Factor XIIIa-catalyzed cross-linking of platelet and muscle actin regulation by nucleotides

Isaac Cohen*, Tikoes A. Blankenberg, Dennis Borden, David R. Kahn, Arthur Veis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

57 Scopus citations


Actin from human blood platelets or rabbit skeletal muscle can serve as substrate for factor XIIIa. The latter catalyzes the incorporation of 1.5-2 mol monodansylcadaverine/mol rabbit actin and 0.5 mol/mol platelet actin. Highly cross-linked platelet and muscle actin polymers form in the absence of added amines, indicating the presence of both acceptor and donor sites. As expected, the cross-link was found to be a γ-glutamyl-ε{lunate}-lysine bond, with an average of 0.3-0.4 mol dipeptide/mol platelet actin. Both cross-linking and amine incorporation are prevented by ATP, ADP, GTP, CTP, but not by AMP and cyclic AMP. These nucleotides may have important regulatory role in muscle and non-muscle systems.

Original languageEnglish (US)
Pages (from-to)365-375
Number of pages11
JournalBBA - General Subjects
Issue numberC
StatePublished - 1980


  • (Platelet, Muscle)
  • Actin
  • Cross linking
  • Factor XIIIa
  • Nucleotide regulation

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry


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