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10.1111/j.1349-7006.1996.tb00202.x http://scihub22266oqcxt.onion/10.1111/j.1349-7006.1996.tb00202.x C5920984!5920984 !8609052     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=8609052 &cmd=llinks): Failed to open stream: HTTP request failed! 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Heparin-binding epidermal growth factor-like growth factor: p91 activation induction of plasminogen activator/inhibitor, and tubular morphogenesis in human microvascular endothelial cells |pdf=|usr=}}{{8609052 }} gab.com Text Heparin-binding epidermal growth factor-like growth factor: p91 activation induction of plasminogen activator/inhibitor, and tubular morphogenesis in human microvascular endothelial cells JO: Jpn J Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=8609052 #FOAvip Epidermal growth factor (EGF) or transforming growth factor-alpha (TGF-alpha) stimulates cell migration, proliferation and the formation of tube-like structures of human microvascular endothelial cells in culture. Heparin-binding EGF-like growth factor(HB-EGF), which shows 35% homology with EGF/TGF-alpha, is a member of the EGF family, and it is ubiquitous in many tissues and organs. We examined whether or not HB-EGF induced angiogenic responses in human microvascular endothelial cells. HB-EGF inhibited the binding of (125) I-EGF to the EGF receptor and induced autophosphorylation of the receptor on endothelial cells. Exogenous HB-EGF induced the loss of more than 70% of the EGF receptor from the cell surface within 30 min, with similar kinetics to that of EGF. The level of c-fos mRNA markedly increased at 30 min in response to HB-EGF as well as EGF. A gel shift assay demonstrated the activation of the transcription factor p91 by HB-EGF and EGF. This factor directly interacts with EGF receptor and mediates the activation of c-fos gene promoter. HB-EGF enhanced the mRNA expression of tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor-1 (PAI-1) mRNA. However, the enhancement of t-PA and PAI-1 by HB-EGF was less than that by EGF. Heparitinase/chlorate, which digests the heparan sulfate proteoglycan of the endothelial cell surface, restored both t-PA and PAI-1 mRNA levels in response to HB-EGF in a manner similar to that by EGF. HB-EGF at 10 ng/ml developed tube-like structures in type I collagen gel at similar levels to that of EGF at 10 ng/ml, suggesting that HB-EGF is also a potent angiogenic factor in the model system for angiogenesis. The tubulogenesis activity of HB-EGF is discussed in relation to the expression of the t-PA and PAI-1 genes. Twit Text FOAVip Heparin-binding epidermal growth factor-like growth factor: p91 activation induction of plasminogen activator/inhibitor, and tubular morphogenesis in human microvascular endothelial cells ????Jpn J Cancer Res http://www.kidney.de/pget.php?&tw=1&pmid=8609052 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=8609052 #FOAvip English Wikipedia <ref>{{Cite pmid|8609052 }}</ref> Heparin-binding epidermal growth factor-like growth factor: p91 activation induction of plasminogen activator/inhibitor, and tubular morphogenesis in human microvascular endothelial cells #MMPMID8609052 Ushiro S ; Ono M ; Izumi H ; Kohno K ; Taniguchi N ; Higashiyama S ; Kuwano M Jpn J Cancer Res 1996[Jan]; 87 (1 ): 68-77 PMID8609052 show ga Epidermal growth factor (EGF) or transforming growth factor-alpha (TGF-alpha) stimulates cell migration, proliferation and the formation of tube-like structures of human microvascular endothelial cells in culture. Heparin-binding EGF-like growth factor(HB-EGF), which shows 35% homology with EGF/TGF-alpha, is a member of the EGF family, and it is ubiquitous in many tissues and organs. We examined whether or not HB-EGF induced angiogenic responses in human microvascular endothelial cells. HB-EGF inhibited the binding of (125) I-EGF to the EGF receptor and induced autophosphorylation of the receptor on endothelial cells. Exogenous HB-EGF induced the loss of more than 70% of the EGF receptor from the cell surface within 30 min, with similar kinetics to that of EGF. The level of c-fos mRNA markedly increased at 30 min in response to HB-EGF as well as EGF. A gel shift assay demonstrated the activation of the transcription factor p91 by HB-EGF and EGF. This factor directly interacts with EGF receptor and mediates the activation of c-fos gene promoter. HB-EGF enhanced the mRNA expression of tissue-type plasminogen activator (t-PA) and plasminogen activator inhibitor-1 (PAI-1) mRNA. However, the enhancement of t-PA and PAI-1 by HB-EGF was less than that by EGF. Heparitinase/chlorate, which digests the heparan sulfate proteoglycan of the endothelial cell surface, restored both t-PA and PAI-1 mRNA levels in response to HB-EGF in a manner similar to that by EGF. HB-EGF at 10 ng/ml developed tube-like structures in type I collagen gel at similar levels to that of EGF at 10 ng/ml, suggesting that HB-EGF is also a potent angiogenic factor in the model system for angiogenesis. The tubulogenesis activity of HB-EGF is discussed in relation to the expression of the t-PA and PAI-1 genes. |Base Sequence [MESH] |Cells, Cultured [MESH] |DNA-Binding Proteins/*physiology [MESH] |Down-Regulation [MESH] |Endothelium, Vascular/*drug effects/metabolism/*ultrastructure [MESH] |Epidermal Growth Factor/metabolism/*pharmacology [MESH] |ErbB Receptors/metabolism [MESH] |Gene Expression Regulation [MESH] |Gene Expression/drug effects [MESH] |Genes, fos [MESH] |Heparin-binding EGF-like Growth Factor [MESH] |Humans [MESH] |Intercellular Signaling Peptides and Proteins [MESH] |Iodine Radioisotopes [MESH] |Microtubules/*drug effects/*metabolism [MESH] |Molecular Sequence Data [MESH] |Neovascularization, Physiologic/drug effects [MESH] |Plasminogen Activator Inhibitor 1/*biosynthesis [MESH] |STAT1 Transcription Factor [MESH] |Tissue Plasminogen Activator/*biosynthesis [MESH]Heparin-binding epidermal growth factor-like growth factor: p91 activa(epmc).pdf DeepDyve Pubget Overpricing