| Autor: |
Hartfield, P.J., Greaves, M.W., Camp, R.D.R. |
| Zdroj: |
Biochemical and Biophysical Research Communications; November 15, 1993, Vol. 196 Issue: 3 p1183-1187, 5p |
| Abstrakt: |
Treatment of T lymphoblasts with stimuli that mobilize [Ca2+]i, such as ionophores (ionomycin and A23187) and endoplasmic reticulum Ca2+-ATPase inhibitors (thapsigargin, 2,5-di-(tert.-butyl)-hydroquinone and cyclopiazonic acid), activated T cell binding to extracellular matrix (ECM) proteins. T lymphoblast adhesion to ECM proteins stimulated by ionomycin, thapsigargin, or PMA was inhibited by an anti-β1 integrin mAb (4B4), confirming the role of β1 integrins in regulated T cell-ECM interactions. Study of the α integrin subunit specificity of activated lymphoblast-fibronectin interactions demonstrated that α5β1 was the major integrin receptor regulating binding to fibronectin. These results indicate that intracellular Ca2+ mobilization plays a major contributory role in the activation of T cell β1 integrins.Copyright 1993, 1999 Academic Press |
| Databáze: |
Supplemental Index |
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