Linked Life Data

8824257

Source:http://linkedlifedata.com/resource/pubmed/id/8824257

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
1996-11-26
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
26131-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8824257-Amino Acid Sequence, pubmed-meshheading:8824257-Animals, pubmed-meshheading:8824257-Base Sequence, pubmed-meshheading:8824257-Bone and Bones, pubmed-meshheading:8824257-COS Cells, pubmed-meshheading:8824257-Cartilage, Articular, pubmed-meshheading:8824257-Cattle, pubmed-meshheading:8824257-DNA, Complementary, pubmed-meshheading:8824257-Drosophila, pubmed-meshheading:8824257-Drosophila Proteins, pubmed-meshheading:8824257-Frizzled Receptors, pubmed-meshheading:8824257-Glycoproteins, pubmed-meshheading:8824257-Humans, pubmed-meshheading:8824257-Insect Hormones, pubmed-meshheading:8824257-Membrane Proteins, pubmed-meshheading:8824257-Molecular Sequence Data, pubmed-meshheading:8824257-Morphogenesis, pubmed-meshheading:8824257-Polymerase Chain Reaction, pubmed-meshheading:8824257-Proteins, pubmed-meshheading:8824257-Rats, pubmed-meshheading:8824257-Receptors, G-Protein-Coupled, pubmed-meshheading:8824257-Sequence Homology, Amino Acid, pubmed-meshheading:8824257-Tissue Distribution
pubmed:year
1996
pubmed:articleTitle
Primary structure and tissue distribution of FRZB, a novel protein related to Drosophila frizzled, suggest a role in skeletal morphogenesis.
pubmed:affiliation
Bone Research Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't