نتایج جستجو برای: vegf receptor 2

تعداد نتایج: 2961377  

Journal: :The American journal of pathology 2002
Samuel Joseph Leibovich Jiang-Fan Chen Grace Pinhal-Enfield Paula C Belem Genie Elson Anthony Rosania Madhuri Ramanathan Carmen Montesinos Marlene Jacobson Michael A Schwarzschild J Stephen Fink Bruce Cronstein

Under normoxic conditions, macrophages from C57BL mice produce low levels of vascular endothelial growth factor (VEGF). Hypoxia stimulates VEGF expression by approximately 500%; interferon-gamma (IFN-gamma) with endotoxin [lipopolysaccharide (LPS)] also stimulates VEGF expression by approximately 50 to 150% in an inducible nitric oxide synthase (iNOS)-dependent manner. Treatment of normoxic mac...

Journal: :Biology 2021

Specific proteolytic cleavages turn on, modify, or off the activity of vascular endothelial growth factors (VEGFs). Proteolysis is most prominent among lymph­angiogenic VEGF-C and VEGF-D, which are synthesized as precursors that need to undergo enzymatic removal their C- N-terminal propeptides before they can activate receptors. At least five different proteases mediate activating cleavage VEGF...

Journal: :Blood 2005
Margherita Gallicchio Stefania Mitola Donatella Valdembri Roberto Fantozzi Brian Varnum Gian Carlo Avanzi Federico Bussolino

GAS6, the product of a growth arrest specific (GAS) gene, is the ligand of the tyrosine kinase receptor Axl. GAS6 and Axl are both expressed in endothelial cells, where they are involved in many processes such as leukocyte transmigration through capillaries and neointima formation in injured vessels. Here, we show that Axl stimulation by GAS6 results in inhibition of the ligand-dependent activa...

Journal: :Circulation research 2007
Salla Keskitalo Tuomas Tammela Johannes Lyytikka Terhi Karpanen Michael Jeltsch Johanna Markkanen Seppo Yla-Herttuala Kari Alitalo

Vascular endothelial growth factor (VEGF)-C and VEGF-D require proteolytic cleavage of the carboxy terminal silk-homology domain for activation. To study the functions of the VEGF-C propeptides, we engineered a chimeric growth factor protein, VEGF-CAC, composed of the amino- and carboxy-terminal propeptides of VEGF-C fused to the receptor-activating core domain of VEGF. Like VEGF-C, VEGF-CAC un...

2010
Laura A. Sullivan Juliet G. Carbon Christina L. Roland Jason E. Toombs Mari Nyquist-Andersen Anita Kavlie Kyle Schlunegger James A. Richardson Rolf A. Brekken

Vascular endothelial growth factor (VEGF) is critical for physiological and pathological angiogenesis. Within the tumor microenvironment, VEGF functions as an endothelial cell survival factor, permeability factor, mitogen, and chemotactic agent. The majority of these functions are mediated by VEGF-induced activation of VEGF receptor 2 (VEGFR2), a high affinity receptor tyrosine kinase expressed...

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