pubmed-article:1771175 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1771175 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:1771175 | lifeskim:mentions | umls-concept:C0002059 | lld:lifeskim |
pubmed-article:1771175 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:1771175 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
pubmed-article:1771175 | lifeskim:mentions | umls-concept:C1514485 | lld:lifeskim |
pubmed-article:1771175 | lifeskim:mentions | umls-concept:C0286382 | lld:lifeskim |
pubmed-article:1771175 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:1771175 | pubmed:dateCreated | 1992-2-27 | lld:pubmed |
pubmed-article:1771175 | pubmed:abstractText | The effect of beta-alanyl-L-histidinato zinc (AHZ) on bone metabolism was investigated in osteoblastic MC3T3-E1 cells. Cells were cultured for 3 days at 37 degrees C in a CO2 incubator in plastic dishes containing alpha-modified minimum essential medium supplemented with 10% fetal bovine serum. After the cultures, the medium was exchanged for that containing 0.1% bovine serum albumin plus various concentrations of AHZ or zinc sulfate, and the cells were cultured further for appropriate periods of time. The presence of AHZ (10(-6)-10(-4) mol/l) stimulated proliferation of cells. AHZ increased alkaline phosphatase activity in a dose-related manner up to 10(-5) mol/l; the increase was about 2-fold over the control value. Studies on the effect of actinomycin D or cycloheximide treatment indicated that AHZ may enhance de novo synthesis of the enzyme. AHZ also increased deoxyribonucleic acid (DNA) content dose dependently (10(-6)-10(-4) mol/l). This increase was completely blocked by treatment with cycloheximide. The AHZ (10(-5) mol/l)-induced increases in alkaline phosphatase activity and DNA content were entirely abolished by the presence of dipicolinate (10(-4) mol/l), a chelator of zinc, indicating that the effect of AHZ needs zinc. However, AHZ had a potent effect, more than that of zinc sulfate, on alkaline phosphatase activity and DNA content. The present results indicate that AHZ has a direct specific anabolic effect on osteoblastic cells in vitro and that this effect is related to protein synthesis. | lld:pubmed |
pubmed-article:1771175 | pubmed:language | eng | lld:pubmed |
pubmed-article:1771175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1771175 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1771175 | pubmed:issn | 0031-7012 | lld:pubmed |
pubmed-article:1771175 | pubmed:author | pubmed-author:YamaguchiMM | lld:pubmed |
pubmed-article:1771175 | pubmed:author | pubmed-author:OhtakeNN | lld:pubmed |
pubmed-article:1771175 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1771175 | pubmed:volume | 43 | lld:pubmed |
pubmed-article:1771175 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1771175 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1771175 | pubmed:pagination | 225-32 | lld:pubmed |
pubmed-article:1771175 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:1771175 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1771175 | pubmed:articleTitle | Effect of beta-alanyl-L-histidinato zinc on osteoblastic MC3T3-E1 cells: increases in alkaline phosphatase and proliferation. | lld:pubmed |
pubmed-article:1771175 | pubmed:affiliation | Department of Environmental Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Japan. | lld:pubmed |
pubmed-article:1771175 | pubmed:publicationType | Journal Article | lld:pubmed |