Linked Life Data

1515761

Source:http://linkedlifedata.com/resource/pubmed/id/1515761

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-10-2
pubmed:abstractText
Collagen extracted either from cartilage or synthesized in vitro was analyzed to identify possible molecular defects in the cartilaginous matrix of a male fetus suffering from a mild form of type II achondrogenesis (Langer-Saldino). The tissue architecture of the patient's cartilage was markedly altered and showed numerous fibrous vascular canals which were focally stained by antibodies against collagens I and III. Collagen II was present, although heterogenously distributed throughout the cartilaginous matrix. Upon electrophoretic separation, however, the patient's femoral head cartilage showed the presence of collagens II, IX and XI only, which was similar to an age-matched control. The hydroxyproline/hydroxylysine ratio of collagen II of the patient was not significantly different from that of the control. Likewise, the compositions of collagens synthesized by cultured chondrocytes as well as fibroblasts were similar in the patient and the control. The results provide strong evidence that, in the present mild case of Langer-Saldino achondrogenesis, collagen II is expressed and regularly hydroxylated at its lysyl residues. This may indicate that cartilage components other than collagen II may be responsible for the altered tissue organization observed. Along with previous observations, our data suggest that the degree of biochemical matrix alterations may be related to the severity of the clinical phenotype.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0803-5253
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
158-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Collagen type II in Langer-Saldino achondrogenesis: absence of major abnormalities in a less severe case.
pubmed:affiliation
Institut für Medizinische Molekularbiologie, Medizinische Universität, Lübeck, Germany.
pubmed:publicationType
Journal Article, In Vitro, Case Reports, Research Support, Non-U.S. Gov't