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Structure, Stability, And Interaction Of Fibrin αC-domain Polymers.
G. Tsurupa, Ariza Mahid, Y. Veklich, J. Weisel, L. Medved
Published 2011 · Chemistry, Medicine
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Our previous studies revealed that in fibrinogen the αC-domains are not reactive with their ligands, suggesting that their binding sites are cryptic and become exposed upon its conversion to fibrin, in which these domains form αC polymers. On the basis of this finding, we hypothesized that polymerization of the αC-domains in fibrin results in the exposure of their binding sites and that these domains adopt the physiologically active conformation only in αC-domain polymers. To test this hypothesis, we prepared a recombinant αC region (residues Aα221-610) including the αC-domain (Aα392-610), demonstrated that it forms soluble oligomers in a concentration-dependent and reversible manner, and stabilized such oligomers by covalently cross-linking them with factor XIIIa. Cross-linked Aα221-610 oligomers were stable in solution and appeared as ordered linear, branching filaments when analyzed by electron microscopy. Spectral studies revealed that the αC-domains in such oligomers were folded into compact structures of high thermal stability with a significant amount of β-sheets. These findings indicate that cross-linked Aα221-610 oligomers are highly ordered and mimic the structure of fibrin αC polymers. The oligomers also exhibited functional properties of polymeric fibrin because, in contrast to the monomeric αC-domain, they bound tPA and plasminogen and stimulated activation of the latter by the former. Altogether, the results obtained with cross-linked Aα221-610 oligomers clarify the structure of the αC-domains in fibrin αC polymers and confirm our hypothesis that their binding sites are exposed upon polymerization. Such oligomers represent a stable, soluble model of fibrin αC polymers that can be used for further structure-function studies of fibrin αC-domains.
This paper references
The structure and function of the αCdomains of fibrinogen
J. Weisel (2001)
The Structure and Biological Features of Fibrinogen and Fibrin
M. Mosesson (2001)
Fibrinogen, fibrin and factor XIII. in Blood Coagulation (Zwaal
A. Henschen (1986)
Noncovalent interaction of alpha(2)-antiplasmin with fibrin(ogen): localization of alpha(2)-antiplasmin-binding sites.
G. Tsurupa (2010)
Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites.
B. Cottrell (1979)
Do the isolated fibrinogen αC-domains form ordered oligomers?
G. Tsurupa (2004)
Clotting of fibrinogen. 2. Calorimetry of the reversal of the effect of calcium on clotting with thrombin and with ancrod.
E. Mihályi (1985)
A simple, sensitive spectrophotometric assay for extrinsic (tissue-type) plasminogen activator applicable to measurements in plasma.
J. Verheijen (1982)
Recognition of Fibrinogen by Leukocyte Integrins
T. Ugarova (2001)
CRYSTAL STRUCTURE OF FIBRINOGEN FRAGMENT D
G. Spraggon (1997)
Structure, stability, and interaction of the fibrin(ogen) alphaC-domains.
G. Tsurupa (2009)
Carboxyl-terminal portions of the _ chains of fibrinogen and fibrin
Y. Veklich (1993)
Role of the alpha C domains of fibrin in clot formation.
O. Gorkun (1994)
Alpha-chain domain of fibrinogen controls generation of fibrinoligase (coagulation factor XIIIa). Calcium ion regulatory aspects.
R. B. Credo (1981)
Interaction of fibrin(ogen) with fibronectin: further characterization and localization of the fibronectin-binding site.
E. Makogonenko (2002)
ELECTRON MICROSCOPY OF FIBRINOGEN, ITS PLASMIC FRAGMENTS AND SMALL POLYMERS *
H. Erickson (1983)
The amino acid sequence of the α-chain of human fibrinogen
R. Doolittle (1979)
The plasminogen (fibrinolytic) system.
D. Collen (1999)
Comparative structural and functional features of the human fibrinogen alpha C domain and the isolated alpha C fragment. Characterization using monoclonal antibodies to defined COOH-terminal A alpha chain regions.
S. Rudchenko (1996)
Domain structure and functional activity of the recombinant human fibrinogen gamma-module (gamma148-411).
L. Medved (1997)
ORIENTATION OF FIBRIN IN STRONG MAGNETIC FIELDS
G. Hudry-Clergeon (1983)
Crystal Structure Studies on Fibrinogen and Fibrin
R. Doolittle (2001)
The role of fibrinogen αC‐domains in the fibrin assembly process
L. Medved (1985)
Direct evidence for specific interactions of the fibrinogen alphaC-domains with the central E region and with each other.
R. Litvinov (2007)
Domains in the fibrinogen molecule.
P. Privalov (1982)
Molecular weight fibrinogen variants determine angiogenesis rate in a fibrin matrix in vitro and in vivo
E. Kaijzel (2006)
A model for fibrinogen: domains and sequence.
J. Weisel (1985)
Interaction of fibrin(ogen) with the endothelial cell receptor VE-cadherin: mapping of the receptor-binding site in the NH2-terminal portions of the fibrin beta chains.
Sergei Gorlatov (2002)
Localization of a cross-link donor site in the α-chain of human fibrin
D. Corcoran (1980)
Conformational Changes upon Conversion of Fibrinogen into Fibrin
L. Medved (2001)
The Fibrinogen Molecule: Its Size, Shape, and Mode of Polymerization
C. E. Hall (1959)
A comparative study of crosslinked and noncrosslinked fibrin from the major classes of vertebrates.
M. Schwartz (1973)
Crystal structure of native chicken fibrinogen at 2.7 A resolution.
Z. Yang (2001)
Hereditary renal amyloidosis associated with a mutant fibrinogen α–chain
M. Benson (1993)
Dysfibrinogenemia (fibrinogen Dusard) associated with impaired fibrin-enhanced plasminogen activation.
