Affinage

CTSV

Cathepsin L2 · UniProt O60911

Round 2 corrected
Length
334 aa
Mass
37.3 kDa
Annotated
2026-04-28
37 papers in source corpus 18 papers cited in narrative 18 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

CTSV (cathepsin L2) is a lysosomal papain-family cysteine protease that undergoes autocatalytic activation at acidic pH, possesses an S2 subsite specificity intermediate between cathepsins L and S, and requires N-glycosylation at Asn221 and Asn292 for proper lysosomal trafficking and enzymatic activity (PMID:10029531, PMID:22967898, PMID:11027133). CTSV functions as the dominant protease converting invariant chain (Ii) to CLIP for MHC class II peptide loading in human cortical thymic epithelial cells, the most potent elastase in human macrophages (regulated by glycosaminoglycan complex formation), and a corneodesmosin-cleaving enzyme in epidermal desquamation that functionally substitutes for murine cathepsin L in transgenic rescue of cathepsin L–knockout skin and hair phenotypes (PMID:12925692, PMID:15192101, PMID:12648222, PMID:15679121). Its activity is tightly controlled by endogenous inhibitors including cystatin F (Ki ~0.2 nM) and cystatin M/E (Ki = 0.47 nM), which bind through a site distinct from the legumain-inhibitory interface (PMID:15752368, PMID:16565075). CTSV is a direct transcriptional target of E2F1 that drives pro-apoptotic lysosomal membrane permeabilization, and its expression is upregulated through EGFR-MEK-ERK and PKCα/δ-ERK-Sp1 cascades in cancer cells where it promotes migration, invasion, and NF-κB-dependent proliferation (PMID:23542171, PMID:32331211, PMID:40674912, PMID:35443863).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1998 High

    Cloning of CTSV from human brain and corneal cDNA libraries established it as a novel cysteine protease closely related to cathepsin L, resolving whether humans possess a second cathepsin L-like gene with tissue-restricted expression.

    Evidence Recombinant expression (E. coli and baculovirus), proteolytic activity on synthetic and protein substrates, class-specific inhibitor profiling (E-64, leupeptin), Northern blot tissue distribution

    PMID:9563472 PMID:9727401

    Open questions at the time
    • Endogenous substrates unknown
    • No structural information
    • Intracellular trafficking mechanism undefined
  2. 1999 High

    Biochemical characterization revealed that CTSV undergoes autocatalytic activation at acidic pH and is more stable at neutral pH than cathepsin L, explaining how it can retain activity in extracellular or mildly acidic compartments and clarifying its functional distinction from cathepsin L.

    Evidence Kinetic and pH-stability assays with Pichia-expressed recombinant protein, chromosomal mapping to 9q22.2

    PMID:10029531

    Open questions at the time
    • No crystal structure yet
    • In vivo substrates not identified
    • Mechanism of greater pH stability not structurally explained
  3. 2000 High

    Determination of the 1.6 Å crystal structure with a vinyl sulfone inhibitor resolved the molecular basis of CTSV's distinct substrate specificity by identifying S2 and S3 subsite differences from related cathepsins, enabling rational inhibitor design.

    Evidence X-ray crystallography with active-site inhibitor co-crystal

    PMID:11027133

    Open questions at the time
    • No structure of CTSV with a physiological substrate or pro-domain
    • Dynamics of autocatalytic processing not captured
  4. 2003 High

    Three concurrent studies established CTSV's key physiological roles: it is the dominant Ii→CLIP-processing protease in human cortical thymic epithelial cells (the human counterpart of mouse cathepsin L in MHC class II antigen loading), it cleaves corneodesmosin during epidermal desquamation, and it is differentially resistant to the serpin hurpin compared with cathepsin L.

    Evidence Active-site labeling in thymic lysosomes plus in vitro Ii degradation reconstitution; corneodesmosin hydrolysis assay; inhibition kinetics with site-directed mutagenesis of hurpin reactive center loop

    PMID:12648222 PMID:12809493 PMID:12925692

    Open questions at the time
    • No genetic loss-of-function in human thymus
    • Relative contribution to desquamation versus other proteases unresolved
    • In vivo regulation in thymus not addressed
  5. 2004 High

    CTSV was identified as the most potent human elastase described at that time in macrophages, with its activity specifically inhibited by glycosaminoglycans, and transgenic expression of CTSV rescued the skin and hair phenotype of cathepsin L–knockout mice, proving functional equivalence in the epidermis.

