Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin α2β1

• Published in: Blood Vol. 102; no. 6; pp. 2085 - 2092
• Main Authors: Lahav, Judith, Wijnen, Eveline M., Hess, Oded, Hamaia, Samir W., Griffiths, Delia, Makris, Michael, Knight, C. Graham, Essex, David W., Farndale, Richard W.
• Format: Journal Article
• Language: English
• Published: Washington, DC Elsevier Inc 15.09.2003; The Americain Society of Hematology
• Subjects: Biological and medical sciences; Blood coagulation. Blood cells; Fundamental and applied biological sciences. Psychology; Hematologic and hematopoietic diseases; Medical sciences; Molecular and cellular biology; Platelet; Platelet diseases and coagulopathies; Human; Membrane protein; Thiol; Molecular structure; Glycoprotein; Glycoprotein VI; Hemopathy; Glanzmann thrombasthenia; Adhesion; Genetic disease; Thrombocytopathy; Platelet; Disulfites; Disulfide bond; Collagen; Platelet function; Very late antigène 2; Catalysis

Integrin α2β1 is the principal adhesive receptor for collagen but platelets also adhere through glycoprotein VI (GPVI). Integrin αIIbβ3 may augment platelet adhesion. We have shown that disulfide exchange is necessary for platelet adhesion to fibrinogen, fibronectin, and collagen. However 2 question...