Antibody against human α1β1 integrin inhibits HeLa cell adhesion to laminin and to type I, IV, and V collagens Journal Article
| Authors: | Riikonen, T.; Vihinen, P.; Potila, M.; Rettig, W.; Heino, J. |
| Article Title: | Antibody against human α1β1 integrin inhibits HeLa cell adhesion to laminin and to type I, IV, and V collagens |
| Abstract: | In HeLa cells β1 integrin forms heterodimers with α1, α2, α3, α5 and α6 integrin subunits. Integrin αvβ5 can also be detected. A monoclonal antibody SR-84 identified the α1 integrin subunit in immunoprecipitation assays and inhibited α1-related cell adhesion to different matrix proteins, laminin-l and type I, IV, and V collagens, whereas its effect on adhesion to type II collagen was marginal. HeLa cells do not attach to type VI collagen. The presence of magnesium was essential for HeLa cell adhesion, whereas calcium alone was not sufficient and high concentrations of calcium even counteracted the effect of magnesium. Cell adhesion to type I collagen was sensitive to changes in pH, unlike cell adhesion to type IV collagen. We conclude that SR-84 is a valuable tool to study α1 integrin-related functions, and that in HeLa cells α1 β1 integrin is a magnesium-dependent receptor for type I, IV, and V collagens but not for type II and VI collagens. © 1995 Academic Press, Inc. |
| Keywords: | human cell; protein protein interaction; calcium; hela cell; hela cells; monoclonal antibody; collagen type 1; extracellular matrix; antibodies, monoclonal; collagen; immunoprecipitation; cell interaction; cell adhesion; antibody; integrin; matrix protein; laminin; integrins; collagen type 4; magnesium ion; magnesium; calcium ion; human; priority journal; article; collagen type 6; support, non-u.s. gov't; integrin alpha1beta1 |
| Journal Title: | Biochemical and Biophysical Research Communications |
| Volume: | 209 |
| Issue: | 1 |
| ISSN: | 0006-291X |
| Publisher: | Elsevier Science, Inc. |
| Date Published: | 1995-04-06 |
| Start Page: | 205 |
| End Page: | 212 |
| Language: | English |
| DOI: | 10.1006/bbrc.1995.1490 |
| PUBMED: | 7726837 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 28 August 2018 -- Source: Scopus |
