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CRISP2  -  cysteine-rich secretory protein 2

Homo sapiens

Synonyms: CRISP-2, CT36, Cancer/testis antigen 36, Cysteine-rich secretory protein 2, GAPDL5, ...
 
 
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Disease relevance of CRISP2

  • Overall, our results provide evidence that a fibrinogen-binding sequence located within the N-terminal domain of TSP-1 mediates the binding of osteosarcoma cell surface-associated TSP-1 to platelet-bound fibrinogen [1].
  • RESULTS: The antibody raised against the 4N1K peptide recognized protein fragments of matrix metalloproteinase 3-digested TSP1 and positively stained the sections of renal cancer tissues [2].
  • The involvement of TSP-1 in the motility of malignant glioma cells was investigated by transfection of TSP-1 complementary deoxyribonucleic acid (cDNA) sense and antisense expression vectors into the glioblastoma cell line T98G-G7 that secretes high amounts of TSP-1 [3].
  • Antibody array profiling reveals serum TSP-1 as a marker to distinguish benign from malignant prostatic disease [4].
  • Based on its effects on tumors, TSP1 is thought to be a potential regulator of tumor growth and metastasis [5].
 

High impact information on CRISP2

  • Finally, TSP1-/- endothelial cells revealed that the antiangiogenic response mediated by ADAMTS1 is greatly dependent on TSP1 [6].
  • Purified soluble TSP-1 added to cultures induced a strong dose-dependent growth inhibition and a slowly developing maturation-independent cell death [7].
  • Less frequently, in 28% of the plasmas, antibodies reacted with the TSP1 repeats 2 to 8 [8].
  • TSP1 and an alpha3beta1 integrin-binding peptide from TSP1 also inhibited proliferation when added in solution [9].
  • High-affinity binding of 125I-labeled TSP1 to OH-1 cells was heparin-dependent and may be mediated by sulfated glycolipids, which are the major sulfated glycoconjugates synthesized by these cells [9].
 

Biological context of CRISP2

  • The comparison of the predicted coding sequences of Tpx-1 and TPX1 showed 77.8% nucleotide and 70% amino acid sequence similarity [10].
  • Together, these results indicate that human TPX1 would be a component of the sperm acrosome that remains associated with sperm after capacitation and AR, and is relevant for sperm-oocyte interaction [11].
  • The presence of anti-TPX1 during gamete co-incubation produced a significant and dose-dependent inhibition in the percentage of penetrated zona-free hamster oocytes without affecting sperm motility, the AR or sperm binding to the oolema [11].
  • Adhesion on TSP1 weakly inhibited SCLC cell proliferation, but this inhibition was strongly enhanced in the presence of epidermal growth factor [9].
  • However, active sites mimicking the function of TSP-1 during platelet-osteosarcoma cell interaction are not known [1].
 

Anatomical context of CRISP2

 

Associations of CRISP2 with chemical compounds

  • It displays all 16 conserved cysteine residues and shows 82% homology to human and 78% to guinea pig CRISP-2 (AA1, TPX 1) and 77% to human CRISP-3 [14].
  • Thrombospondin 1 (TSP1) is a homotrimeric glycoprotein composed of 150-kDa subunits connected by disulfide bridges [15].
  • Metalloprotease domain did not bind GST-VWF73-H detectably, but the disintegrin domain, first TSP1 repeat, Cys-rich domain, and spacer domain bound GST-VWF73-H with K(d) values of 489, 136, 121, and 108 nm, respectively [16].
  • These results provide direct evidence for high capacity, cooperative and specific binding of Ca2+ to conformationally labile aspartate-rich repeats of TSP1 [17].
  • Ca2+ binding to TSP1 was found to be cooperative with 10% occupancy at 15-20 microM CaCl2, 90% occupancy at 100 microM CaCl2, and a Hill coefficient of 2.4 +/- 0.2 The average apparent Kd was 52 +/- 5 microM [17].
 

Other interactions of CRISP2

 

