Cross-link in Fibrin Polymerized by Factor XIII: ε-(γ-Glutamyl)lysine

@article{Pisano1968CrosslinkIF,
  title={Cross-link in Fibrin Polymerized by Factor XIII: $\epsilon$-($\gamma$-Glutamyl)lysine},
  author={Judge Joel Pisano and J. S. Finlayson and Marjorie P. Peyton},
  journal={Science},
  year={1968},
  volume={160},
  pages={892 - 893}
}
ε-(γ-Glutamyl)lysine has been isolated from enzymatic hydrolyzates of cross-linked human fibrin. This compound was not detected in "non-cross-linked" fibrin prepared with ethylenediaminetetraacetic acid, which inhibits factor XIII; intermediate amounts were observed when the fibrin was prepared with glycine ethyl ester, which inhibits factor XIII competitively. These and ancillary experiments furnish conclusive evidence that ε-(γ-glutamyl)lysine cross-links form in human fibrin during… Expand
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  • T. Takagi, S. Iwanaga
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
  • 1970
TLDR
The cross-linkage in stabilized fibrin may be formed with one or two pairs of γ-chain peptides, because the molecular weight of “X” isolated from S-sulfo-stabilized fibrIn seems to be approximately 150,000 to 200,000, judging from the elution volume on a Sepharose 6B column. Expand
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  • L. Lorand
  • Chemistry, Medicine
  • Annals of the New York Academy of Sciences
  • 2001
TLDR
Analysis of the individual reaction steps and regulatory control mechanisms involved in clot stabilization enabled us to reconstruct the entire physiological process and serves as a guide for the differential diagnosis of the variety of molecular defects of fibrin stabilization. Expand
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Salmon plasma contains an exceedingly active protease which possesses the ability to rapidly destroy fibrinogen clottability even when the plasma is stored at a temperature of −20°C. Expand
Defect in the gamma polypeptide chain of a congenital abnormal fibrinogen (Paris I)
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Thrombin converts Factor XIII to an active form, called plasma transglutaminase3, which in turn catalyses the formation of covalentγ-glutamyl-ε-lysine isopeptide bonds4 between two γ chains and more than two α chains of different fibrin molecules5 to render it resistant to chemical or physical modifications. Expand
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It is suggested that the α chain crosslinks are removed from crosslinked fibrin by plasmin attack, since the D-like core fragment of crosslinkedfibrin is really a dimer of D and may be readily confused with the early degradation fragments of fibr inogen (X and Y) and could further confuse the distinction between fibrInogen and fibrine degradation products. Expand
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It is indicated that the FXIIIa-induced dimeric cross-linking of gamma-chains by itself is not sufficient to stiffen the fibrin networks, and the augmentation of clot rigidity was more strongly correlated with the formation of Gamma-multimers, alpha(n)-polymers, and alpha(p)gamma(q)-hybrid cross-links. Expand
Identification of respective lysine donor and glutamine acceptor sites involved in factor XIIIa-catalyzed fibrin α chain cross-linking.
  • Weixun Wang
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 2011
TLDR
A fit-for-purpose algorithm was developed to assign cross-linked peptide pairs of fibrin α chains to the monoisotopic masses relying on accurate mass measurement as the primary criterion for identification and tandem mass spectrometry was used to confirm the identities of the cross- linked peptides. Expand
Amino acid sequence of the factor XIIIa acceptor site in bovine plasma fibronectin
TLDR
The ammo acid sequence in bovine fibronectin is reported which contains the glutamine residue labelled with radioactive putrescine by factor XIII, located at position 3 from the N-terminus of fibronECTin. Expand
Fibrin cross-linking in congenital factor XIII deficiency.
TLDR
The results indicate that the homozygous patients reported here were not completely devoid of functioning factor XIII, and the range of transamidase activity was 0.5-1.7%. Expand
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