| 1996 |
CRISP3 (SGP28) is localized in specific granules of human neutrophils, as determined by subcellular fractionation of human neutrophils and partial primary structure determination of the purified 28 kDa glycoprotein. |
Protein purification from neutrophil exocytosed material, cDNA cloning, subcellular fractionation |
FEBS letters |
High |
8601434
|
| 2002 |
CRISP3 is a matrix protein localized in a subset of peroxidase-negative granules with overlapping characteristics of specific and gelatinase granules in neutrophils, and is also present in granules of eosinophils; it exists as both glycosylated and unglycosylated forms with identical subcellular distribution. |
Three-layer Percoll density gradient fractionation, secretagogue release studies, double-labeling immunogold electron microscopy |
Journal of leukocyte biology |
High |
12223513
|
| 2005 |
Beta-microseminoprotein (MSP/PSP94) and CRISP3 form stable, non-covalent high-affinity complexes in human seminal plasma, with CRISP3 binding MSP through its amino-terminal SCP-domain. |
Immunoprecipitation, gel filtration, surface plasmon resonance |
Biochemical and biophysical research communications |
High |
15950934
|
| 1996 |
CRISP3 expression in mouse B cells is transcriptionally activated by the Oct2 transcription factor via two variant octamer motifs in the CRISP3 promoter; the C-terminal transactivation domain of Oct2 is required, and CRISP3 is specifically expressed at the pre-B-cell stage. |
Nuclear run-on experiments, Oct2-deficient primary B cells, cotransfection reporter assays, site-directed mutagenesis of octamer motifs, in vitro Oct2–DNA binding |
Molecular and cellular biology |
High |
8887646
|
| 1993 |
CRISP3 gene expression in mouse salivary gland is strongly androgen-dependent, as demonstrated by castration abolishing/reducing expression in male mice and absence of expression in female salivary gland. |
cDNA cloning, RNA blot analysis of castrated vs. intact males and females |
Endocrinology |
Medium |
8319566
|
| 1995 |
The mouse CRISP3 gene spans over 20 kb, consists of eight exons and seven introns, has a TATA box-proximal transcription start site, and contains two androgen-responsive element consensus sequences in its promoter along with putative OTF- and GATA-binding elements. |
Genomic library screening, DNA sequencing, primer extension mapping, PCR sizing of introns |
The Biochemical journal |
Medium |
7639699
|
| 2008 |
NMR analysis of the MSP–CRISP3 complex shows that only one side of MSP (comprising beta-strands 1, 4, 5, and 8, with beta-strands 1 and 8 forming the main binding surface) is affected by complex formation with the N-terminal SCP domain of CRISP3. |
Multidimensional NMR (15N-HSQC and 3D-NMR of triply-labeled MSP in complex with recombinant N-terminal CRISP3 domain) |
Biochemical and biophysical research communications |
Medium |
19026612
|
| 2011 |
Equine CRISP3 purified from seminal plasma suppresses binding between spermatozoa and polymorphonuclear neutrophils (PMNs), identifying CRISP3 as a seminal plasma protein that modulates sperm elimination from the female reproductive tract. |
Sequential ammonium sulfate precipitation, size-exclusion and ion-exchange chromatography, 1D/2D SDS-PAGE, Western blotting, flow cytometry PMN/sperm binding assay |
Biology of reproduction |
High |
21389342
|
| 2010 |
Human CRISP3 binds alpha-1B-glycoprotein (A1BG) in serum; A1BG orthologs from cow, horse, and rabbit also bind CRISP3, while mouse kininogen-1 binds CRISP3 in mouse serum, suggesting a conserved mechanism of CRISP binding by A1BG-family proteins. |
Gel filtration, ligand blotting, affinity isolation, mass spectrometry, N-terminal sequencing |
Biochimica et biophysica acta |
Medium |
20116414
|
| 2013 |
The binding interface of PSP94–CRISP3 complex was mapped: PSP94 residues Y3, F4, P56, and its C-terminal beta-strand (plus the C37–C73 disulfide bond) are critical for CRISP3 binding; on CRISP3, the N-terminal SCP domain alone is insufficient—the hinge region is also required, but the C-terminal ICR domain is not. |
Site-directed mutagenesis of PSP94 and CRISP3, co-immunoprecipitation |
Biochimica et biophysica acta |
Medium |
23375721
|
| 2014 |
Native, glycosylated human and mouse CRISP3 expressed in HEK 293 cells exist as monomers in solution; N-glycosylation sites and patterns differ between human and mouse CRISP3. |
Eukaryotic expression in HEK 293 cells, ion exchange and size exclusion chromatography, substrate-affinity assays, glycosylation characterization |
Scientific reports |
Medium |
24573035
|
| 2011 |
CRISP3 is a direct transcriptional target of the ERG transcription factor (driven by TMPRSS2-ERG fusion) in prostate cancer, as shown by chromatin immunoprecipitation with an anti-ERG antibody demonstrating ERG binding at the CRISP3 locus. |
Genome-wide mRNA expression analysis, quantitative RT-PCR, immunohistochemistry, chromatin immunoprecipitation (ChIP) with anti-ERG antibody |
PloS one |
Medium |
21814574
|
| 2018 |
CRISP3 expression in prostate cancer cells is androgen-dependent and regulated by androgen receptor (AR) through epigenetic mechanisms: in AR-negative cells the CRISP3 promoter is silenced by histone deacetylation; DHT treatment of LNCaP cells increases CRISP3 transcript and protein; AR occupancy at the CRISP3 promoter was confirmed by ChIP. |
