MMP9 processing of HSPB1 regulates tumor progression

Matrix metalloproteinases regulate pathophysiological events by processing matrix proteins and secreted proteins. Previously, we demonstrated that soluble heat shock protein B1 (HSPB1) is released primarily from endothelial cells (ECs) and regulates angiogenesis via direct interaction with vascular...

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Veröffentlicht in:	PloS one 2014-01, Vol.9 (1), p.e85509
Hauptverfasser:	Choi, Seo-hyun, Lee, Hae-June, Jin, Yeung Bae, Jang, Junho, Kang, Ga-young, Lee, Minyoung, Kim, Chun-Ho, Kim, Joon, Yoon, Sam S, Lee, Yun-sil, Lee, Yoon-Jin
Format:	Artikel
Sprache:	eng
Schlagworte:	Activation Adenocarcinoma - genetics Adenocarcinoma - metabolism Adenocarcinoma - pathology Amino acids Angiogenesis Animals Apoptosis Atherosclerosis Biology Cancer Cancer therapies Carcinogenesis - genetics Carcinogenesis - metabolism Carcinogenesis - pathology Cell Movement Cell Proliferation Cleavage Clinical trials Colon Colorectal cancer Development and progression Disease Progression Endothelial cells Endothelial Cells - metabolism Endothelium Fragmentation Fragments Gelatinase B Heat shock proteins Hostages HSP27 Heat-Shock Proteins - genetics HSP27 Heat-Shock Proteins - metabolism Humans Inhibitors Laboratories Life sciences Liver Lung cancer Lung Neoplasms - genetics Lung Neoplasms - metabolism Lung Neoplasms - pathology Lungs Matrix Metalloproteinase 9 - genetics Matrix Metalloproteinase 9 - metabolism Matrix metalloproteinases Medical prognosis Medical research Medicine Melanoma Metastasis Mice Pharmaceutical sciences Pharmacy Phosphorylation Physiological aspects Proteins Receptors, Vascular Endothelial Growth Factor - genetics Receptors, Vascular Endothelial Growth Factor - metabolism Rodents Sarcoma - genetics Sarcoma - metabolism Sarcoma - pathology Secretion Soft Tissue Neoplasms - genetics Soft Tissue Neoplasms - metabolism Soft Tissue Neoplasms - pathology Vascular endothelial growth factor
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