A type X collagen mutation causes Schmid metaphyseal chondrodysplasia

Nat Genet. 1993 Sep;5(1):79-82. doi: 10.1038/ng0993-79.


The expression of type X collagen is restricted to hypertrophic chondrocytes in regions undergoing endochondral ossification, such as growth plates. The precise function of type X collagen is unknown but the tissue-specific expression prompted us to examine the gene in hereditary disorders of cartilage and bone growth (osteochondrodysplasias). We have identified a 13 base pair deletion in one type X collagen allele segregating with autosomal dominant Schmid metaphyseal chondrodysplasia in a large Mormon kindred (lod score = 18.2 at theta = 0). The mutation produces a frameshift which alters the highly conserved C-terminal domain of the alpha 1(X) chain and reduces the length of the polypeptide by nine residues. This mutation may prevent association of the mutant polypeptide during trimer formation, resulting in a decreased amount of normal protein.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alleles
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Chickens
  • Collagen / genetics*
  • DNA Mutational Analysis
  • Genes*
  • Genes, Dominant
  • Humans
  • Mice
  • Molecular Sequence Data
  • Osteochondrodysplasias / genetics*
  • Pedigree
  • Sequence Alignment
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Species Specificity


  • Collagen