Luciferase reporter assays with CRISP3 promoter fragments, ChIP-PCR, DHT treatment, histone deacetylase inhibition |
The Journal of steroid biochemistry and molecular biology |
Medium |
29477539
|
| 2015 |
Recombinant CRISP3 enhances adhesion and proliferation of human endometrial epithelial cells in vitro; CRISP3 is secreted by primary human endometrial epithelial cells and accumulates in uterine lavage fluid, with higher abundance during the proliferative phase. |
Treatment of endometrial epithelial cells with recombinant CRISP3, adhesion and proliferation assays, uterine lavage ELISA, immunohistochemistry |
Biology of reproduction |
Medium |
25715794
|
| 2020 |
CRISP3 facilitates prostate cancer progression from carcinoma in situ to invasive cancer in vivo; CRISP3 exposure enhances cancer cell motility and invasion; mass spectrometry revealed CRISP3 induces changes in abundance of cell-cell adhesion proteins LASP1 and TJP1 both in vivo and in vitro. |
Genetically engineered mouse model of prostate cancer, human and mouse prostate cancer cell motility/invasion assays, mass spectrometry proteomics |
Endocrine-related cancer |
High |
32357309
|
| 2010 |
PSP94 and CRISP3 each independently inhibit prostate cancer cell growth in a cell-line-specific manner; growth inhibition by CRISP3 is not affected by presence or absence of PSP94, suggesting CRISP3 participates in PSP94-independent activities. |
Ectopic expression of PSP94 and CRISP3 in prostate cell lines, clonogenic survival assay, Western blot, immunofluorescence |
Asian journal of andrology |
Medium |
20676114
|
| 2016 |
CRISP3 was purified from human seminal plasma using PSP94-immobilized affinity chromatography and confirmed to bind PSP94 with high affinity by surface plasmon resonance; it exists as glycosylated (~28 kDa) and unglycosylated (~26 kDa) forms. |
PSP94-affinity chromatography, SDS-PAGE, immunoblotting, MALDI-TOF MS, deglycosylation, surface plasmon resonance |
Journal of chromatography B |
Medium |
27825912
|
| 2024 |
Exogenous CRISP3 downregulates P2RX7 (an ATP-gated ion channel) in PC3 prostate cancer cells and THP1 macrophages, reducing ATP-induced cytotoxicity and IL-1β secretion; this effect is abrogated when CRISP3 is complexed with PSP94. CRISP3 mediates these effects through CITED2 (a transcriptional coregulator that reduces p300 availability at the P2RX7 promoter); PSP94 also affects CRISP3 endocytosis and its interaction with flotillin-2. |
Recombinant protein treatment, P2RX7 expression assays, ATP cytotoxicity assay, IL-1β ELISA, antibody array, CITED2 overexpression, CUT&RUN assay for p300 at P2RX7 promoter, Co-IP with flotillin-2 |
Biochimica et biophysica acta. Molecular cell research |
Medium |
40473221
|
| 2024 |
Boar CRISP3 is localized in the post-acrosomal region of the sperm head and migrates to the anterior end of the tail after capacitation; recombinant CRISP3 downregulates inflammatory factors IL-1α, IL-1β, and IL-6 in LPS-stimulated RAW264.7 macrophages, indicating immunomodulatory function. |
Immunofluorescence localization, recombinant protein treatment of macrophages, RT-PCR and Western blot for inflammatory cytokines |
International journal of molecular sciences |
Medium |
38396941
|
| 2024 |
Equine seminal plasma CRISP3 selectively suppresses PMN binding to live spermatozoa but not to dead spermatozoa or bacteria; immunocytochemistry confirmed CRISP3 binds to live but not dead spermatozoa, suggesting selective recognition of viable sperm surface. |
CRISP3 purification from seminal plasma, flow cytometry PMN binding assay with live/dead sperm populations, immunocytochemistry |
Theriogenology |
Medium |
38377715
|
| 2024 |
EP300 histone acetyltransferase regulates CRISP3 expression in triple-negative breast cancer by modifying H3K27ac at the CRISP3 promoter; CRISP3 overexpression promotes tumor stemness and lobaplatin resistance, and knockdown of EP300 reduces these phenotypes in a manner rescued by CRISP3 overexpression. |
ChIP for H3K27ac at CRISP3 promoter, EP300 knockdown and CRISP3 overexpression rescue experiments, in vitro and in vivo stemness/resistance assays |
Human cell |
Medium |
38879857
|
| 2022 |
hsa_circ_0003823 promotes ESCC progression and apatinib resistance through the miR-607/CRISP3 axis: the circular RNA sequesters miR-607, leading to upregulation of CRISP3; CRISP3 was validated as a miR-607 target by RNA immunoprecipitation and dual-luciferase reporter assays. |
RNA immunoprecipitation (RIP), dual-luciferase reporter assay, Western blot, knockdown experiments |
International journal of biological sciences |
Medium |
36263172
|
| 2026 |
CRISP3 acts as a tumor suppressor in high-grade serous ovarian carcinoma by inhibiting cell proliferation, migration, and invasion through suppression of the PI3K/AKT signaling pathway; CRISP3 knockdown activates PI3K/AKT and overexpression suppresses it. |
CRISP3 knockdown and overexpression in HGSOC cells, CCK-8/EdU proliferation and Transwell invasion assays, RNA-seq, GSEA, Western blotting for PI3K/AKT pathway components, in vivo mouse model |
Biomedicines |
Medium |
41751369
|