A family of cellular proteins related to snake venom disintegrins.
- 29 March 1994
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 91 (7) , 2748-2751
- https://doi.org/10.1073/pnas.91.7.2748
Abstract
Disintegrins are short soluble integrin ligands that were initially identified in snake venom. A previously recognized cellular protein with a disintegrin domain was the guinea pig sperm protein PH-30, a protein implicated in sperm-egg membrane binding and fusion. Here we present peptide sequences that are characteristic for several cellular disintegrin-domain proteins. These peptide sequences were deduced from cDNA sequence tags that were generated by polymerase chain reaction from various mouse tissue and a mouse muscle cell line. Northern blot analysis with four sequence tags revealed distinct mRNA expression patterns. Evidently, cellular proteins containing a disintegrin domain define a superfamily of potential integrin ligands that are likely to function in important cell-cell and cell-matrix interactions.Keywords
This publication has 29 references indexed in Scilit:
- Molecular Mechanisms of Sperm-Egg Membrane Binding and Fusion in MammalsDevelopmental Biology, 1993
- Expression of beta 1 integrin complexes on the surface of unfertilized mouse oocyte.1993
- Characterization of the integrin specificities of disintegrins isolated from American pit viper venoms.Journal of Biological Chemistry, 1993
- Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity.Proceedings of the National Academy of Sciences, 1993
- Membrane FusionScience, 1992
- Structure, function and evolutionary relationship of proteins containing a disintegrin domainCurrent Opinion in Cell Biology, 1992
- A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptidesBiochemical Journal, 1992
- Coagulation factor X activating enzyme from Russell's viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains.1992
- Integrins: Versatility, modulation, and signaling in cell adhesionCell, 1992
- A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusionNature, 1992