The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains.
Type IX collagen molecules contain three genetically distinct subunits. One of the subunits, alpha 2(IX), contains a covalently attached glycosaminoglycan side chain. A second subunit, alpha 1 (IX), has been found to be synthesized in two forms. The two forms are generated by the alternative use of two transcription start sites and splice patterns. The two forms have been found in chicken, mouse and human but cDNAs encoding both forms have only been reported for chicken. In the present report we describe the isolation of cDNA clones encoding the complete translated portion of both forms of human alpha 1(IX) collagen chains. Nucleotide sequence analysis has permitted the determination of the primary structure of both forms. These probes and sequences should prove useful in future studies of chondrodysplasias involving type IX collagen.
Muragaki
Y
Y
Department of Anatomy and Cellular Biology, Harvard Medical School, Boston, MA 02115.
Kimura
T
T
Ninomiya
Y
Y
Olsen
B R
BR
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002645:Chickens; D003001:Cloning, Molecular; D003094:Collagen / Q000737:chemistry*; D004247:DNA / Q000032:analysis; D006025:Glycosaminoglycans / Q000032:analysis; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D015341:Nucleic Acid Probes; D016133:Polymerase Chain Reaction; D013045:Species Specificity; D014157:Transcription Factors / Q000032:analysis
D006025:Glycosaminoglycans; D015341:Nucleic Acid Probes; D014157:Transcription Factors; D003094:Collagen; D004247:DNA