Growth factors: Difference between revisions
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*[[Vascular Endothelial Growth Factor]] and [[Vascular Endothelial Growth Factor Receptor]] (VEGFR). VEGFR belongs to [[Receptor tyrosine kinases]], class IV. | *[[Vascular Endothelial Growth Factor]] and [[Vascular Endothelial Growth Factor Receptor]] (VEGFR). VEGFR belongs to [[Receptor tyrosine kinases]], class IV. | ||
<scene name='Vascular_Endothelial_Growth_Factor/Vegf-a_opening/1'>VEGF-A</scene> is a homodimer composed of two 23 kDa subunits. VEGF-A exists in a number of different isoforms following alternative splicing of its precursor mRNA <ref>PMID: 11181169</ref>. In humans, 6 variants have been found: VEGF-A-121, VEGF-A-145, VEGF-A-165, VEGF-A-183, VEGF-A-189, and VEGF-A-206, with VEGF-A-165 the most abundantly expressed. All VEGF-A isoforms bind to VEGFR-1 and -2. | |||
The amino acids determined to be <scene name='Vascular_Endothelial_Growth_Factor/Vegf-a_binding_to_vegfr1/2'>critical to binding to VEGFR-1</scene> are D63, L66, and E67. VEGF-A binding by VEGFR-1 leads to cellular proliferation, migration, and increased cellular permeability resulting in vasculogenesis and angiogenesis. Those residues <scene name='Vascular_Endothelial_Growth_Factor/Vegf-a_binding_to_vegfr2/2'>critical to binding to VEGFR-2</scene> are I43, I46, Q79, I83, K84 and P85.<ref>pmid:9207067</ref> Binding of VEGF-A to VEGFR-2 results in similar Vasculogenesis and angiogenesis, but also lymphangiogenesis in embryos. The remainder of the <scene name='Vascular_Endothelial_Growth_Factor/Vegf-a_full_binding_site/1'>binding pocket </scene> is formed by D34, S50, E64, and F36. It is upon binding of VEGFR by VEGF that the subsequent signal cascade is initiated leading to angiogenesis, etc.<ref>pmid:8621427</ref> | |||
*[[TGF-beta receptor|Transforming Growth Factor and its receptor]] | *[[TGF-beta receptor|Transforming Growth Factor and its receptor]] | ||