Visualization of purified fibronectin-transglutaminase complexes.
نویسندگان
چکیده
منابع مشابه
Small Molecule Inhibitors Target the Tissue Transglutaminase and Fibronectin Interaction
Tissue transglutaminase (TG2) mediates protein crosslinking through generation of ε-(γ-glutamyl) lysine isopeptide bonds and promotes cell adhesion through interaction with fibronectin (FN) and integrins. Cell adhesion to the peritoneal matrix regulated by TG2 facilitates ovarian cancer dissemination. Therefore, disruption of the TG2-FN complex by small molecules may inhibit cell adhesion and m...
متن کاملTissue Transglutaminase Is an Integrin-Binding Adhesion Coreceptor for Fibronectin
The protein cross-linking enzyme tissue transglutaminase binds in vitro with high affinity to fibronectin via its 42-kD gelatin-binding domain. Here we report that cell surface transglutaminase mediates adhesion and spreading of cells on the 42-kD fibronectin fragment, which lacks integrin-binding motifs. Overexpression of tissue transglutaminase increases its amount on the cell surface, enhanc...
متن کاملFibronectin and immune complexes in rheumatic diseases.
The relation between fibronectin and immune complexes in rheumatic disease was examined in a series of linked studies. Fibronectin was present in immune complexes formed in vitro in the absence of C1q. Gel filtration chromatography showed complexed fibronectin was present in the serum of a patient with rheumatoid vasculitis, but not in normal serum; the complexed fibronectin coeluted with IgA a...
متن کاملFibronectin is a component of the sodium dodecyl sulfate-insoluble transglutaminase substrate.
Liver plasma membranes contain a morphologically distinct protein complex which serves as a substrate for the plasma membrane-associated transglutaminase. The complex, which appears as a two-dimensional sheet, is insoluble in sodium dodecyl sulfate and reducing agents and has been named SITS for sodium dodecyl sulfate-insoluble transglutaminase substrate (Tyrrell, D. J., Sale, W. S., and Slife,...
متن کاملDissociation of fibrinogen and fibronectin binding from transglutaminase-mediated cross-linking at the hepatocyte surface.
The interaction of fibrinogen and fibronectin with hepatocytes has been dissociated into distinct binding and cross-linking steps. Binding and cross-linking of 125I-labeled ligands were both decreased by transglutaminase inhibitors, but not by heparin or hirudin. Transglutaminase activity was manifest by Ca2+-dependent incorporation of [14C]putrescine into cells. Preferential cross-linking of f...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1992
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)42595-1