biology of the Cell High 18508921
2008 MT1-MMP associates with CD151 through its hemopexin domain, forming α3β1/CD151/MT1-MMP ternary complexes at endothelial junctions; CD151 knockdown enhances MT1-MMP–mediated MMP2 activation but diminishes collagen degradation at the cell periphery by disrupting MT1-MMP subcellular localization and its association with detergent-resistant microdomains. siRNA knockdown of CD151 in HUVECs and ex vivo CD151-null endothelial cells; FRET; co-immunoprecipitation; collagen degradation assays; MT1-MMP localization by immunofluorescence Blood High 18663148
2008 CD151 specifically regulates N-glycosylation of α3β1 integrin (Fucα1-2Gal and bisecting GlcNAc linkages on α3 subunit), not other CD151-associated proteins; this glycosylation function requires direct integrin contact and glycosylation of CD151 itself at Asn159; changes in α3 glycosylation caused by CD151 depletion correlate with reduced laminin-332 migration. CD151 knockdown and mutant rescue (N159Q glycosylation mutant, QRD integrin-binding mutant); lectin-based glycan analysis; glycosylation-deficient CD151 re-expression; cell migration assays The Journal of Biological Chemistry High 18852263
2008 CD151 ablation redistributes α6β4 integrin subcellularly, severs molecular links between integrins and tetraspanin-enriched microdomains, and reduces signaling through FAK, Rac1, and Lck while disrupting EGFR–α6 integrin collaboration in basal-like mammary cells. CD151 siRNA ablation; subcellular fractionation; co-immunoprecipitation; signaling Western blots; xenograft tumor models Cancer Research High 18451146
2008 CD151 deletion in mice causes severe glomerular disease on FVB but not B6 background; CD151 co-localizes with α3-integrin at podocyte foot process attachment sites; earliest lesions are GBM thickening and splitting, followed by podocyte foot process effacement. Cd151-null mice on two genetic backgrounds; electron microscopy; immunostaining for CD151, α3 integrin; histopathology; proteinuria measurement The American Journal of Pathology High 18787104
2008 CD151 knockdown reduces α3β1 integrin bulk extractability, disrupts α3β1 association with tetraspanin-enriched microdomains, impairs α3β1 internalization during migration on laminin-5, and causes persistent lateral adhesive contacts; CD151 re-expression reverses these defects. Retroviral RNAi; detergent extractability assays; integrin internalization assays; live cell migration imaging; re-expression rescue Molecular Biology of the Cell High 16571677
2010 CD151 is required for formation of signaling complexes between Met (HGF receptor) and β4 integrin; CD151 depletion impairs HGF-induced β4 phosphorylation, Grb2-Gab1 association, and MAPK (but not AKT) activation, thereby inhibiting HGF-driven proliferation and anchorage-independent growth. RNAi-mediated CD151 silencing; co-immunoprecipitation of Met–β4 complexes; phosphorylation assays; signaling pathway analysis; xenograft models The Journal of Biological Chemistry High 20937830
2010 CD151 knockdown, together with trastuzumab, inhibits ErbB2 activation and downstream FAK, Akt, and Erk1/2 signaling; the laminin-5–integrin–CD151–FAK axis confers resistance to ErbB2-targeting agents in ErbB2+ breast cancer cells. CD151 knockdown; pharmacological inhibition of FAK/integrin; trastuzumab/lapatinib resistance assays; Western blot for ErbB2 phosphorylation and downstream signals Cancer Research Medium 20197472
2010 CD151 re-expression with a series of mutants shows that both CD151–integrin association (QRD motif) and CD151–tetraspanin association (palmitoylation sites) are required for α3β1-dependent migration; only CD151–integrin association is required for stable α6β4-dependent adhesion on laminin-332. RNAi silencing of endogenous CD151 with re-expression of QRD and palmitoylation mutants; cell adhesion and migration assays on laminin-332 The Journal of Biological Chemistry High 21193415
