Source:http://linkedlifedata.com/resource/pubmed/id/21121067
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2010-12-1
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pubmed:abstractText |
In this paper, we investigate the effect and the possible mechanism of high glucose levels on the calcification of human aortic smooth muscle cells (HASMCs). HASMCs were divided into four groups: normal glucose group (NG), osmolality control group (OC), high glucose group (HG, HASMCs culture medium containing 30 mmol/L glucose), and high glucose plus recombinant human Noggin protein (bone morphogenetic protein-2 (BMP-2) antagonist) group (HN). The mRNA levels and the protein expressions of BMP-2 and core binding factor alpha-1 (Cbf?-1) were measured by real-time quantitative polymerase chain reaction (PCR) and Western blot. After induced by 10 mmol/L ?-glycerol phosphoric acid, cells were harvested for assessments of alkaline phosphatase (ALP) activities at Days 1, 2, and 3, and intracellular calcium contents at Days 7 and 14, respectively. High glucose levels increased the mRNA levels and the protein expressions of BMP-2 and Cbf?-1 (P<0.05). The expression of Cbf?-1 was partially blocked by Noggin protein (P<0.05), while BMP-2 was not (P>0.05). After being induced by ?-glycerol phosphoric acid, high glucose levels increased the ALP activity [(48.63±1.03) vs. (41.42±2.28) U/mg protein, Day 3; P<0.05] and the intracellular calcium content [(2.76±0.09) vs. (1.75±0.07) ?mol/mg protein, Day 14; P<0.05] in a time-dependent manner when compared with the NG group, while the ALP activity could not be blocked by Noggin protein [(48.63±1.03) vs. (47.37±0.97) U/mg protein, Day 3; P>0.05]. These results show that high glucose levels can evoke the calcification of HASMCs by inducing osteoblastic trans-differentiation and intracellular calcium deposition via the BMP-2/Cbf?-1 pathway, which can be partially blocked by Noggin protein.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/BMP2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bone Morphogenetic Protein 2,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Core Binding Factor Alpha 1 Subunit,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/noggin protein
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1862-1783
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
905-11
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pubmed:meshHeading |
pubmed-meshheading:21121067-Alkaline Phosphatase,
pubmed-meshheading:21121067-Bone Morphogenetic Protein 2,
pubmed-meshheading:21121067-Calcinosis,
pubmed-meshheading:21121067-Calcium,
pubmed-meshheading:21121067-Carrier Proteins,
pubmed-meshheading:21121067-Cell Differentiation,
pubmed-meshheading:21121067-Cells, Cultured,
pubmed-meshheading:21121067-Core Binding Factor Alpha 1 Subunit,
pubmed-meshheading:21121067-Glucose,
pubmed-meshheading:21121067-Humans,
pubmed-meshheading:21121067-Muscle, Smooth, Vascular,
pubmed-meshheading:21121067-Myocytes, Smooth Muscle,
pubmed-meshheading:21121067-Osteoblasts,
pubmed-meshheading:21121067-RNA, Messenger,
pubmed-meshheading:21121067-Vascular Diseases
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pubmed:year |
2010
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pubmed:articleTitle |
Effect of high glucose levels on the calcification of vascular smooth muscle cells by inducing osteoblastic differentiation and intracellular calcium deposition via BMP-2/Cbf?-1 pathway.
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pubmed:affiliation |
Division of Nephrology, West China Hospital, Sichuan University, Chengdu, China.
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pubmed:publicationType |
Journal Article
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