Fibroblast Activation Protein Peptide Substrates Identified from Human Collagen I Derived Gelatin Cleavage Sites
نویسندگان
چکیده
منابع مشابه
Cleavage of Type I Collagen by Fibroblast Activation Protein-α Enhances Class A Scavenger Receptor Mediated Macrophage Adhesion
Pathophysiological conditions such as fibrosis, inflammation, and tumor progression are associated with modification of the extracellular matrix (ECM). These modifications create ligands that differentially interact with cells to promote responses that drive pathological processes. Within the tumor stroma, fibroblasts are activated and increase the expression of type I collagen. In addition, ac...
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AIMS Collagen degradation in atherosclerotic plaques with thin fibrous caps renders them more prone to rupture. Fibroblast activation protein (FAP) plays a role in arthritis and tumour formation through its collagenase activity. However, the significance of FAP in thin-cap human fibroatheromata remains unknown. METHODS AND RESULTS We detected enhanced FAP expression in type IV-V human aortic ...
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Gelatin and collagen were used to produce the scaffold for fibroblast cell culture. The properties of scaffolds obtained from type A and type B gelatin were compared to scaffold obtained from collagen, which is widely used in skin substitute. Porous scaffolds were prepared by freeze drying and dehydrothermal (DHT) crosslinking method. DHT treatment time was performed at 24 and 48 h and the degr...
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A synthetic peptide-1, an 18 amino acid residue peptide derived from a hydrophilic domain of a cloned platelet type I collagen receptor, was used to study the role of the receptor on types I and III collagen-induced platelet aggregation and the release of ATP. The peptide inhibits the type I, but not the type III, collagen-induced platelet aggregation and the release of ATP in a dose-dependent ...
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The ability of purified human neutrophil elastase (EC 3.4.21.37) to cleave native type I collagen has been investigated. Soluble human, bovine or rat type I collagen was incubated with neutrophil elastase for 16 h at 25 degrees C before catalysis was stopped with 3, 4-dichloroisocoumarin. Analysis by SDS/PAGE of the collagen digests revealed 3/4-length fragments similar in size to those produce...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 2007
ISSN: 0006-2960,1520-4995
DOI: 10.1021/bi701921b