2011 CD151 maintains vascular stability by promoting endothelial cell-cell adhesion and confining RhoA-driven cytoskeletal tension; CD151 loss elevates RhoA signaling and reduces Rac1 activity; RhoA inhibition or cAMP activation stabilizes CD151-null endothelial structures. CD151-null mice; CD151 siRNA in HUVECs; RhoA/Rac1 activity assays; vascular permeability assays; pharmacological RhoA inhibition rescue experiments Blood High 21832275
2011 CD151 (in podocytes) interacts with integrin α3β1 in situ in humans; podocyte-specific CD151 deletion reduces adhesive strength to laminin and redistributes α3β1 at the cell-matrix interface; blood pressure elevation triggers nephropathy in otherwise-resistant global Cd151-null B6 mice, establishing CD151 as a modifier of integrin-mediated podocyte adhesion strength. Human kidney co-immunoprecipitation; podocyte-specific Cd151 conditional KO; isolated glomerular epithelial cell adhesion assays; hypertension induction model; ACE inhibitor rescue The Journal of Clinical Investigation High 22201679
2011 CD151 amplifies laminin-5–stimulated PI3K–Akt–Snail signaling via the α6β1 integrin complex, inducing epithelial-mesenchymal transition (EMT) in HCC cells; this requires co-expression of both α6 and CD151; PI3K inhibition or antibodies against CD151/α6 reverse EMT. Immunoprecipitation (α6–CD151 complex); RNAi; pharmacological PI3K inhibition; in vitro and in vivo invasion/migration assays; EMT marker analysis Gastroenterology Medium 21320503
2012 CD151 facilitates molecular association between β1 integrins and small GTPases Ras, Rac1, and Cdc42 (but not Rho) at the cell membrane, forming α3β1/α6β1–CD151–GTPase complexes; cell adhesion to laminin enhances this complex formation, enabling FAK/Src-dependent GTPase activation that drives MMP-9 expression and motility. Co-immunoprecipitation of CD151–integrin–GTPase complexes; GTPase activation assays; CD151 siRNA; comparison of 4 tetraspanins; homophilic adhesion experiments The Journal of Biological Chemistry High 22843693
2012 CD151 supports ErbB2-driven mammary tumor onset and metastasis via α6β4 integrin; CD151 deletion prevents PKC- and EGFR/ERK-dependent α6β4 phosphorylation at S1424 and retains epithelial polarity; CD151 ablation reduces FAK and MAPK pathway activation during tumor initiation. CD151-null mice crossed with MMTV-ErbB2 transgene; 3D colony assays; signaling Western blots; in vivo tumor latency; histological analysis of metastasis Neoplasia High 22952421
2012 CD151 supports de novo skin squamous cell carcinoma by activating STAT3 and supporting PKCα–α6β4 integrin association and PKC-dependent β4 S1424 phosphorylation, redistributing α6β4 away from a polarized state toward a less-polarized, invasive configuration. Two-stage chemical carcinogenesis in CD151-null vs wild-type mice; PKCα–α6β4 co-immunoprecipitation; β4 phosphorylation assays; STAT3 activation assays Oncogene High 22824799
2013 Integrin α3β1–CD151 complexes regulate ErbB2 dimerization and phosphorylation through RhoA; depletion of α3β1 or CD151 elevates RhoA, reduces ErbB2 dimerization, and diminishes Herceptin-dependent ErbB2 dephosphorylation; Herceptin efficacy is enhanced in cells expressing both α3β1 and CD151. α3β1 and CD151 siRNA depletion; 3D laminin-rich ECM cultures; ErbB2 dimerization assays; RhoA activity measurement; Herceptin treatment Oncogene Medium 23792450
2013 CD151 associates more efficiently than Tspan8 with proteases MMP9 and MMP13, promoting their activation and collagen I/IV/laminin111 degradation; Tspan8, via distinct β4 integrin recruitment and FAK/Src/Ras activation, overrides the adhesive features of CD151-α3β1 to promote motility. Knockdown of CD151 or Tspan8 in rat pancreatic adenocarcinoma cells; co-immunoprecipitation of integrin/tetraspanin/protease complexes; collagen degradation assays; β4 phosphorylation; FAK/Src/Ras activation European Journal of Cancer Medium 23683890
