MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains Journal Article
| Authors: | Weskamp, G.; Krätzschmar, J.; Reid, M. S.; Blobel, C. P. |
| Article Title: | MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains |
| Abstract: | Cellular disintegrins are a family of proteins that are related to snake venom integrin ligands and metalloproteases. We have cloned and sequenced the mouse and human homologue of a widely expressed cellular disintegrin, which we have termed MDC9 (for metalloprotease/disintegrin/cysteine-rich protein 9). The deduced mouse and human protein sequences are 82% identical. MDC9 contains several distinct protein domains: a signal sequence is followed by a predomain and a domain with sequence similarity to snake venom metalloproteases, a disintegrin domain, a cysteine-rich region, an EGF repeat, a membrane anchor, and a cytoplasmic tail. The cytoplasmic tail of MDC9 has two proline-rich sequences which can bind the SH3 domain of Src, and may therefore function as SH3 ligand domains. Western blot analysis shows that MDC9 is an ~84-kD glycoprotein in all mouse tissues examined, and in NIH 3T3 fibroblast and C2C12 myoblast mouse cell lines. MDC9 can be both cell surface biotinylated and 125I-labeled in NIH 3T3 mouse fibroblasts, indicating that the protein is present on the plasma membrane. Expression of MDC9 in COS-7 cells yields an 84-kD protein, and immunofluorescence analysis of COS-7 cells expressing MDC9 shows a staining pattern that is consistent with a plasma membrane localization. The apparent molecular mass of 84 kD suggests that MDC9 contains a membrane-anchored metalloprotease and disintegrin domain. We propose that MDC9 might function as a membrane- anchored integrin ligand or metalloprotease, or that MDC9 may combine both activities in one protein. |
| Keywords: | nonhuman; polymerase chain reaction; protein localization; animal cell; mouse; animals; mice; animal tissue; cell line; membrane proteins; immunofluorescence; animalia; cloning, molecular; amino acid sequence; molecular sequence data; sequence homology, amino acid; sequence alignment; cell membrane; ligand; peptides; immunoblotting; cytoplasm; glycoprotein; cysteine; metalloproteinase; adam proteins; 3t3 cells; dna, complementary; northern blotting; disintegrin; disintegrins; metalloendopeptidases; snake venom; humans; priority journal; article; src homology domains; serpentes; cercopithecidae |
| Journal Title: | Journal of Cell Biology |
| Volume: | 132 |
| Issue: | 4 |
| ISSN: | 0021-9525 |
| Publisher: | Rockefeller University Press |
| Date Published: | 1996-02-15 |
| Start Page: | 717 |
| End Page: | 726 |
| Language: | English |
| DOI: | 10.1083/jcb.132.4.717 |
| PUBMED: | 8647900 |
| PROVIDER: | scopus |
| PMCID: | PMC2199860 |
| DOI/URL: | |
| Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |
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