    Evidence In vitro elastin degradation and GAG-cathepsin complex assays in macrophages; transgenic K14-CTSV rescue in cathepsin L KO mice with histological analysis

    PMID:15192101 PMID:15679121

    Open questions at the time
    • Structural basis of GAG-mediated inhibition undefined
    • In vivo elastolytic contribution in atherosclerosis not causally tested
    • CTSV-specific KO mouse not available
  6. 2005 High

    Quantitative kinetic analysis revealed that cystatin F is a sub-nanomolar inhibitor of CTSV (Ki ~0.2 nM), establishing CTSV as its preferred target and suggesting tight endogenous regulation in immune cells.

    Evidence In vitro Ki determination with recombinant cystatin F and CTSV

    PMID:15752368

    Open questions at the time
    • Physiological consequence of cystatin F-CTSV interaction in immune cells not shown
    • In vivo relevance not tested
  7. 2006 High

    Cystatin M/E was shown to inhibit CTSV at sub-nanomolar affinity through a binding site distinct from its legumain-inhibitory interface, and co-localization in the stratum granulosum implied functional regulation during epidermal differentiation.

    Evidence Inhibition kinetics with site-directed mutagenesis (W135A, N64 variants), immunohistochemistry in human skin

    PMID:16565075

    Open questions at the time
    • Functional consequence of cystatin M/E loss on CTSV activity in skin not tested in vivo
    • Relative importance versus other epidermal cystatin–cathepsin pairs unclear
  8. 2012 High

    Identification of Asn221 and Asn292 as N-glycosylation sites required for lysosomal trafficking and enzymatic activity resolved how CTSV is sorted to lysosomes and why glycosylation-deficient mutants are non-functional.

    Evidence Mass spectrometry glycopeptide mapping, site-directed mutagenesis, trafficking and activity assays in HT1080 cells

    PMID:22967898

    Open questions at the time
    • Mannose-6-phosphate receptor dependence not formally tested
    • Contribution of each glycosylation site individually to trafficking versus stability not fully separated
  9. 2013 High

    Discovery that CTSV is a direct E2F1 transcriptional target required for E2F1-induced lysosomal membrane permeabilization and apoptosis placed CTSV in an oncogene-responsive cell death pathway and explained how lysosomal proteases connect to the intrinsic apoptosis program.

    Evidence ChIP for E2F1 at CTSL2 promoter, RNAi knockdown and overexpression with LMP and mitochondrial depolarization readouts, HDAC inhibitor sensitization

    PMID:23542171

    Open questions at the time
    • Identity of CTSV substrates that trigger LMP or mitochondrial depolarization unknown
    • Whether this pathway operates in non-cancer cells not tested
  10. 2020 Medium

    Placing CTSV downstream of EGFR-MEK-ERK in renal cell carcinoma established that growth-factor signaling transcriptionally controls CTSV to promote cell migration and invasion, extending its pro-metastatic role beyond thyroid and colon cancers.

    Evidence EGF stimulation, pharmacological inhibition (Praeruptorin B), siRNA knockdown, migration/invasion assays in RCC cells

    PMID:32331211

    Open questions at the time
    • Promoter-level mechanism of ERK-driven transcription not mapped
    • Independent replication in additional RCC models needed
    • In vivo metastasis assay not performed
  11. 2022 Medium

    Demonstration that CTSV activates NF-κB-dependent proliferation in bladder cancer (rescued by NF-κB inhibitor) identified a second downstream signaling pathway through which CTSV promotes tumor growth, distinct from the EGFR-ERK axis.

    Evidence Overexpression and knockdown with NF-κB dual-luciferase reporter, xenograft tumor growth in nude mice, NF-κB inhibitor rescue

    PMID:35443863

    Open questions at the time
    • Mechanism by which a lysosomal protease activates NF-κB not defined
    • Direct versus indirect NF-κB activation not distinguished
    • Single cancer type tested
  12. 2025 Medium

    Identification of the PKCα/δ-ERK-Sp1 axis as a transcriptional regulator of CTSV in colorectal cancer provided a second upstream kinase cascade converging on CTSV expression, reinforcing its role as a convergent effector of multiple MAPK-dependent pro-invasive programs.

