| pubmed-article:9022054 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9022054 | lifeskim:mentions | umls-concept:C0025936 | lld:lifeskim |
| pubmed-article:9022054 | lifeskim:mentions | umls-concept:C0009331 | lld:lifeskim |
| pubmed-article:9022054 | lifeskim:mentions | umls-concept:C1160401 | lld:lifeskim |
| pubmed-article:9022054 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:9022054 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9022054 | pubmed:dateCreated | 1997-3-6 | lld:pubmed |
| pubmed-article:9022054 | pubmed:abstractText | Skeletal development of transgenic mice with a type II collagen mutation was analyzed and compared with wild-type littermates. The single base substitution in Col2a1 resulted in a glycine to serine mutation within the helical domain and corresponded to one previously identified in a patient with the lethal human chondrodysplasia, hypochondrogenesis (Horton et al. [1992] Proc. Natl. Acad. Sci. U.S.A. 89:4583-4587). Skeletal staining of embryos from 14.5 through 18.5 days of gestation demonstrated a dwarf phenotype in the transgenic embryos, most notably short limb bones and vertebral column that was first detected at 15.5 days post-coitus. In addition to the reduced length, the extent of ossification was less in the transgenic mice. The architecture of the long bone growth plate was abnormal in the transgenic tissue, in particular there was no discernible proliferative zone. There were few stacks of characteristically flattened cells and the overall length of the growth plate in the mutant embryos was reduced. At the ultrastructural level, there were fewer collagen fibrils present in the transgenic mouse cartilage compared to that of wild-type littermates. Ultrastructural localization of collagen types II, IX and XI revealed a similar pattern between the transgenic and wild-type pups, suggesting that the collagen fibrils present in the matrix of littermates with both phenotypes had a similar composition. Skeletal analysis and cartilage histochemistry indicated that effect of the type II collagen mutation was to reduce the density of the collagen fibrils within the cartilage matrix which was associated with delayed bone formation and resulted in a short-limbed phenotype. | lld:pubmed |
| pubmed-article:9022054 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9022054 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9022054 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9022054 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9022054 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9022054 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9022054 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9022054 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9022054 | pubmed:issn | 1058-8388 | lld:pubmed |
| pubmed-article:9022054 | pubmed:author | pubmed-author:SmithCC | lld:pubmed |
| pubmed-article:9022054 | pubmed:author | pubmed-author:HortonW AWA | lld:pubmed |
| pubmed-article:9022054 | pubmed:author | pubmed-author:GarofaloSS | lld:pubmed |
| pubmed-article:9022054 | pubmed:author | pubmed-author:KeeneD RDR | lld:pubmed |
| pubmed-article:9022054 | pubmed:author | pubmed-author:MaddoxB KBK | lld:pubmed |
| pubmed-article:9022054 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9022054 | pubmed:volume | 208 | lld:pubmed |
| pubmed-article:9022054 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9022054 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9022054 | pubmed:pagination | 170-7 | lld:pubmed |
| pubmed-article:9022054 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:meshHeading | pubmed-meshheading:9022054-... | lld:pubmed |
| pubmed-article:9022054 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9022054 | pubmed:articleTitle | Skeletal development in transgenic mice expressing a mutation at Gly574Ser of type II collagen. | lld:pubmed |
| pubmed-article:9022054 | pubmed:affiliation | Research Department, Shriners Hospital for Children, Portland, Oregon 97201, USA. | lld:pubmed |
| pubmed-article:9022054 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9022054 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9022054 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:12824 | entrezgene:pubmed | pubmed-article:9022054 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9022054 | lld:pubmed |
