Expression of Two Alternative Splice Forms of the Insulin-Like Growth Factor-l Gene in Human Vascular Endothelial Cells

1993 ◽  
Vol 30 (2) ◽  
pp. 121-124 ◽  
Author(s):  
Heather Glazebrook ◽  
Nicholas P.J. Bundle
Keyword(s):  
Endothelial Cells ◽  
Growth Factor ◽  
Alternative Splice ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Insulin Like Growth Factor ◽  
Splice Forms

scholarly journals Synthesis and physiological activity of heterodimers comprising different splice forms of vascular endothelial growth factor and placenta growth factor

1996 ◽  
Vol 316 (3) ◽  
pp. 703-707 ◽  
Author(s):  
Ralf BIRKENHÄGER ◽  
Bernard SCHNEPPE ◽  
Wolfgang RÖCKL ◽  
Jörg WILTING ◽  
Herbert A. WEICH ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Growth Factor ◽  
Vascular Endothelial Cells ◽  
Physiological Activity ◽  
Expression System ◽  
Vascular Endothelial ◽  
Placenta Growth Factor ◽  
Splice Forms

Vascular endothilial growth factor (VEGF) and placenta growth factor (PIGF) are members of a dimeric-growth-factor family with angiogenic properties. VEGF is a highly potent and specific mitogen for endothelial cells, playing a vital role in angiogenesis in vivo. The role of PIGF is less clear. We expressed the monomeric splice forms VEGF-165, VEGF-121, PIGF-1 and PlGF-2 as unfused genes in Escherichia coli using the pCYTEXP expression system. In vitro dimerization experiments revealed that both homo- and hetero-dimers can be formed from these monomeric proteins. The dimers were tested for their ability to promote capillary growth in vivo and stimulate DNA synthesis in cultured human vascular endothelial cells. Heterodimers comprising different VEGF splice forms, or combinations of VEGF/PlGF splice forms, showed mitogenic activity. The results demonstrate that four different heterodimeric growth factors are likely to have as yet uncharacterized functions in vivo.

IGFBP-3 binding to endothelial cells inhibits plasmin and thrombin proteolysis

2002 ◽  
Vol 282 (1) ◽  
pp. E52-E58 ◽  
Author(s):  
B. A. Booth ◽  
M. Boes ◽  
B. L. Dake ◽  
K. L. Knudtson ◽  
R. S. Bar
Keyword(s):  
Endothelial Cells ◽  
Growth Factor ◽  
Vascular Endothelial Cells ◽  
Binding Protein ◽  
Vascular Endothelial ◽  
Insulin Like Growth Factor ◽  
Heparin Binding ◽  
Binding Region ◽  
Factor Binding ◽  
Igfbp 3

Insulin-like growth factor-binding protein (IGFBP)-3 contains a highly basic COOH-terminal heparin-binding region, the P3 region, which is thought to be important in the binding of IGFBP-3 to endothelial cells. IGFBP-3 and IGFBP-4, and their chimeras IGFBP-34 and IGFBP-43, were treated with plasmin and with thrombin, proteases known to cleave IGFBP-3. IGFBP-3 was highly susceptible to plasmin, whereas IGFBP-4 was less so. Substitution of the P3 region for the P4 region in IGFBP-4 (IGFBP-43) increased the ability of the protease to digest IGFBP-43; substitution of the P4 region for the P3 region in IGFBP-3 (IGFBP-34) decreased the digestion of IGFBP-34. When 125I-labeled IGFBP-3 or125I-IGFBP-43 was first bound to vascular endothelial cells, subsequent proteolysis by either plasmin or thrombin was substantially inhibited. Proteolysis of125I-IGFBP-34 was not inhibited in the presence of endothelial cells. The P3 peptide was cleaved by plasmin but not by thrombin. We conclude that the P3 region is central to proteolysis of IGFBP-3 by plasmin and thrombin, processes which were inhibited by association of IGFBP-3 with endothelial cells.

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