Linked Life Data

8634155

Source:http://linkedlifedata.com/resource/pubmed/id/8634155

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-7-9
pubmed:databankReference
pubmed:abstractText
Hsp47 is a major stress-inducible protein that is localized to the endoplasmic reticulum of avian and mammalian cells and is thought to act as a molecular chaperone specific for the processing of procollagen. Although hsp47 is coordinately expressed together with several collagen types, and vertebrate embryos are known to express collagen genes in complex spatial and temporal patterns, limited information is available regarding the function or regulation of hsp47 during early embryonic development. We have initiated an examination of hsp47 in the zebrafish, Danio rerio, which offers a number of features that make it attractive as a model developmental system with which to examine the expression and function of hsp47. A polymerase chain reaction (PCR)-based cloning strategy was used to isolate a hsp47 cDNA from an embryonic zebrafish cDNA library. The deduced translation product of the cDNA is a 404-amino-acid polypeptide that is 72% identical to chicken, 64% identical to mouse and rat, and 69% identical to human hsp47. The protein contains a typical hydrophobic signal sequence, an RDEL endoplasmic reticulum retention signal, and a serine protease inhibitor signature sequence, all of which are characteristic of hsp47 in higher vertebrates. Thus, it is likely that hsp47 in zebrafish is also localized to the endoplasmic reticulum and may play a similar role to its counterpart in higher vertebrates. Northern blot analysis revealed that the hsp47 gene is expressed at relatively low levels in embryos during normal development but is strongly induced following exposure to heat shock at the gastrula, midsomitogenesis, 2-day, and 3-day larval stages. The level of induction was much higher than has previously been reported in chicken and mouse cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1044-5498
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8634155-Amino Acid Sequence, pubmed-meshheading:8634155-Animals, pubmed-meshheading:8634155-Base Sequence, pubmed-meshheading:8634155-Cloning, Molecular, pubmed-meshheading:8634155-DNA, Complementary, pubmed-meshheading:8634155-DNA Primers, pubmed-meshheading:8634155-Gene Expression Regulation, Developmental, pubmed-meshheading:8634155-Genes, pubmed-meshheading:8634155-HSP47 Heat-Shock Proteins, pubmed-meshheading:8634155-Heat-Shock Proteins, pubmed-meshheading:8634155-Humans, pubmed-meshheading:8634155-Integrins, pubmed-meshheading:8634155-Mice, pubmed-meshheading:8634155-Molecular Sequence Data, pubmed-meshheading:8634155-Phylogeny, pubmed-meshheading:8634155-Rats, pubmed-meshheading:8634155-Receptors, Collagen, pubmed-meshheading:8634155-Sequence Alignment, pubmed-meshheading:8634155-Sequence Homology, Amino Acid, pubmed-meshheading:8634155-Zebrafish, pubmed-meshheading:8634155-Zebrafish Proteins
pubmed:year
1996
pubmed:articleTitle
Cloning and characterization of a cDNA encoding the collagen-binding stress protein hsp47 in zebrafish.
pubmed:affiliation
Department of Anatomy and Cell Biology, University of Saskatchewan, Saskatoon, Canada.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't