Document Detail

Primary structure and tissue distribution of FRZB, a novel protein related to Drosophila frizzled, suggest a role in skeletal morphogenesis.
MedLine Citation:
PMID:  8824257     Owner:  NLM     Status:  MEDLINE    
Articular cartilage extracts were prepared to characterize protein fractions with in vivo chondrogenic activity (Chang, S., Hoang, B., Thomas, J. T., Vukicevic, S., Luyten, F. P., Ryba, N. J. P., Kozak, C. A., Reddi, A. H., and Moos, M. (1994) J. Biol. Chem. 269, 28227-28234). Trypsin digestion of highly purified chondrogenic protein fractions allowed the identification of several unique peptides by amino acid sequencing. We discovered a novel cDNA encoding a deduced 36-kDa protein by using degenerate oligonucleotide primers derived from a 30-residue peptide in reverse transcription polymerase chain reactions. Its N-terminal domain showed approximately 50% amino acid identity to the corresponding region of the Drosophila gene frizzled, which has been implicated in the specification of hair polarity during development. Hydropathy and structural analyses of the open reading frame revealed the presence of a signal peptide and a hydrophobic domain followed by multiple potential serine/threonine phosphorylation sites and a serine-rich C terminus. Cell fractionation studies of primary bovine articular chondrocytes and transfected COS cells suggested that the protein is membrane-associated. In situ hybridization and immunostaining of human embryonic sections demonstrated predominant expression surrounding the chondrifying bone primordia and subsequently in the chondrocytes of the epiphyses in a graded distribution that decreased toward the primary ossification center. Transcripts were present in the craniofacial structures but not in the vertebral bodies. Because it is expressed primarily in the cartilaginous cores of developing long bones during embryonic and fetal development (6-13 weeks) and is homologous to the polarity-determining gene frizzled, we believe that this gene, which we named frzb, is involved in morphogenesis of the mammalian skeleton.
B Hoang; M Moos; S Vukicevic; F P Luyten
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  271     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1996 Oct 
Date Detail:
Created Date:  1996-11-26     Completed Date:  1996-11-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  26131-7     Citation Subset:  IM    
Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892, USA.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/U24163;  U24164
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MeSH Terms
Amino Acid Sequence
Base Sequence
Bone and Bones / embryology*
COS Cells
Cartilage, Articular / chemistry
DNA, Complementary / chemistry
Drosophila Proteins*
Frizzled Receptors
Insect Hormones / chemistry
Membrane Proteins / chemistry
Molecular Sequence Data
Morphogenesis / physiology
Polymerase Chain Reaction
Proteins / chemistry*,  genetics,  physiology
Receptors, G-Protein-Coupled
Sequence Homology, Amino Acid
Tissue Distribution
Reg. No./Substance:
0/DNA, Complementary; 0/Drosophila Proteins; 0/FRZB protein; 0/Frizzled Receptors; 0/Glycoproteins; 0/Insect Hormones; 0/Membrane Proteins; 0/Proteins; 0/Receptors, G-Protein-Coupled; 0/fz protein, Drosophila

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