Linked Life Data

10751411

Source:http://linkedlifedata.com/resource/pubmed/id/10751411

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
2000-8-16
pubmed:databankReference
pubmed:abstractText
hsp27 is involved in development of tolerance to stress, possibly by its involvement in molecular chaperoning, maintenance of glutathione status, and/or modulation of microfilament structure and function. We hypothesize that hsp27 function depends on specific association with other proteins. To discover proteins that associate with hsp27, we made a differentiated rat Sertoli cell cDNA expression library and screened it using the yeast two-hybrid system. We obtained a cDNA coding for a novel protein of 428 amino acids that we have named PASS1 (protein associated with small stress proteins 1). BLAST searches did not reveal major similarity of PASS1 to any known protein, but the cDNA sequence matched several mouse EST clones and shares 34% homology with a Caenorhabditis elegans genomic sequence. In vitro, bacterially expressed glutathione S-transferase-PASS1 fusion protein bound to hsp27, and hsp27 was co-immunoprecipitated with c-Myc-tagged PASS1 overexpressed in several cell lines. The region of PASS1 responsible for association with hsp27 was identified as existing predominantly between amino acids 108 and 208 of PASS1. Northern hybridization and Western blot analysis demonstrated that PASS1 is expressed in several tissues, with the highest expression occurring in testis, primarily in Sertoli cells. The presence of a 1.4-kilobase PASS1 mRNA in kidney as well as the 1. 8-kilobase mRNA seen in other tissues suggests that alternate splicing may occur in this organ. Ectopic expression of PASS1 in two cultured cell lines was observed to inhibit the ability of hsp27 to protect cells against heat shock, indicating that PASS1 does interact with hsp27 in the live cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18724-31
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10751411-Amino Acid Sequence, pubmed-meshheading:10751411-Animals, pubmed-meshheading:10751411-Base Sequence, pubmed-meshheading:10751411-Caenorhabditis elegans Proteins, pubmed-meshheading:10751411-Carrier Proteins, pubmed-meshheading:10751411-Cell Line, pubmed-meshheading:10751411-Cloning, Molecular, pubmed-meshheading:10751411-DNA, Complementary, pubmed-meshheading:10751411-HSP27 Heat-Shock Proteins, pubmed-meshheading:10751411-Heat-Shock Proteins, pubmed-meshheading:10751411-Heat-Shock Response, pubmed-meshheading:10751411-Male, pubmed-meshheading:10751411-Mice, pubmed-meshheading:10751411-Molecular Sequence Data, pubmed-meshheading:10751411-Neoplasm Proteins, pubmed-meshheading:10751411-Protein Binding, pubmed-meshheading:10751411-Rats, pubmed-meshheading:10751411-Sertoli Cells
pubmed:year
2000
pubmed:articleTitle
Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27.
pubmed:affiliation
Departments of Cell and Developmental Biology and Plastic and Reconstructive Surgery, University of Michigan Medical School, Ann Arbor, Michigan 48109, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.