Effect of phosphorylation in vitro of human fibrinogen with protein kinase C on thrombin-induced gelation.
Thrombin-induced gel formation of fibrinogen phosphorylated by protein kinase C yielded a transparent gel, whereas unphosphorylated fibrinogen yielded a coarse gel. The mass-length ratio was found to be one order of magnitude higher for the unphosphorylated than for the phosphorylated fibrinogen. Since the phosphorylated sites are located near the cross-linking sites in the A alpha-chain of fibrinogen, it is likely that the introduction of charged phosphate groups in this region prevent the lateral growth of the fibrin fibres.
Heldin
P
P
Department of Physiological Chemistry, University of Uppsala, Sweden.
Hessel
B
B
Humble
E
E
Blombäck
B
B
Engström
L
L
D004591:Electrophoresis, Polyacrylamide Gel; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism* / Q000502:physiology; D005344:Fibrinopeptide A / Q000378:metabolism; D005345:Fibrinopeptide B / Q000378:metabolism; D006801:Humans; D010766:Phosphorylation; D011487:Protein Conformation; D011493:Protein Kinase C / Q000494:pharmacology*; D013917:Thrombin / Q000494:pharmacology*; D013997:Time Factors
D005344:Fibrinopeptide A; D005345:Fibrinopeptide B; D005337:Fibrin; D005340:Fibrinogen; D011493:Protein Kinase C; D013917:Thrombin