pubmed-article:7863822 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0018283 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0225369 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0009339 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C2246343 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0162788 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:7863822 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
pubmed-article:7863822 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:7863822 | pubmed:dateCreated | 1995-3-20 | lld:pubmed |
pubmed-article:7863822 | pubmed:abstractText | Type X collagen is produced by hypertrophic chondrocytes and serves as a highly specific marker for chondrocyte maturation. This study was designed to compare the expression of type II and type X collagen in growth plate sections and in distinct populations of chondrocytes in culture by in situ hybridization. Growth plate sections were treated with type II and type X collagen cDNA probes. Type II collagen mRNA was present throughout the growth plate but greatest in the lower proliferating and upper hypertrophic regions. In contrast, type X collagen was expressed only in the hypertrophic region. Northern analysis confirmed the specificity of the probe for type X collagen mRNA. Chick growth plate chondrocytes were separated by countercurrent centrifugal elutriation into five distinct populations and plated in serum-containing medium. These cultures were examined at varying times after plating for the expression of type II and type X collagen mRNA. At 3 h, type II collagen was present in the majority of the cells in all fractions, and approximately 15-20% of the cells expressed type X collagen mRNA. The cells expressing type X were from the hypertrophic region. At 24 h, however, nearly all cells in culture expressed type X mRNA, and there was a decrease in expression of type II collagen mRNA. Similar results were obtained in cultures in the absence of serum, and SDS-PAGE analysis of collagen synthesis confirmed the expression of type X collagen in all populations of fractionated cells at 24 h at the protein level. Type X collagen is an important marker through which cellular matruation can be evaluated in culture.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
pubmed-article:7863822 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7863822 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7863822 | pubmed:language | eng | lld:pubmed |
pubmed-article:7863822 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7863822 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7863822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7863822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7863822 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7863822 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7863822 | pubmed:month | Nov | lld:pubmed |
pubmed-article:7863822 | pubmed:issn | 0884-0431 | lld:pubmed |
pubmed-article:7863822 | pubmed:author | pubmed-author:PuzasJ EJE | lld:pubmed |
pubmed-article:7863822 | pubmed:author | pubmed-author:RosierR NRN | lld:pubmed |
pubmed-article:7863822 | pubmed:author | pubmed-author:O'KeefeR JRJ | lld:pubmed |
pubmed-article:7863822 | pubmed:author | pubmed-author:HicksD GDG | lld:pubmed |
pubmed-article:7863822 | pubmed:author | pubmed-author:LoveysLL | lld:pubmed |
pubmed-article:7863822 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7863822 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:7863822 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7863822 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7863822 | pubmed:pagination | 1713-22 | lld:pubmed |
pubmed-article:7863822 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:7863822 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7863822 | pubmed:articleTitle | Analysis of type II and type X collagen synthesis in cultured growth plate chondrocytes by in situ hybridization: rapid induction of type X collagen in culture. | lld:pubmed |
pubmed-article:7863822 | pubmed:affiliation | Department of Orthopaedics, University of Rochester School of Medicine and Dentistry, New York. | lld:pubmed |
pubmed-article:7863822 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7863822 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:7863822 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7863822 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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