H. R. Lijnen (1984)
Early events in the plasmin digestion of fibrinogen and fibrin. Effects of plasmin on fibrin polymerization.
L. L. Shen (1977)
Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen.
V. Yee (1997)
Covalent Cross-linking of Fibronectin to Fibrin Is Required for Maximal Cell Adhesion to a Fibronectin-Fibrin Matrix*
S. Corbett (1997)
Involvement of the COOH-terminal portion of the alpha-chain of fibrin in the branching of fibers to form a clot.
J. Weisel (1987)
Calculation of protein conformation from circular dichroism.
J. Yang (1986)
Polymerization properties of two normally circulating fibrinogens, HMW and LMW. Evidence that the COOH-terminal end of the a-chain is of importance for fibrin polymerization.
B. Holm (1985)
Hereditary renal amyloidosis with a novel variant fibrinogen.
T. Uemichi (1994)
Interaction of Fibrin with VE‐Cadherin
J. Martínez (2001)
Identification and Characterization of Novel Lysine-independent Apolipoprotein(a)-binding Sites in Fibrin(ogen) αC-domains*
G. Tsurupa (2003)
Structural aspects of the fibrinogen to fibrin conversion.
R. Doolittle (1973)
The crystal structure of modified bovine fibrinogen.
J. Brown (2000)
Nonclottable fibrin obtained from partially reduced fibrinogen: characterization and tissue plasminogen activator stimulation.
R. Procyk (1992)
Carboxyl-terminal portions of the alpha chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated alpha C fragments on polymerization.
Y. Veklich (1993)
Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids A alpha 461-610 (Lys 461 AAA-->stop TAA).
J. Koopman (1992)
Mechanics of Motor Proteins and the Cytoskeleton
J. Howard (2001)
Natively unfolded regions of the vertebrate fibrinogen molecule
R. Doolittle (2006)
Crystal structure of the complex between thrombin and the central "E" region of fibrin.
I. Pechik (2004)
The effect of plasmin on the subunit structure of human fibrinogen.
S. Pizzo (1972)
Renal amyloidosis with a frame shift mutation in fibrinogen aalpha-chain gene producing a novel amyloid protein.
L. Hamidi Asl (1997)
Review of some unusual effects of calcium binding to fibrinogen.
Elemer Mihalyi (2004)
Recognition of distinct adhesive sites on fibrinogen by related integrins on platelets and endothelial cells
D. Cheresh (1989)
Transglutaminase-mediated oligomerization of the fibrin(ogen) alphaC domains promotes integrin-dependent cell adhesion and signaling.
A. Belkin (2005)
Fibrinogen and fibrin.
R. Doolittle (1981)
Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin.
P. McKee (1970)
Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-Å resolution
J. Madrazo (2001)
The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis.
J. Collet (2005)
Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) alpha C-domains.
G. Tsurupa (2001)
Molecular mechanisms of initiation of fibrinolysis by fibrin.
L. Medved (2003)
Laser Raman spectroscopy study of bovine fibrinogen and fibrin.
J. Marx (1979)
NMR Solution Structure, Stability, and Interaction of the Recombinant Bovine Fibrinogen alphaC-Domain Fragment
R. A. Burton (2007)
A frame shift mutation in the fibrinogen A alpha chain gene in a kindred with renal amyloidosis.
T. Uemichi (1996)
The Structure and Function of the αC Domains of Fibrinogen
J. Weisel (2001)
Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR.
R. A. Burton (2006)
Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia.
J. Koopman (1993)
Crystal structure of human fibrinogen.
J. Kollman (2009)
Fibrin and Wound Healing
R. A. Clark (2001)
Recommendations for nomenclature on fibrinogen and fibrin
L. Medved (2009)
Factor XIIIa-catalyzed cross-linking of recombinant alpha C fragments of human fibrinogen.
Y. Matsuka (1996)
Structural organization of C‐terminal parts of fibrinogen Aα‐chains
L. Medved (1983)
Structural Organization of the Fibrin(ogen) αC-Domain†
G. Tsurupa (2002)
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Characterization of Anopheles gambiae Transglutaminase 3 (AgTG3) and Its Native Substrate Plugin*
B. V. Le (2013)
Atomic Structural Models of Fibrin Oligomers.
A. Zhmurov (2018)
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Sarah K Westbury (2013)
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Marcos Moradas Estrada (2018)
Fibrin clot structure and mechanics associated with specific oxidation of methionine residues in fibrinogen.
Katie M. Weigandt (2012)
Age-Dependent Differential Staining of Fibrin in Blood Clots and Thrombi
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Le dosage des monomères de fibrine : étude in vitro, et intérêt en traumatologie
Laurent Weinmann (2016)
Occurrence of fibronectin–fibrin complexes in plasma of patients with multimorbidity due to the inflamm-aging phenomenon
M. Pupek (2016)
Heterozygous FGA p.Asp473Ter (fibrinogen Nieuwegein) presenting as antepartum cerebral thrombosis.
Mercedeh Tajdar (2018)
Roles of serum fibrinogen α chain‐derived peptides in Alzheimer's disease
Miwa Noguchi (2014)
Fibrinogen Dusart presenting as recurrent thromboses in the hepatic portal system.
Y. Shen (2014)
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P. Burney (2014)
Differences in the function and secretion of congenital aberrant fibrinogenemia between heterozygous γD320G (Okayama II) and γΔN319-ΔD320 (Otsu I).
Saki Mukai (2015)
Identification of respective lysine donor and glutamine acceptor sites involved in factor XIIIa-catalyzed fibrin α chain cross-linking.
W. Wang (2011)
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