Linked Life Data

12070119

Source:http://linkedlifedata.com/resource/pubmed/id/12070119

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2002-6-18
pubmed:abstractText
BACKGROUND: Vascular smooth muscle cell proliferation plays an important role in the development of atherosclerosis. We previously reported that adiponectin, an adipocyte-specific plasma protein, accumulated in the human injured artery and suppressed endothelial inflammatory response as well as macrophage-to-foam cell transformation. The present study investigated the effects of adiponectin on proliferation and migration of human aortic smooth muscle cells (HASMCs). Methods and Results- HASMC proliferation was estimated by [(3)H] thymidine uptake and cell number. Cell migration assay was performed using a Boyden chamber. Physiological concentrations of adiponectin significantly suppressed both proliferation and migration of HASMCs stimulated with platelet-derived growth factor (PDGF)-BB. Adiponectin specifically bound to (125)I-PDGF-BB and significantly inhibited the association of (125)I-PDGF-BB with HASMCs, but no effects were observed on the binding of (125)I-PDGF-AA or (125)I-heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) to HASMCs. Adiponectin strongly and dose-dependently suppressed PDGF-BB-induced p42/44 extracellular signal-related kinase (ERK) phosphorylation and PDGF beta-receptor autophosphorylation analyzed by immunoblot. Adiponectin also reduced PDGF-AA-stimulated or HB-EGF-stimulated ERK phosphorylation in a dose-dependent manner without affecting autophosphorylation of PDGF alpha-receptor or EGF receptor. CONCLUSIONS: The adipocyte-derived plasma protein adiponectin strongly suppressed HASMC proliferation and migration through direct binding with PDGF-BB and generally inhibited growth factor-stimulated ERK signal in HASMCs, suggesting that adiponectin acts as a modulator for vascular remodeling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1524-4539
pubmed:author
pubmed:issnType
Electronic
pubmed:day
18
pubmed:volume
105
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2893-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12070119-Adipocytes, pubmed-meshheading:12070119-Adiponectin, pubmed-meshheading:12070119-Aorta, pubmed-meshheading:12070119-Blood Proteins, pubmed-meshheading:12070119-Cell Division, pubmed-meshheading:12070119-Cell Movement, pubmed-meshheading:12070119-Cells, Cultured, pubmed-meshheading:12070119-Dose-Response Relationship, Drug, pubmed-meshheading:12070119-Growth Inhibitors, pubmed-meshheading:12070119-Growth Substances, pubmed-meshheading:12070119-Humans, pubmed-meshheading:12070119-Intercellular Signaling Peptides and Proteins, pubmed-meshheading:12070119-Mitogen-Activated Protein Kinases, pubmed-meshheading:12070119-Muscle, Smooth, Vascular, pubmed-meshheading:12070119-Phosphorylation, pubmed-meshheading:12070119-Platelet-Derived Growth Factor, pubmed-meshheading:12070119-Proteins, pubmed-meshheading:12070119-Receptors, Growth Factor, pubmed-meshheading:12070119-Signal Transduction
pubmed:year
2002
pubmed:articleTitle
Adipocyte-derived plasma protein adiponectin acts as a platelet-derived growth factor-BB-binding protein and regulates growth factor-induced common postreceptor signal in vascular smooth muscle cell.
pubmed:affiliation
Department of Internal Medicine and Molecular Science, Graduate School of Medicine, Osaka University, Osaka and First Institute of New Drug Research, Otsuka Pharmaceutical Co, Ltd, Tokushima, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't