Analytical, diagnostic and therapeutic context of CRISP2

References

  1. Platelet-osteosarcoma cell interaction is mediated through a specific fibrinogen-binding sequence located within the N-terminal domain of thrombospondin 1. Voland, C., Serre, C.M., Delmas, P., Clézardin, P. J. Bone Miner. Res. (2000) [Pubmed]
  2. Expression of thrombospondin-derived 4N1K peptide-containing proteins in renal cell carcinoma tissues is associated with a decrease in tumor growth and angiogenesis. Miyata, Y., Koga, S., Takehara, K., Kanetake, H., Kanda, S. Clin. Cancer Res. (2003) [Pubmed]
  3. Antisense-mediated reduction in thrombospondin-1 expression reduces cell motility in malignant glioma cells. Amagasaki, K., Sasaki, A., Kato, G., Maeda, S., Nukui, H., Naganuma, H. Int. J. Cancer (2001) [Pubmed]
  4. Antibody array profiling reveals serum TSP-1 as a marker to distinguish benign from malignant prostatic disease. Shafer, M.W., Mangold, L., Partin, A.W., Haab, B.B. Prostate (2007) [Pubmed]
  5. Stromal expression of thrombospondin-1 is correlated with growth and metastasis of human gallbladder carcinoma. Ohtani, Y., Kijima, H., Dowaki, S., Kashiwagi, H., Tobita, K., Tsukui, M., Tanaka, Y., Tsuchida, T., Tokunaga, T., Yamazaki, H., Nakamura, M., Ueyama, Y., Tanaka, M., Tajima, T., Makuuchi, H. Int. J. Oncol. (1999) [Pubmed]
  6. ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2. Lee, N.V., Sato, M., Annis, D.S., Loo, J.A., Wu, L., Mosher, D.F., Iruela-Arispe, M.L. EMBO J. (2006) [Pubmed]
  7. Type 3 repeat/C-terminal domain of thrombospondin-1 triggers caspase-independent cell death through CD47/alphavbeta3 in promyelocytic leukemia NB4 cells. Saumet, A., Slimane, M.B., Lanotte, M., Lawler, J., Dubernard, V. Blood (2005) [Pubmed]
  8. Epitope mapping of ADAMTS13 autoantibodies in acquired thrombotic thrombocytopenic purpura. Klaus, C., Plaimauer, B., Studt, J.D., Dorner, F., Lämmle, B., Mannucci, P.M., Scheiflinger, F. Blood (2004) [Pubmed]
  9. Thrombospondin-1 promotes alpha3beta1 integrin-mediated adhesion and neurite-like outgrowth and inhibits proliferation of small cell lung carcinoma cells. Guo, N., Templeton, N.S., Al-Barazi, H., Cashel, J.A., Sipes, J.M., Krutzsch, H.C., Roberts, D.D. Cancer Res. (2000) [Pubmed]
  10. Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene. Kasahara, M., Gutknecht, J., Brew, K., Spurr, N., Goodfellow, P.N. Genomics (1989) [Pubmed]
  11. Human testicular protein TPX1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction. Busso, D., Cohen, D.J., Hayashi, M., Kasahara, M., Cuasnicú, P.S. Mol. Hum. Reprod. (2005) [Pubmed]
  12. The human cysteine-rich secretory protein (CRISP) family. Primary structure and tissue distribution of CRISP-1, CRISP-2 and CRISP-3. Krätzschmar, J., Haendler, B., Eberspaecher, U., Roosterman, D., Donner, P., Schleuning, W.D. Eur. J. Biochem. (1996) [Pubmed]
  13. Evidence for an alpha-granular pool of the cytoskeletal protein alpha-actinin in human platelets that redistributes with the adhesive glycoprotein thrombospondin-1 during the exocytotic process. Dubernard, V., Arbeille, B.B., Lemesle, M.B., Legrand, C. Arterioscler. Thromb. Vasc. Biol. (1997) [Pubmed]
  14. Equine CRISP-3: primary structure and expression in the male genital tract. Schambony, A., Gentzel, M., Wolfes, H., Raida, M., Neumann, U., Töpfer-Petersen, E. Biochim. Biophys. Acta (1998) [Pubmed]
  15. Physical characterization of the procollagen module of human thrombospondin 1 expressed in insect cells. Misenheimer, T.M., Huwiler, K.G., Annis, D.S., Mosher, D.F. J. Biol. Chem. (2000) [Pubmed]
  16. The proximal carboxyl-terminal domains of ADAMTS13 determine substrate specificity and are all required for cleavage of von Willebrand factor. Ai, J., Smith, P., Wang, S., Zhang, P., Zheng, X.L. J. Biol. Chem. (2005) [Pubmed]
  17. Calcium ion binding to thrombospondin 1. Misenheimer, T.M., Mosher, D.F. J. Biol. Chem. (1995) [Pubmed]
  18. Characterization and localization of cysteine-rich secretory protein 3 (CRISP-3) in the human male reproductive tract. Udby, L., Bjartell, A., Malm, J., Egesten, A., Lundwall, A., Cowland, J.B., Borregaard, N., Kjeldsen, L. J. Androl. (2005) [Pubmed]
  19. Unique distribution of thrombospondin-1 in human ocular surface epithelium. Sekiyama, E., Nakamura, T., Cooper, L.J., Kawasaki, S., Hamuro, J., Fullwood, N.J., Kinoshita, S. Invest. Ophthalmol. Vis. Sci. (2006) [Pubmed]
  20. Production and accumulation of thrombospondin-1 in human retinal pigment epithelial cells. Miyajima-Uchida, H., Hayashi, H., Beppu, R., Kuroki, M., Fukami, M., Arakawa, F., Tomita, Y., Kuroki, M., Oshima, K. Invest. Ophthalmol. Vis. Sci. (2000) [Pubmed]
  21. Immunolocalization of thrombospondin-1 in human atherosclerotic and restenotic arteries. Riessen, R., Kearney, M., Lawler, J., Isner, J.M. Am. Heart J. (1998) [Pubmed]
 
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