Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-7-25
pubmed:databankReference
pubmed:abstractText
cDNAs for hyaluronic acid synthases (HAS2 and HAS3) were cloned from a cDNA library of cultured rabbit synovial membrane cells. The cDNA encoding the open reading frame of rabbit HAS2 and HAS3 was 1659 nucleotides in length with a predicted molecular mass of about 63 kDa. The amino acid sequence showed that the rabbit HAS2 was 98.7 and 98.4%, and HAS3 was 98.2 and 97.5% identical with human and mouse forms of the proteins, respectively. The predicted sequences for hyaluronic acid (HA) binding motifs and the catalytic domains related to beta 1-4 and beta 1-3 linkages, essential for HA synthesis, were almost conserved in both rabbit HAS2 and HAS3, similarly to human and mouse HASs. RT-PCR analysis and in situ hybridization revealed that the mRNA of HAS2 was highly expressed in the synovial membrane and articular cartilage, whereas the expression of HAS3 mRNA was slightest in these tissues. Thus, it is demonstrated that rabbit HASs are highly conserved in sequence content as compared to the human and mouse homologues described previously, and that HAS2 is predominantly expressed in the synovial membrane and articular cartilage, but HAS3 is not.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronosyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Glycosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/HAS1 protein, Xenopus, http://linkedlifedata.com/resource/pubmed/chemical/Has2 protein, Xenopus, http://linkedlifedata.com/resource/pubmed/chemical/Has2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Has3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Transferases, http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins, http://linkedlifedata.com/resource/pubmed/chemical/hyaluronan synthase
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
1520
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11470161-Amino Acid Sequence, pubmed-meshheading:11470161-Animals, pubmed-meshheading:11470161-Base Sequence, pubmed-meshheading:11470161-Cartilage, Articular, pubmed-meshheading:11470161-Cloning, Molecular, pubmed-meshheading:11470161-Glucuronosyltransferase, pubmed-meshheading:11470161-Glycosyltransferases, pubmed-meshheading:11470161-In Situ Hybridization, pubmed-meshheading:11470161-Isoenzymes, pubmed-meshheading:11470161-Membrane Proteins, pubmed-meshheading:11470161-Molecular Sequence Data, pubmed-meshheading:11470161-RNA, Messenger, pubmed-meshheading:11470161-Rabbits, pubmed-meshheading:11470161-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11470161-Sequence Alignment, pubmed-meshheading:11470161-Synovial Membrane, pubmed-meshheading:11470161-Transferases, pubmed-meshheading:11470161-Xenopus Proteins
pubmed:year
2001
pubmed:articleTitle
Molecular cloning of rabbit hyaluronic acid synthases and their expression patterns in synovial membrane and articular cartilage.
pubmed:affiliation
Department of Orthodontics, Hiroshima University, Faculty of Dentistry, Japan. shigebon@hiroshima-u.ac.jp
pubmed:publicationType
Journal Article, Comparative Study