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Biochemical Journal logoLink to Biochemical Journal
. 1995 Nov 15;312(Pt 1):239–244. doi: 10.1042/bj3120239

Analysis of transcripts encoding novel members of the mammalian metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family and their expression in reproductive and non-reproductive monkey tissues.

A C Perry 1, R Jones 1, L Hall 1
PMCID: PMC1136250  PMID: 7492319

Abstract

A number of sequence-related, cysteine-rich proteins containing metalloprotease-like and disintegrin-like domains (the MDC protein family), at least one of which has been shown to play a role in egg recognition during fertilization, are abundantly expressed in the mammalian male reproductive tract. In this paper we report the cloning and sequence analysis of three closely related isoforms of a novel member of this family which are expressed not only in the testis, but also in the liver, albeit at a lower level. Using a PCR-based approach we also demonstrate the presence of transcripts encoding additional, novel, disintegrin-containing proteins, in the liver and epididymis. We conclude that while some members of the MDC family are specific to the reproductive tract, suggesting functions peculiar to those tissues, others have a broader tissue distribution and may therefore play a more general role in integrin-mediated cell-cell recognition, adhesion or signalling.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Au L. C., Huang Y. B., Huang T. F., Teh G. W., Lin H. H., Choo K. B. A common precursor for a putative hemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodostoma: molecular cloning and sequence analysis. Biochem Biophys Res Commun. 1991 Dec 16;181(2):585–593. doi: 10.1016/0006-291x(91)91230-a. [DOI] [PubMed] [Google Scholar]
  2. Barker H. L., Perry A. C., Jones R., Hall L. Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) protein family. Biochim Biophys Acta. 1994 Aug 2;1218(3):429–431. doi: 10.1016/0167-4781(94)90198-8. [DOI] [PubMed] [Google Scholar]
  3. Blobel C. P., Myles D. G., Primakoff P., White J. M. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J Cell Biol. 1990 Jul;111(1):69–78. doi: 10.1083/jcb.111.1.69. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blobel C. P., Wolfsberg T. G., Turck C. W., Myles D. G., Primakoff P., White J. M. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 1992 Mar 19;356(6366):248–252. doi: 10.1038/356248a0. [DOI] [PubMed] [Google Scholar]
  5. Emi M., Katagiri T., Harada Y., Saito H., Inazawa J., Ito I., Kasumi F., Nakamura Y. A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers. Nat Genet. 1993 Oct;5(2):151–157. doi: 10.1038/ng1093-151. [DOI] [PubMed] [Google Scholar]
  6. Fusi F. M., Vignali M., Busacca M., Bronson R. A. Evidence for the presence of an integrin cell adhesion receptor on the oolemma of unfertilized human oocytes. Mol Reprod Dev. 1992 Mar;31(3):215–222. doi: 10.1002/mrd.1080310309. [DOI] [PubMed] [Google Scholar]
  7. Fusi F. M., Vignali M., Gailit J., Bronson R. A. Mammalian oocytes exhibit specific recognition of the RGD (Arg-Gly-Asp) tripeptide and express oolemmal integrins. Mol Reprod Dev. 1993 Oct;36(2):212–219. doi: 10.1002/mrd.1080360212. [DOI] [PubMed] [Google Scholar]
  8. Gomis-Rüth F. X., Kress L. F., Bode W. First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases. EMBO J. 1993 Nov;12(11):4151–4157. doi: 10.1002/j.1460-2075.1993.tb06099.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hite L. A., Jia L. G., Bjarnason J. B., Fox J. W. cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins. Arch Biochem Biophys. 1994 Jan;308(1):182–191. doi: 10.1006/abbi.1994.1026. [DOI] [PubMed] [Google Scholar]
  10. Miyata T., Takeya H., Ozeki Y., Arakawa M., Tokunaga F., Iwanaga S., Omori-Satoh T. Primary structure of hemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis. J Biochem. 1989 May;105(5):847–853. doi: 10.1093/oxfordjournals.jbchem.a122756. [DOI] [PubMed] [Google Scholar]
  11. Musial J., Niewiarowski S., Rucinski B., Stewart G. J., Cook J. J., Williams J. A., Edmunds L. H., Jr Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins. RGD-containing peptides from viper venoms. Circulation. 1990 Jul;82(1):261–273. doi: 10.1161/01.cir.82.1.261. [DOI] [PubMed] [Google Scholar]
  12. Neeper M. P., Jacobson M. A. Sequence of a cDNA encoding the platelet aggregation inhibitor trigramin. Nucleic Acids Res. 1990 Jul 25;18(14):4255–4255. doi: 10.1093/nar/18.14.4255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Osaka A., Just M., Habermann E. Action of snake venom hemorrhagic principles on isolated glomerular basement membrane. Biochim Biophys Acta. 1973 Oct 25;323(3):415–428. doi: 10.1016/0005-2736(73)90187-9. [DOI] [PubMed] [Google Scholar]
  14. Paine M. J., Desmond H. P., Theakston R. D., Crampton J. M. Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family. J Biol Chem. 1992 Nov 15;267(32):22869–22876. [PubMed] [Google Scholar]
  15. Palombi F., Salanova M., Tarone G., Farini D., Stefanini M. Distribution of beta 1 integrin subunit in rat seminiferous epithelium. Biol Reprod. 1992 Dec;47(6):1173–1182. doi: 10.1095/biolreprod47.6.1173. [DOI] [PubMed] [Google Scholar]
  16. Patriarca C., Roncalli M., Gambacorta M., Cominotti M., Coggi G., Viale G. Patterns of integrin common chain beta 1 and collagen IV immunoreactivity in hepatocellular carcinoma. Correlations with tumour growth rate, grade and size. J Pathol. 1993 Sep;171(1):5–11. doi: 10.1002/path.1711710104. [DOI] [PubMed] [Google Scholar]
  17. Perry A. C., Barker H. L., Jones R., Hall L. Genetic evidence for an additional member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family of mammalian proteins and its abundant expression in the testis. Biochim Biophys Acta. 1994 Jul 20;1207(1):134–137. doi: 10.1016/0167-4838(94)90062-0. [DOI] [PubMed] [Google Scholar]
  18. Perry A. C., Gichuhi P. M., Jones R., Hall L. Cloning and analysis of monkey fertilin reveals novel alpha subunit isoforms. Biochem J. 1995 May 1;307(Pt 3):843–850. doi: 10.1042/bj3070843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Perry A. C., Jones R., Barker P. J., Hall L. A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptides. Biochem J. 1992 Sep 15;286(Pt 3):671–675. doi: 10.1042/bj2860671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Primakoff P., Hyatt H., Myles D. G. A role for the migrating sperm surface antigen PH-20 in guinea pig sperm binding to the egg zona pellucida. J Cell Biol. 1985 Dec;101(6):2239–2244. doi: 10.1083/jcb.101.6.2239. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Takeya H., Oda K., Miyata T., Omori-Satoh T., Iwanaga S. The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis. J Biol Chem. 1990 Sep 25;265(27):16068–16073. [PubMed] [Google Scholar]
  22. Weskamp G., Blobel C. P. A family of cellular proteins related to snake venom disintegrins. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2748–2751. doi: 10.1073/pnas.91.7.2748. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wolfsberg T. G., Bazan J. F., Blobel C. P., Myles D. G., Primakoff P., White J. M. The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10783–10787. doi: 10.1073/pnas.90.22.10783. [DOI] [PMC free article] [PubMed] [Google Scholar]

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