2014 CD151–α3β1 integrin complexes suppress ovarian cancer growth by repressing Slug-mediated EMT and inhibiting canonical Wnt signaling (β-catenin, Axin-2 levels); CD151 or α3 knockdown increases β-catenin-dependent transcription, Slug expression, E-cadherin loss, and tumor growth in vivo. CD151/α3 RNAi; Slug knockdown epistasis; β-catenin reporter assay; in vivo xenograft; EMT marker analysis; clinical specimen analysis Oncotarget Medium 25356755
2014 CD151 and CD9 concentrate at the T-cell side of the immunological synapse; silencing CD151 reduces α4β1 integrin relocalization to the IS and decreases high-affinity β1 integrin accumulation there, accompanied by diminished FAK and ERK1/2 phosphorylation and blunted IL-2 secretion and CD69 upregulation. CD151 siRNA; immunofluorescence of IS formation; integrin high-affinity conformer detection; FAK/ERK phosphorylation Western blots; IL-2 ELISA European Journal of Immunology Medium 24723389
2016 CD151 binds integrin αvβ3 via its EC2 domain at the classical RGD ligand-binding site (specificity loop of β3); the constant region helices A and B (not the variable region) mediate this interaction; Lys residues at positions 116 and 144/148 of CD81 EC2 are critical for binding, as predicted by docking and confirmed by mutagenesis. EC2 domain adhesion assay; cRGDfV inhibitor; mAb 7E3 (ligand-binding site of β3) blocking; docking simulation; site-directed mutagenesis of CD81 EC2 at αvβ3-binding interface The Biochemical Journal Medium 27993971
2016 CD151 is required for GPCR-induced peak intracellular calcium release in airway smooth muscle cells and supports PKC translocation to the cell membrane; CD151-null mice are refractory to allergen-induced airway hyperreactivity, establishing CD151 as a positive regulator of Ca2+/PKC-mediated smooth muscle contraction. CD151 gain/loss-of-function in ASM cells; intracellular Ca2+ measurements; PKC translocation assays; CD151-null mouse allergen challenge model The Journal of Allergy and Clinical Immunology High 27233153
2019 CD151, through binding α3β1, stabilizes a hybrid adhesion structure containing CD151–α3β1/α6β4/plectin complexes (not anchored to keratin filaments) in the central region of keratinocytes; canonical hemidesmosomes (keratin-anchored, containing BP180 and BP230) do not require CD151 for formation. CD151 knockout keratinocytes; immunofluorescence; TIRF microscopy; co-immunoprecipitation; integrin rescue experiments Journal of Cell Science High 31488507
2019 CD151 supports drug resistance independent of integrin binding; the CD151-QRD mutant (diminished integrin association) and wild-type CD151 equally protect cells from gefitinib/camptothecin-induced apoptosis; anti-cancer drug treatment selectively upregulates non-integrin-associated intracellular CD151. CD151 ablation in multiple tumor lines; CD151-QRD mutant reconstitution; α3/α6 integrin ablation comparison; caspase-3, PARP, annexin V, PI staining; drug sensitivity assays Cellular and Molecular Life Sciences Medium 30778617
2019 CD151 induces p38 expression, a negative regulator of cardiomyocyte proliferation; miR-199a-3p directly targets Cd151 mRNA, suppressing its expression; Cd151 gain-of-function reduces cardiomyocyte proliferation while Cd151 loss-of-function increases it; pharmacological p38 inhibition rescues CD151-induced proliferation block. miR-199a-3p mimics/luciferase reporter (target validation); Cd151 overexpression/knockdown in cardiomyocytes; p38 expression/activity assays; p38 inhibitor rescue; cell cycle analysis Biochemical and Biophysical Research Communications Medium 31186138
2019 CD151 forms a complex with α6β4 integrin and interacts with EGFR in T cells; CD151 forms complexes with VLA-4 and LFA-1 integrins in T lymphocytes; CCL2 suppresses CD151 expression and dissociates CD151–integrin complexes, attenuating T-cell migration; a CD151 extracellular loop peptide inhibits T-cell migration in vitro and in vivo and reduces colitis severity. Co-immunoprecipitation of CD151–VLA-4 and CD151–LFA-1 complexes; CD151 peptide inhibitor design; T-cell migration assays; DSS colitis model Inflammatory Bowel Diseases Medium 26529559
