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Fibrinogen Marburg Fibrin Network Structure

Published online by Cambridge University Press:  02 July 2020

J.P. DiOrio ,
M.W. Mosesson ,
I. Hernandez ,
T. Sugo  and
M. Matsuda
J.P. DiOrio
Affiliation:
Baxter International, Round Lake, IL60073
M.W. Mosesson
Affiliation:
Sinai Samaritan Med Ctr, Univ Wise Med Schl-Milw Clin Campus, Milwaukee, WI53201
I. Hernandez
Affiliation:
Sinai Samaritan Med Ctr, Univ Wise Med Schl-Milw Clin Campus, Milwaukee, WI53201
T. Sugo
Affiliation:
Jichi Med Schl, Tochigi-Ken329-04, Japan
M. Matsuda
Affiliation:
Jichi Med Schl, Tochigi-Ken329-04, Japan
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Extract

Fibrinogen is composed of three pairs of polypeptide chains, termed Aα, Bβ and γ, respectively. Proteolytic conversion of fibrinogen to fibrin by thrombin releases fibrinopeptide A and exposes an N-terminal polymerization site ('EA’) in the central E domain of the molecule. This site interacts with a constitutive complementary site in each outer D domain ('Da’) to drive the molecular assembly process by end-to-middle domain non-covalent ‘Da:EA’ interactions. End-to-end aligned double-stranded fibrils are formed in coordination with another recently described constitutive self-association site (termed ‘D:D’)fhat is situated at the outer end of each D domain. The D:D site contributes to end-to-end molecular alignment of fibrin molecules within each fibril strand. Concomitant branching and lateral fibril associations to form thick fibers, lead to formation of the mature fibrin clot.

Fibrinogen Marburg is a homozygous hypodysfibrinogenemia lacking amino acid residues Aα461- 610 due to a stop codon at position 461 of the Aα chain.

Type
Blood/Immunology
Information
Microscopy and Microanalysis , Volume 5 , Issue S2: Proceedings: Microscopy & Microanalysis '99, Microscopy Society of America 57th Annual Meeting, Microbeam Analysis Society 33rd Annual Meeting, Portland, Oregon August 1-5, 1999 , August 1999 , pp. 1120 - 1121
Copyright
Copyright © Microscopy Society of America

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References

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