The absence of type II collagen and changes in proteoglycan structure of hyaline cartilage in a case of Langer-Saldino achondrogenesis

Structural analysis of hyaline cartilage extracellular matrix components from the ribs and knee joint of a stillborn female with type II achondrogenesis was carried out. The absence of type II collagen, a decrease in the amount of proteoglycans (PG), and structural changes in PG, namely, increased e...

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Bibliographic Details
Published in:Human genetics 1989-04, Vol.82 (1), p.49-54
Main Authors: FESHCHENKO, S. P, REBRIN, I. A, SOKOLNIK, V. P, SHER, B. M, SOKOLOV, B. P, KALININ, V. N, LAZJUK, G. I
Format: Article
Language:English
Subjects:
Achondroplasia - pathology
Autopsy
Biological and medical sciences
Cartilage - pathology
Collagen - deficiency
Diseases of the osteoarticular system
Electrophoresis, Polyacrylamide Gel
Extracellular Matrix - analysis
Extracellular Matrix Proteins
Female
Fetal Death
Humans
Lung - pathology
Malformations and congenital and or hereditary diseases involving bones. Joint deformations
Medical sciences
Pregnancy
Proteins - analysis
Proteoglycans - analysis
Spectrophotometry, Infrared
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Summary:Structural analysis of hyaline cartilage extracellular matrix components from the ribs and knee joint of a stillborn female with type II achondrogenesis was carried out. The absence of type II collagen, a decrease in the amount of proteoglycans (PG), and structural changes in PG, namely, increased electrophoretic mobility of PG, lower relative content of chondroitin 4-sulfate (Ch4-S), lower molecular weight and decreased total chondroitin sulfate (ChS) sulfation, were detected. Increased amounts of type I and type III collagens, atypical for hyaline cartilage, were revealed. Among the link proteins (LPs), a large protein with a mol. wt. of 48 kDa was predominant. Molecular and cellular mechanisms of the pathogenesis of achondrogenesis ("chondrogenesis imperfecta") are discussed. The data obtained suggest that the primary defect in type II achondrogenesis involves ChS or type II collagen synthesis.
ISSN:0340-6717
1432-1203
DOI:10.1007/BF00288271