2020 CD151 stimulates monocyte recruitment to inflammatory breast cancer cells via midkine secretion; CD151 increases midkine production, and CD151-associated extracellular vesicles attract monocytes; midkine antibody blocks EV chemoattractant activity, placing CD151→midkine→EV as a pathway regulating immune microenvironment. In vitro monocyte migration assays; midkine antibody blocking; EV isolation; chemokine profiling; CD151 KD in IBC xenografts; macrophage infiltration quantification The Journal of Pathology Medium 32129471
2021 CD151 regulates the ERK/Nrf2 antioxidant pathway in trophoblast cells; CD151 knockdown reduces HO-1, NQO-1, GCLC, and SOD-1 expression; ERK or Nrf2 inhibition abolishes the protective effect of CD151 on antioxidant gene expression; downregulation of CD151 in mouse placentas mimics preeclampsia phenotype (hypertension, proteinuria). CD151 overexpression/knockdown in trophoblast cells; ERK/Nrf2 inhibitor studies; antioxidant gene qPCR/Western blot; in vivo mouse model with placental CD151 downregulation Free Radical Biology and Medicine Medium 33450381
2024 CD151 promotes migrasome formation in hepatocellular carcinoma cells; decreased CD151 expression reduces migrasome generation, impairs cellular invasion, and diminishes in vivo metastatic potential; VEGF-enriched migrasomes derived from CD151-high cells promote angiogenesis and HCC progression. CD151 overexpression/knockdown; migrasome imaging; in vitro invasion assays; VEGF level analysis; in vivo metastasis; tissue chip analysis Journal of Experimental & Clinical Cancer Research Medium 38840183

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology. Molecular biology of the cell 199 11907260
2004 CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood 188 15265795
1999 Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. The Biochemical journal 185 10229664
2000 The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes. The Journal of cell biology 183 10811835
2006 Kidney failure in mice lacking the tetraspanin CD151. The Journal of cell biology 181 17015618
1997 Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society 175 9111230
2011 CD151 amplifies signaling by integrin α6β1 to PI3K and induces the epithelial-mesenchymal transition in HCC cells. Gastroenterology 158 21320503
2018 LncRNA SNHG3 induces EMT and sorafenib resistance by modulating the miR-128/CD151 pathway in hepatocellular carcinoma. Journal of cellular physiology 157 30132868
2008 CD151 accelerates breast cancer by regulating alpha 6 integrin function, signaling, and molecular organization. Cancer research 147 18451146
2015 The tetraspanins CD151 and Tspan8 are essential exosome components for the crosstalk between cancer initiating cells and their surrounding. Oncotarget 146 25544774
2004 Characterization of mice lacking the tetraspanin superfamily member CD151. Molecular and cellular biology 143 15199151
2006 Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro. Blood 137 17023588
2002 An extracellular site on tetraspanin CD151 determines alpha 3 and alpha 6 integrin-dependent cellular morphology. The Journal of cell biology 133 12356873
2002 Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo. Journal of cell science 129 11884516
2005 Potentiation of the ligand-binding activity of integrin alpha3beta1 via association with tetraspanin CD151. Proceedings of the National Academy of Sciences of the United States of America 125 15677332
2007 Tetraspanin CD151 promotes cell migration by regulating integrin trafficking. The Journal of biological chemistry 113 17716972
2010 Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists. Cancer research 111 20197472
2006 A critical role for tetraspanin CD151 in alpha3beta1 and alpha6beta4 integrin-dependent tumor cell functions on laminin-5. Molecular biology of the cell 109 16571677
2005 Colocalization of the tetraspanins, CO-029 and CD151, with integrins in human pancreatic adenocarcinoma: impact on cell motility. Clinical cancer research : an official journal of the American Association for Cancer Research 109 15837731
