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Cloning and sequence analysis of bovine bone sialoprotein cDNA: Conservation of acidic domains, tyrosine sulfation consensus repeats, and RGD cell attachment domain
Author(s) -
Chenu C.,
Ibaraki K.,
Robey P. Gehron,
Delmas P.D.,
Young M.F.
Publication year - 1994
Publication title -
journal of bone and mineral research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.882
H-Index - 241
eISSN - 1523-4681
pISSN - 0884-0431
DOI - 10.1002/jbmr.5650090318
Subject(s) - bone sialoprotein , complementary dna , peptide sequence , biology , microbiology and biotechnology , signal peptide , nucleic acid sequence , consensus sequence , amino acid , cdna library , biochemistry , dna , gene , osteocalcin , alkaline phosphatase , enzyme
We isolated and sequenced a cDNA encoding bovine bone sialoprotein (BSP) using a bovine cDNA library made from mRNA isolated from bone‐derived cell cultures and ligated to a phage λgt11. One of the cDNA clones isolated from this library had a 1800 base pair long insert and was found to contain the entire protein‐encoding region. The deduced protein sequence revealed a 310 amino acid protein containing a signal peptide sequence of 16 hydrophobic amino acids. The protein sequence shows remarkable conservation with previously published human and rat sequences (more than 80% similarity for both species). The potential functional domains of BSP, including three acid amino acid‐rich sequences, tyrosine sulfation consensus repeats, and the RGD cell binding sequence, are all present in the bovine sequence. Northern analysis of RNA from different bovine tissues indicated the presence of BSP message in bone but not in other nonmineralized tissues, confirming that bone is the major site of BSP message production.