Hierarchies in the binding of human factor XIII, factor XIIIa, and endothelial cell transglutaminase to human plasma fibrinogen, fibrin, and fibronectin (Q28295860)

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English	Hierarchies in the binding of human factor XIII, factor XIIIa, and endothelial cell transglutaminase to human plasma fibrinogen, fibrin, and fibronectin	scientific article

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scholarly article

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Hierarchies in the binding of human factor XIII, factor XIIIa, and endothelial cell transglutaminase to human plasma fibrinogen, fibrin, and fibronectin (English)

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author name string

K E Achyuthan

1

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T C Rowland

2

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P J Birckbichler

3

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K N Lee

4

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P D Bishop

5

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A M Achyuthan

6

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language of work or name

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publication date

6 September 1996

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Molecular and Cellular Biochemistry

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162

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1

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43-9

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A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase

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Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers

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https://pubmed.ncbi.nlm.nih.gov/8905624

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Transglutaminases catalyze cross-linking of plasminogen to fibronectin and human endothelial cells

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Immunoelectrophoretic and immunohistochemical characterizations of fibrinogen derivatives in atherosclerotic aortic intimas and vascular prosthesis pseudo-intimas

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Factor XIII-induced crosslinking in solutions of fibrinogen and fibronectin

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Localization of cellular transglutaminase on the extracellular matrix after wounding: characteristics of the matrix bound enzyme

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The N epsilon-(gamma-glutamic)lysine cross-link: method of analysis, occurrence in extracellular and cellular proteins

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The transglutaminase in vascular cells and tissues could provide an alternate pathway for fibrin stabilization.

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https://pubmed.ncbi.nlm.nih.gov/8905624

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b-chains prevent the proteolytic inactivation of the a-chains of plasma factor XIII

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The binding sites on fibrin(ogen) for guinea pig liver transglutaminase are similar to those of blood coagulation factor XIII. Characterization of the binding of liver transglutaminase to fibrin

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Transglutaminase stabilizes melanoma adhesion under laminar flow

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The zymogen forms of blood coagulation factor XIII bind specifically to fibrinogen.

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Binding and degradation of blood coagulation factor XIII by cultured fibroblasts

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Studies on the mechanism of thrombin. Interaction with fibrin

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Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor

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The fibronectin-binding domain of transglutaminase

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Interactions of factor XIII with fibrin as substrate and cofactor

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Characterization of the kinetic pathway for fibrin promotion of alpha-thrombin-catalyzed activation of plasma factor XIII

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Cellular transglutaminase, growth, and transformation

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A microtiter plate assay for factor XIII A-chain-fibrin interactions.

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Immunochemical analyses of human plasma fibronectin-cytosolic transglutaminase interactions

1 reference

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Fibronectin. Effect of disulfide bond reduction on its physical and functional properties

1 reference

https://pubmed.ncbi.nlm.nih.gov/8905624

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Factor XIIIa formation promoted by complexing of alpha-thrombin, fibrin, and plasma factor XIII

1 reference

https://pubmed.ncbi.nlm.nih.gov/8905624

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Transglutaminases: multifunctional cross‐linking enzymes that stabilize tissues

1 reference

https://pubmed.ncbi.nlm.nih.gov/8905624

12 December 2020

based on heuristic

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Increase in epsilon(gamma-glutamyl)lysine crosslinks in atherosclerotic aortas

1 reference

https://pubmed.ncbi.nlm.nih.gov/8905624

12 December 2020

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Visualization of purified fibronectin-transglutaminase complexes

1 reference

https://pubmed.ncbi.nlm.nih.gov/8905624

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. Use of 2-[(2-oxopropyl)thio] imidazolium derivatives as cellular

1 reference

https://pubmed.ncbi.nlm.nih.gov/8905624

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inferred from PubMed ID database lookup

Identifiers

10.1007/BF00250994

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Springer Nature article ID

10.1007/bf00250994

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