2002 Function of the tetraspanin CD151-alpha6beta1 integrin complex during cellular morphogenesis. Molecular biology of the cell 108 11809818
2001 Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis. The Journal of biological chemistry 94 11479292
2006 Homophilic interactions of Tetraspanin CD151 up-regulate motility and matrix metalloproteinase-9 expression of human melanoma cells through adhesion-dependent c-Jun activation signaling pathways. The Journal of biological chemistry 90 16798740
1995 Molecular cloning of cDNA encoding a novel platelet-endothelial cell tetra-span antigen, PETA-3. Blood 90 7632941
2008 Deletion of CD151 results in a strain-dependent glomerular disease due to severe alterations of the glomerular basement membrane. The American journal of pathology 87 18787104
1999 Transmembrane 4 superfamily protein CD151 (PETA-3) associates with beta 1 and alpha IIb beta 3 integrins in haemopoietic cell lines and modulates cell-cell adhesion. The Biochemical journal 87 9931299
2013 CD151 in cancer progression and metastasis: a complex scenario. Laboratory investigation; a journal of technical methods and pathology 85 24247563
2004 The tetraspanin superfamily member CD151 regulates outside-in integrin alphaIIbbeta3 signaling and platelet function. Blood 84 15226180
2007 Roles of rapH and rapG in positive regulation of rapamycin biosynthesis in Streptomyces hygroscopicus. Journal of bacteriology 82 17468238
2013 MicroRNA-124 suppresses breast cancer cell growth and motility by targeting CD151. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 79 23816858
2008 DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151. Molecular biology of the cell 79 18508921
2007 Role of CD151, A tetraspanin, in porcine reproductive and respiratory syndrome virus infection. Virology journal 79 17572908
2008 MT1-MMP collagenolytic activity is regulated through association with tetraspanin CD151 in primary endothelial cells. Blood 77 18663148
2009 CD151 regulates tumorigenesis by modulating the communication between tumor cells and endothelium. Molecular cancer research : MCR 72 19531562
2006 Wound healing is defective in mice lacking tetraspanin CD151. The Journal of investigative dermatology 72 16410781
2012 Integrin-associated CD151 drives ErbB2-evoked mammary tumor onset and metastasis. Neoplasia (New York, N.Y.) 67 22952421
2011 Blood pressure influences end-stage renal disease of Cd151 knockout mice. The Journal of clinical investigation 67 22201679
2006 Bacillus subtilis RghR (YvaN) represses rapG and rapH, which encode inhibitors of expression of the srfA operon. Molecular microbiology 66 16553878
2024 CD151-enriched migrasomes mediate hepatocellular carcinoma invasion by conditioning cancer cells and promoting angiogenesis. Journal of experimental & clinical cancer research : CR 63 38840183
2005 Pericellular activation of proMMP-7 (promatrilysin-1) through interaction with CD151. Laboratory investigation; a journal of technical methods and pathology 62 16200075
2012 Clinical significance of CD151 overexpression in subtypes of invasive breast cancer. British journal of cancer 60 22294188
2012 Tetraspanin CD151 plays a key role in skin squamous cell carcinoma. Oncogene 59 22824799
2021 Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer. Molecular & cellular proteomics : MCP 58 34265469
2013 Tspan8 and CD151 promote metastasis by distinct mechanisms. European journal of cancer (Oxford, England : 1990) 57 23683890
2008 Regulation of CD151 by hypoxia controls cell adhesion and metastasis in colorectal cancer. Clinical cancer research : an official journal of the American Association for Cancer Research 56 19073968
2014 Tetraspanins CD9 and CD151 at the immune synapse support T-cell integrin signaling. European journal of immunology 53 24723389
2008 Tetraspanin CD151 regulates glycosylation of (alpha)3(beta)1 integrin. The Journal of biological chemistry 52 18852263
2013 Integrin-free tetraspanin CD151 can inhibit tumor cell motility upon clustering and is a clinical indicator of prostate cancer progression. Cancer research 48 24220242
