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. 1996 Sep 1;318(Pt 2):459–462. doi: 10.1042/bj3180459

Cloning of a novel membrane-linked metalloproteinase from human myeloma cells.

N McKie 1, D J Dallas 1, T Edwards 1, J F Apperley 1, R G Russell 1, P I Croucher 1
PMCID: PMC1217643  PMID: 8809033

Abstract

We have isolated a novel cDNA from human myeloma cells encoding a member of the reprolysin family of metalloproteinases. Derived amino acid sequence predicts a protein of approx. 76 kDa. The open reading frame predicts the presence of a leader peptide, a pro-peptide with a 'cysteine switch', a metalloproteinase domain, a disintegrin-like domain, a cysteine-rich domain, an epidermal growth factor-like domain and a putative transmembrane sequence. Expression of the mRNA for this metalloproteinase has been demonstrated in human myeloma cells.

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Selected References

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  1. Bjarnason J. B., Fox J. W. Snake venom metalloendopeptidases: reprolysins. Methods Enzymol. 1995;248:345–368. doi: 10.1016/0076-6879(95)48023-4. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. 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]
  4. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987 Apr;162(1):156–159. doi: 10.1006/abio.1987.9999. [DOI] [PubMed] [Google Scholar]
  5. Docherty A. J., O'Connell J., Crabbe T., Angal S., Murphy G. The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases. Trends Biotechnol. 1992 Jun;10(6):200–207. doi: 10.1016/0167-7799(92)90214-g. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Fox J. W., Bjarnason J. B. Atrolysins: metalloproteinases from Crotalus atrox venom. Methods Enzymol. 1995;248:368–387. doi: 10.1016/0076-6879(95)48024-2. [DOI] [PubMed] [Google Scholar]
  8. Gregoretti M. G., Gottardi D., Ghia P., Bergui L., Merico F., Marchisio P. C., Caligaris-Cappio F. Characterization of bone marrow stromal cells from multiple myeloma. Leuk Res. 1994 Sep;18(9):675–682. doi: 10.1016/0145-2126(94)90067-1. [DOI] [PubMed] [Google Scholar]
  9. Manabe A., Coustan-Smith E., Behm F. G., Raimondi S. C., Campana D. Bone marrow-derived stromal cells prevent apoptotic cell death in B-lineage acute lymphoblastic leukemia. Blood. 1992 May 1;79(9):2370–2377. [PubMed] [Google Scholar]
  10. Myles D. G., Kimmel L. H., Blobel C. P., White J. M., Primakoff P. Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4195–4198. doi: 10.1073/pnas.91.10.4195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. 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]
  12. Rawlings N. D., Barrett A. J. Evolutionary families of metallopeptidases. Methods Enzymol. 1995;248:183–228. doi: 10.1016/0076-6879(95)48015-3. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Wolfsberg T. G., Primakoff P., Myles D. G., White J. M. ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J Cell Biol. 1995 Oct;131(2):275–278. doi: 10.1083/jcb.131.2.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Wolfsberg T. G., Straight P. D., Gerena R. L., Huovila A. P., Primakoff P., Myles D. G., White J. M. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol. 1995 May;169(1):378–383. doi: 10.1006/dbio.1995.1152. [DOI] [PubMed] [Google Scholar]
  16. Yoshida S., Setoguchi M., Higuchi Y., Akizuki S., Yamamoto S. Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage. Int Immunol. 1990;2(6):585–591. doi: 10.1093/intimm/2.6.585. [DOI] [PubMed] [Google Scholar]

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