Results 151 to 160 of about 20,449 (205)
Albumin coatings for counteracting uremic metabolites effects on host responses to biomaterials. [PDF]
Front Bioeng BiotechnolSharma I +4 more
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Advancements in the <i>in vitro</i> culture of human pluripotent stem cells: progress, challenges, and future directions: comprehensive review. [PDF]
Front ToxicolChaudhary N, Villa-Diaz LG.
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The International Journal of Biochemistry & Cell Biology, 1999
Vitronectin is a multifunctional glycoprotein present in blood and in the extracellular matrix. It binds glycosaminoglycans, collagen, plasminogen and the urokinase-receptor, and also stabilizes the inhibitory conformation of plasminogen activation inhibitor-1.
I, Schvartz, D, Seger, S, Shaltiel
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Vitronectin is a multifunctional glycoprotein present in blood and in the extracellular matrix. It binds glycosaminoglycans, collagen, plasminogen and the urokinase-receptor, and also stabilizes the inhibitory conformation of plasminogen activation inhibitor-1.
I, Schvartz, D, Seger, S, Shaltiel
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Vitronectin in atherosclerotic disease
Clinica Chimica Acta, 2006Atherosclerosis is characterized by the development of an intimal thickening that contains monocytes, T lymphocytes, and smooth muscle cells within an accumulation of lipid and extracellular matrix proteins. Vitronectin is a plasma glycoprotein implicated as a regulator of diverse physiological process, including blood coagulation, fibrinolysis ...
Ozlem Balci, Ekmekçi, Hakan, Ekmekçi
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Vitronectin is a substrate for transglutaminases
Biochemical and Biophysical Research Communications, 1988Vitronectin (VN) was found to be a substrate for both plasma transglutaminase (Factor XIIIa) and guinea pig liver transglutaminase (TG). Incorporation of [3H]-putrescine indicated the presence of reactive glutaminyl residues in VN. When VN was incubated with TG or Factor XIIIa, in the absence of putrescine, multimeric covalent complexes were identified,
D C, Sane +5 more
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Current Opinion in Cell Biology, 1993
The extracellular matrix protein vitronectin is recognized as an adhesive substrate by cells expressing at least one of four known vitronectin receptors: integrins alpha v beta 1, alpha v beta 3, alpha v beta 5 or alpha IIb beta 3. Cell interaction with vitronectin may induce spreading and migration and have an effect on cell growth and differentiation
B, Felding-Habermann, D A, Cheresh
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The extracellular matrix protein vitronectin is recognized as an adhesive substrate by cells expressing at least one of four known vitronectin receptors: integrins alpha v beta 1, alpha v beta 3, alpha v beta 5 or alpha IIb beta 3. Cell interaction with vitronectin may induce spreading and migration and have an effect on cell growth and differentiation
B, Felding-Habermann, D A, Cheresh
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Vitronectin and Integrin Vitronectin Receptor Localization in Multiple Sclerosis Lesions
Journal of Neuropathology and Experimental Neurology, 1995Vitronectin (Vn) is a multifunctional plasma and extracellular matrix glycoprotein involved in cell attachment, coagulation, phagocytosis, and the protection of bystander cells from complement- and T cell-mediated lysis. To determine where Vn is localized and where cells expressing integrin Vn receptors may recognize it in central nervous system (CNS ...
R A, Sobel +3 more
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Current Protocols in Cell Biology, 1999
AbstractThis unit describes the purification of extracellular vitronectin from plasma by a series of affinity chromatography steps. First plasma is depleted of fibronectin and other heparin‐binding proteins; the sample is then treated with urea to activate the heparin‐binding activity of vitronectin. The resulting vitronectin is ∼98% pure.
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AbstractThis unit describes the purification of extracellular vitronectin from plasma by a series of affinity chromatography steps. First plasma is depleted of fibronectin and other heparin‐binding proteins; the sample is then treated with urea to activate the heparin‐binding activity of vitronectin. The resulting vitronectin is ∼98% pure.
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