2012 Tetraspanin CD151 stimulates adhesion-dependent activation of Ras, Rac, and Cdc42 by facilitating molecular association between β1 integrins and small GTPases. The Journal of biological chemistry 48 22843693
2011 Tetraspanin CD151 maintains vascular stability by balancing the forces of cell adhesion and cytoskeletal tension. Blood 47 21832275
2010 The tetraspanin CD151 is required for Met-dependent signaling and tumor cell growth. The Journal of biological chemistry 47 20937830
2010 Structure-function analysis of tetraspanin CD151 reveals distinct requirements for tumor cell behaviors mediated by α3β1 versus α6β4 integrin. The Journal of biological chemistry 45 21193415
2007 CD151 dynamics in carcinoma-stroma interaction: integrin expression, adhesion strength and proteolytic activity. Laboratory investigation; a journal of technical methods and pathology 45 17632541
2014 CD151-α3β1 integrin complexes suppress ovarian tumor growth by repressing slug-mediated EMT and canonical Wnt signaling. Oncotarget 44 25356755
2011 Diminished metastasis in tetraspanin CD151-knockout mice. Blood 44 21536858
2017 Recessive mutation in tetraspanin CD151 causes Kindler syndrome-like epidermolysis bullosa with multi-systemic manifestations including nephropathy. Matrix biology : journal of the International Society for Matrix Biology 43 29138120
2021 CD151 drives cancer progression depending on integrin α3β1 through EGFR signaling in non-small cell lung cancer. Journal of experimental & clinical cancer research : CR 42 34108040
2020 The activation of GPER inhibits cells proliferation, invasion and EMT of triple-negative breast cancer via CD151/miR-199a-3p bio-axis. American journal of translational research 40 32051735
2013 The CD9/CD81 tetraspanin complex and tetraspanin CD151 regulate α3β1 integrin-dependent tumor cell behaviors by overlapping but distinct mechanisms. PloS one 40 23613949
2010 Overexpression of CD151 as an adverse marker for intrahepatic cholangiocarcinoma patients. Cancer 40 20715158
2014 MiR-22 suppresses the proliferation and invasion of gastric cancer cells by inhibiting CD151. Biochemical and biophysical research communications 39 24495805
2014 miR-152 suppresses gastric cancer cell proliferation and motility by targeting CD151. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 39 25119599
2012 Genetic ablation of the tetraspanin CD151 reduces spontaneous metastatic spread of prostate cancer in the TRAMP model. Molecular cancer research : MCR 39 23131993
2003 The tetraspanin CD151 functions as a negative regulator in the adhesion-dependent activation of Ras. The Journal of biological chemistry 39 12782641
2014 MiR-506 inhibits PRRSV replication in MARC-145 cells via CD151. Molecular and cellular biochemistry 38 24878990
2008 The tetraspanin CD151 regulates cell morphology and intracellular signaling on laminin-511. The FEBS journal 38 18492066
2005 Role of tetraspanins CD9 and CD151 in primary melanocyte motility. The Journal of investigative dermatology 38 16297202
2019 miR-199a-3p promotes cardiomyocyte proliferation by inhibiting Cd151 expression. Biochemical and biophysical research communications 37 31186138
2019 Marine natural compound cyclo(L-leucyl-L-prolyl) peptide inhibits migration of triple negative breast cancer cells by disrupting interaction of CD151 and EGFR signaling. Chemico-biological interactions 37 31669320
2014 The tetraspanin CD151 in papillomavirus infection. Viruses 36 24553111
2011 Profiling of the tetraspanin CD151 web and conspiracy of CD151/integrin β1 complex in the progression of hepatocellular carcinoma. PloS one 36 21961047
2015 CD151-A Striking Marker for Cancer Therapy. Biomarkers in cancer 35 25861224
2013 Integrin α3β1-CD151 complex regulates dimerization of ErbB2 via RhoA. Oncogene 35 23792450
2006 Dissociation of the complex between CD151 and laminin-binding integrins permits migration of epithelial cells. Experimental cell research 35 16490193