    Evidence Phospho-Western blots, siRNA epistasis (ERK, CTSV), TPA rescue, proteomic protease array, migration/invasion assays

    PMID:40674912

    Open questions at the time
    • Sp1 binding to CTSV promoter not confirmed by ChIP
    • Overlap or redundancy with EGFR-ERK pathway not addressed
    • In vivo metastasis model lacking

Open questions

Synthesis pass · forward-looking unresolved questions
  • Major unresolved questions include the full repertoire of endogenous CTSV substrates in thymus and skin, the molecular mechanism by which CTSV triggers NF-κB activation and lysosomal membrane permeabilization, the phenotype of a CTSV-specific knockout in human or humanized models, and structural elucidation of CTSV–glycosaminoglycan inhibitory complexes.
  • No CTSV-specific genetic knockout phenotype in a human-relevant model
  • No unbiased substrate profiling (e.g. TAILS/ATOMS) reported
  • Structural basis of GAG-mediated inhibition unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 6 GO:0016787 hydrolase activity 5
Localization
GO:0005764 lysosome 3 GO:0005576 extracellular region 1 GO:0005634 nucleus 1
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 2 R-HSA-392499 Metabolism of proteins 1 R-HSA-5357801 Programmed Cell Death 1
Partners
CD74CST6CST7E2F1

