Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.

Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Research Abstract Details 

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Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Abstract Text:

Rustem I Litvinov,Sergiy Yakovlev,Galina Tsurupa,Oleg V Gorkun,Leonid Medved,John W Weisel,

The carboxyl-terminal regions of the fibrinogen Aalpha chains (alphaC regions) form compact alphaC-domains tethered to the bulk of the molecule with flexible alphaC-connectors. It was hypothesized that in fibrinogen two alphaC-domains interact intramolecularly with each other and with the central E region preferentially through its N-termini of Bbeta chains and that removal of fibrinopeptides A and B upon fibrin assembly results in dissociation of the alphaC regions and their switch to intermolecular interactions. To test this hypothesis, we studied the interactions of the recombinant alphaC region (Aalpha221-610 fragment) and its subfragments, alphaC-connector (Aalpha221-391) and alphaC-domain (Aalpha392-610), between each other and with the recombinant (Bbeta1-66)2 and (beta15-66)2 fragments and NDSK corresponding to the fibrin(ogen) central E region, using laser tweezers-based force spectroscopy. The alphaC-domain, but not the alphaC-connector, bound to NDSK, which contains fibrinopeptides A and B, and less frequently to desA-NDSK and (Bbeta1-66)2 containing only fibrinopeptides B; it was poorly reactive with desAB-NDSK and (beta15-66)2 both lacking fibrinopeptide B. The interactions of the alphaC-domains with each other and with the alphaC-connector were also observed, although they were weaker and heterogeneous in strength. These results provide the first direct evidence for the interaction between the alphaC-domains and the central E region through fibrinopeptide B, in agreement with the hypothesis given above, and indicate that fibrinopeptide A is also involved. They also confirm the hypothesized homomeric interactions between the alphaC-domains and display their interaction with the alphaC-connectors, which may contribute to covalent cross-linking of alpha polymers in fibrin.

Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Publishing Authors By Initials

RI Litvinov,S Yakovlev,G Tsurupa,OV Gorkun,L Medved,JW Weisel,

For similar proteins: recombinant proteins research abstracts see: proteins: recombinant proteins research

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Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Biochemistry

VOLUME: 46

Page Numbers: 9133-42

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 13

MONTH: 07

YEAR: 2007

Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370623

Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Keywords Mesh Terms:

KEYWORDS: Recombinant Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other. Information

Substance Name: Fibrinogen

Registry Number: 9001-32-5

Grant and Affiliation Information for Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.

AFFILIATION: Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6058, USA. litvinov@mail.med.upenn.edu

Country: United States

AGENCY: United States NHLBI

GRANT: HL-56051

ACRONYM: HL

MEDLINETA: Biochemistry

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