2018 Tspan8 and Tspan8/CD151 knockout mice unravel the contribution of tumor and host exosomes to tumor progression. Journal of experimental & clinical cancer research : CR 34 30541597
2001 Differential tissue expression of epitopes of the tetraspanin CD151 recognised by monoclonal antibodies. Tissue antigens 33 11703821
2018 MiR-124 aggravates failing hearts by suppressing CD151-facilitated angiogenesis in heart. Oncotarget 32 29581851
2017 Interrogation of Functional Cell-Surface Markers Identifies CD151 Dependency in High-Grade Serous Ovarian Cancer. Cell reports 32 28273451
2006 Tetraspanin CD151 is expressed in osteoarthritic cartilage and is involved in pericellular activation of pro-matrix metalloproteinase 7 in osteoarthritic chondrocytes. Arthritis and rheumatism 32 17009258
2009 CD151 gene delivery after myocardial infarction promotes functional neovascularization and activates FAK signaling. Molecular medicine (Cambridge, Mass.) 30 19603100
2019 Tetraspanin CD151 and integrin α3β1 contribute to the stabilization of integrin α6β4-containing cell-matrix adhesions. Journal of cell science 27 31488507
2016 The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding site of integrin αvβ3. The Biochemical journal 27 27993971
2016 Anti-invasion and anti-migration effects of miR-199a-3p in hepatocellular carcinoma are due in part to targeting CD151. International journal of oncology 26 27599545
2021 Activation of GPER by E2 promotes proliferation, invasion and migration of breast cancer cells by regulating the miR-124/CD151 pathway. Oncology letters 24 33868470
2020 The CD151-midkine pathway regulates the immune microenvironment in inflammatory breast cancer. The Journal of pathology 24 32129471
2016 CD151 mediates netrin-1-induced angiogenesis through the Src-FAK-Paxillin pathway. Journal of cellular and molecular medicine 24 27558487
2015 CD151 knockdown inhibits osteosarcoma metastasis through the GSK-3β/β-catenin/MMP9 pathway. Oncology reports 24 26707073
2012 CD151 promotes cancer cell metastasis via integrins α3β1 and α6β1 in vitro. Molecular medicine reports 23 23007325
2013 CD151 is associated with prostate cancer cell invasion and lymphangiogenesis in vivo. Oncology reports 22 24174171
2011 An atypical Phr peptide regulates the developmental switch protein RapH. Journal of bacteriology 21 21908671
2019 Integrin-independent support of cancer drug resistance by tetraspanin CD151. Cellular and molecular life sciences : CMLS 20 30778617
2016 Regulation of Glioblastoma Tumor-Propagating Cells by the Integrin Partner Tetraspanin CD151. Neoplasia (New York, N.Y.) 20 26992919
2011 Role of tetraspanin CD151-α3/α6 integrin complex: Implication in angiogenesis CD151-integrin complex in angiogenesis. The international journal of biochemistry & cell biology 20 21237282
2023 Exploring the role of CD151 in the tumor immune microenvironment: Therapeutic and clinical perspectives. Biochimica et biophysica acta. Reviews on cancer 19 37094754
2021 Downregulation of CD151 induces oxidative stress and apoptosis in trophoblast cells via inhibiting ERK/Nrf2 signaling pathway in preeclampsia. Free radical biology & medicine 19 33450381
2020 CD151 in Respiratory Diseases. Frontiers in cell and developmental biology 19 32117989
2020 Expression and distribution of CD151 as a partner of alpha6 integrin in male germ cells. Scientific reports 19 32152440
2016 CD151 Regulates T-Cell Migration in Health and Inflammatory Bowel Disease. Inflammatory bowel diseases 19 26529559
2016 CD151, a laminin receptor showing increased expression in asthmatic patients, contributes to airway hyperresponsiveness through calcium signaling. The Journal of allergy and clinical immunology 19 27233153
2012 Application of RNA-Seq transcriptome analysis: CD151 is an Invasion/Migration target in all stages of epithelial ovarian cancer. Journal of ovarian research 19 22272937
2010 Activation of the ERK signaling pathway is involved in CD151-induced angiogenic effects on the formation of CD151-integrin complexes. Acta pharmacologica Sinica 19 20581856