Evidence

Reading pass · 18 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 CTSV (cathepsin L2/cathepsin V) was cloned from a human brain cDNA library and identified as a novel cysteine proteinase with 78% amino acid identity to cathepsin L. Recombinant protein expressed in E. coli demonstrated proteolytic activity on the synthetic substrate Z-Phe-Arg-AMC, which was abolished by the cysteine proteinase inhibitor E-64 (trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane), confirming active-site cysteine-dependent catalysis. Expression was found predominantly in thymus and testis, with upregulation in colorectal and breast carcinomas. Recombinant protein expression, enzyme activity assay with synthetic substrate, inhibitor studies (E-64), Northern blot Cancer research High 9563472
1998 CTSV was independently identified as the major cysteine protease in human corneal epithelium. Recombinant CTSV expressed in a baculovirus system cleaved BSA and was inhibited by E-64 and leupeptin (cysteine proteinase inhibitors) but not by pepstatin A, PMSF, or EDTA, establishing it as a cysteine protease rather than aspartyl or serine protease. Baculovirus recombinant expression, enzyme activity assay on BSA substrate, class-specific inhibitor profiling, RT-PCR tissue distribution Investigative ophthalmology & visual science High 9727401
1999 Recombinant CTSV expressed in Pichia pastoris undergoes autocatalytic activation at acidic pH. Its S2 subsite specificity is intermediate between cathepsins L and S, accepting both aromatic and non-aromatic hydrophobic residues. CTSV is significantly more stable at mildly acidic and neutral pH than cathepsin L but less stable than cathepsin S. CTSV showed only weak collagenolytic activity (unlike cathepsin L). Chromosomal mapping placed CTSV at 9q22.2, adjacent to the cathepsin L locus, suggesting evolution from a common ancestor by gene duplication. A homology model revealed a neutral-to-weakly-positive electrostatic potential near the active site cleft, contrasting with cathepsin L's negative surface. Recombinant protein expression (Pichia pastoris), kinetic assays, pH stability assays, collagenolysis assay, class-specific inhibitor profiling, homology modeling, chromosomal mapping Biochemistry High 10029531
2000 The 1.6 Å resolution crystal structure of human CTSV was determined with an irreversible vinyl sulfone inhibitor bound at the active site. The fold is similar to the papain superfamily of cysteine proteases. Comparison of the active site with related proteases identified differences in the S2 and S3 subsites that distinguish CTSV from other family members and can be exploited for selective inhibitor design. X-ray crystallography (1.6 Å resolution), active-site inhibitor co-crystal Biochemistry High 11027133
2003 CTSV is the dominant cysteine protease in cortical human thymic epithelial cells (TECs), while cathepsins L and S are restricted to dendritic and macrophage-like cells. Active CTSV in thymic lysosomal preparations was demonstrated by active-site labeling. Recombinant CTSV efficiently converts the invariant chain (Ii) into CLIP (class II-associated invariant chain peptide), identifying CTSV as the protease controlling MHC class II peptide loading in human thymus (analogous to cathepsin L in mouse). CTSV expression is significantly elevated in thymi of myasthenia gravis patients compared to healthy controls. Active-site labeling (activity-based probe), cell fractionation, recombinant protein in vitro Ii degradation assay, immunohistochemistry, Western blot The Journal of clinical investigation High 12925692
2003 CTSV (cathepsin L2) was identified as the stratum corneum thiol protease (SCTP) previously described in human epidermis. CTSV can hydrolyze corneodesmosin, a marker of corneocyte cohesion, implicating it in the desquamation process. Expression analysis showed CTSV is expressed as a pro-enzyme in lower epidermal layers and is partially activated in upper layers during keratinocyte differentiation. Protein purification/gel filtration, specific antibody immunoidentification, caseinolytic activity assay, corneodesmosin hydrolysis assay, RT-PCR The Journal of investigative dermatology Medium 12648222
2003 Hurpin (serpinB13/PI13), an intracellular serpin expressed in keratinocytes, potently and selectively inhibits cathepsin L (k_assoc = 4.6×10⁵ M⁻¹s⁻¹, SI = 1.7) but only inefficiently inhibits CTSV. Site-directed mutagenesis of the reactive center loop (P1-P1' bond Thr356-Ser357) confirmed the conventional serpin inhibitory mechanism. This establishes CTSV as resistant to hurpin-mediated serpin inhibition, in contrast to cathepsin L. In vitro inhibition kinetics, site-directed mutagenesis of serpin reactive center loop, recombinant protein assays Biochemistry High 12809493
2004 Macrophages express CTSV as a potent elastolytic cysteine protease — the most potent elastase activity yet described among human proteases. Approximately 60% of total macrophage elastolytic activity is attributable to cysteine proteases (cathepsins V, K, and S contributing equally). Two-thirds of this activity is extracellular and one-third intracellular, with the intracellular portion credited specifically to CTSV. Glycosaminoglycans (GAGs) such as chondroitin sulfate specifically inhibit the elastolytic activities of CTSV and cathepsin K via formation of specific cathepsin-GAG complexes, whereas cathepsin S is not inhibited. CTSV was detected in atherosclerotic plaque specimens. In vitro elastin degradation assays, macrophage cysteine protease activity profiling, GAG-cathepsin complex formation assay, activity-based inhibitors, plaque immunohistochemistry The Journal of biological chemistry High 15192101
