Open AccessThe complete primary structure of two distinct forms of human α(IX) collagen chains
Author(s) -
MURAGAKI Yasuteru,
KIMURA Tomoatsu,
NINOMIYA Yoshifumi,
OLSEN Bjorn Reino
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19279.x
Subject(s) - protein primary structure , complementary dna , protein subunit , splice , biology , sequence (biology) , microbiology and biotechnology , peptide sequence , nucleic acid sequence , genetics , chemistry , gene
Type IX collagen molecules contain three genetically distinct subunits. One of the subunits, α2(IX), contains a covalently attached glycosaminoglycan side chain. A second subunit, α1(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 α1(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.