2004 Transgenic keratinocyte-specific expression of CTSV (under the keratin 14 promoter) in cathepsin L knockout mice rescues both the skin phenotype (epidermal hyperplasia/hyperproliferation) and the hair loss phenotype. This genetic complementation demonstrates that CTSV can functionally substitute for cathepsin L in mouse epidermis and hair follicles, establishing a conserved keratinocyte-specific proteolytic function. Transgenic mouse generation, genetic epistasis (transgene rescue of KO phenotype), histological analysis of epidermis, hair follicle morphology European journal of cell biology High 15679121
2005 Cystatin F, expressed in immune cells, tightly inhibits CTSV with a Ki of 0.17–0.35 nM (among the highest affinities measured), compared to ~30 nM for cathepsins S and H, and no inhibition of cathepsins C and X. This establishes CTSV as a preferred high-affinity target of cystatin F among lysosomal cysteine proteases. In vitro inhibition kinetics with recombinant proteins, Ki measurement The FEBS journal High 15752368
2006 Cystatin M/E is a high-affinity inhibitor of CTSV (Ki = 0.47 nM) and cathepsin L (Ki = 1.78 nM). Site-directed mutagenesis of cystatin M/E identified that residue W135 is required for inhibition of CTSV and cathepsin L (W135A abolishes this activity) but not for legumain inhibition, while N64 is required for legumain inhibition but not for CTSV/cathepsin L inhibition. This demonstrates that papain-like cysteine proteases (including CTSV) and legumain are inhibited by two distinct, non-overlapping sites on cystatin M/E. Immunohistochemistry showed co-localization of cystatin M/E with CTSV in the stratum granulosum of human skin. In vitro inhibition kinetics, site-directed mutagenesis, immunohistochemistry The Journal of biological chemistry High 16565075
2010 CTSV immunoreactivity localizes to the nucleus in peri-nucleolar patterns in the anaplastic thyroid carcinoma cell line HTh74, as demonstrated by immunofluorescence and biochemical subcellular fractionation. Co-localization studies and in vitro degradation assays suggest nuclear CTSV variants may be involved in modification of DNA-associated proteins in thyroid malignancies. This is distinct from cathepsin L, which does not show nuclear localization in this context. Immunofluorescence, subcellular fractionation, in vitro degradation assay, co-localization microscopy Biological chemistry Medium 20536394
2012 CTSV is N-glycosylated at two specific asparagine residues, Asn221 and Asn292, as confirmed by mass spectrometry and site-directed mutagenesis. N-glycosylation is required for proper lysosomal trafficking, secretion, and enzymatic activity of CTSV in HT1080 cells. Mutation of either glycosylation site disrupts these functions. Mass spectrometry (glycopeptide identification), site-directed mutagenesis of N-glycosylation sites, lysosomal trafficking assay, secretion assay, enzymatic activity assay FEBS letters High 22967898
2013 CTSV (CTSL2) is a direct transcriptional target of E2F1. E2F1 directly binds to the CTSL2 promoter, and CTSV is regulated by both exogenous and endogenous E2F1. RNAi-mediated knockdown of CTSV abrogates E2F1-induced apoptosis, reduces lysosomal membrane permeabilization (LMP), and prevents mitochondrial membrane depolarization. CTSV depletion also inhibits apoptosis induced by DNA-damage-activated endogenous E2F1 and by histone deacetylase inhibitors (HDACi), while overexpression of CTSV sensitizes cancer cells to HDACi. This places CTSV downstream of E2F1 in a pro-apoptotic pathway involving lysosomal membrane permeabilization. Chromatin immunoprecipitation (ChIP), RNAi knockdown, luciferase reporter assay, apoptosis assays, LMP measurement, mitochondrial membrane potential assay, overexpression Oncogene High 23542171
2020 CTSV expression in renal cell carcinoma (RCC) is regulated by the EGFR-MEK-ERK signaling pathway. Praeruptorin B reduces CTSV mRNA and protein levels in RCC cells by inhibiting phosphorylation of EGFR, MEK, and ERK. EGF treatment upregulates CTSV expression via EGFR-MEK-ERK, and this is blocked by Praeruptorin B. Downregulation of CTSV correlates with reduced RCC cell migration and invasion, placing CTSV downstream of EGFR-MEK-ERK in a pro-metastatic signaling cascade. siRNA knockdown, Western blot, migration/invasion assays, EGF stimulation, pharmacological inhibition, RT-PCR International journal of molecular sciences Medium 32331211
2021 CTSV can cleave multiple sites on the SARS-CoV-2 spike protein, including within the S1/S2 region critical for viral activation and membrane fusion. Computational prediction of cleavage sites (PACMANS) was verified by molecular docking and immunoblotting, identifying CTSV as one of several cathepsins capable of processing the spike protein and potentially facilitating viral entry. Computational cleavage site prediction (PACMANS), molecular docking, immunoblotting Protein science Low 33786919
2022 CTSV promotes bladder cancer cell proliferation through activation of the NF-κB inflammatory signaling pathway. Overexpression of CTSV increases NF-κB transcriptional activity as measured by dual-luciferase reporter assay, while CTSV deletion inhibits proliferation and viability in vitro and suppresses tumor growth in vivo. The proliferative effect of CTSV overexpression is restored to baseline by an NF-κB inhibitor. siRNA knockdown, overexpression, CCK8 and colony formation assays, dual-luciferase reporter (NF-κB), in vivo nude mouse xenograft, NF-κB inhibitor rescue Bioengineered Medium 35443863
2025 In colorectal cancer cells, CTSV expression is controlled by the PKCα/PKCδ-ERK-Sp1 signaling axis. Trichodermin inhibits phosphorylation of PKCα, PKCδ, and ERK, which in turn reduces Sp1 transcriptional activity and CTSV expression. siRNA knockdown of either ERK or CTSV enhances the anti-migration and anti-invasion effects of trichodermin. PKC activator TPA rescues CTSV expression and cell migration/invasion, which is counteracted by trichodermin, placing CTSV downstream of PKC-ERK-Sp1 as a mediator of CRC metastatic behavior. siRNA knockdown, proteomic protease array, Western blot (phospho-PKC, phospho-ERK, Sp1), migration/invasion assays, pharmacological activation (TPA) and inhibition Phytomedicine Medium 40674912

Source papers

Stage 0 corpus · 37 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2015 A Dynamic Protein Interaction Landscape of the Human Centrosome-Cilium Interface. Cell 433 26638075
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
2016 An organelle-specific protein landscape identifies novel diseases and molecular mechanisms. Nature communications 211 27173435
1999 Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry 184 10029531
2004 Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages. The Journal of biological chemistry 158 15192101
2007 An intracellular serpin regulates necrosis by inhibiting the induction and sequelae of lysosomal injury. Cell 133 17889653
2013 Proteomic analysis of podocyte exosome-enriched fraction from normal human urine. Journal of proteomics 126 23376485
1998 Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer research 122 9563472
2003 Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis. The Journal of clinical investigation 98 12925692
2006 Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification. The Journal of biological chemistry 91 16565075
2020 Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases. Molecular cell 88 32707033
2004 DNA sequence and analysis of human chromosome 9. Nature 86 15164053
2017 Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones. The Journal of cell biology 78 28515276
2005 Inhibitory properties of cystatin F and its localization in U937 promonocyte cells. The FEBS journal 68 15752368
1998 Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Investigative ophthalmology & visual science 66 9727401
2003 Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis. Biochemistry 65 12809493
2021 Multiple sites on SARS-CoV-2 spike protein are susceptible to proteolysis by cathepsins B, K, L, S, and V. Protein science : a publication of the Protein Society 62 33786919
2000 Crystal structure of human cathepsin V. Biochemistry 61 11027133
2003 Analysis of proteins with caseinolytic activity in a human stratum corneum extract revealed a yet unidentified cysteine protease and identified the so-called "stratum corneum thiol protease" as cathepsin l2. The Journal of investigative dermatology 52 12648222
2010 Nuclear cysteine cathepsin variants in thyroid carcinoma cells. Biological chemistry 49 20536394
2004 The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles. European journal of cell biology 41 15679121
2019 MaXLinker: Proteome-wide Cross-link Identifications with High Specificity and Sensitivity. Molecular & cellular proteomics : MCP 39 31839598
2012 Determination of cathepsin V activity and intracellular trafficking by N-glycosylation. FEBS letters 37 22967898
2007 Polymorphisms in the cathepsin L2 (CTSL2) gene show association with type 1 diabetes and early-onset myasthenia gravis. Human immunology 28 17869649
2022 CTSV (cathepsin V) promotes bladder cancer progression by increasing NF-κB activity. Bioengineered 17 35443863
2020 Praeruptorin B Mitigates the Metastatic Ability of Human Renal Carcinoma Cells through Targeting CTSC and CTSV Expression. International journal of molecular sciences 17 32331211
2013 CTSL2 is a pro-apoptotic target of E2F1 and a modulator of histone deacetylase inhibitor and DNA damage-induced apoptosis. Oncogene 7 23542171
2007 Evaluation of the CTSL2 gene as a candidate gene for alopecia X in Pomeranians and Keeshonden. Animal biotechnology 7 17934903
2025 CTSL-2 upon specifically recognizing Vibrio splendidus directly cleaves complement C3 to promote the bacterial phagocytosis and degradation in oyster. Cell communication and signaling : CCS 1 40275325
2025 Trichodermin, an endophytic fungal sesquiterpene, suppresses colorectal cancer cell migration and invasion by targeting the PKC-ERK-Sp1-CTSV axis. Phytomedicine : international journal of phytotherapy and phytopharmacology 1 40674912