Linked Life Data

12933801

Source:http://linkedlifedata.com/resource/pubmed/id/12933801

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:12933801rdf:typepubmed:Citationlld:pubmed
pubmed-article:12933801lifeskim:mentionsumls-concept:C0332307lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C2752508lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C0002812lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1622525lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1167322lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1442758lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C0439851lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1706211lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1709694lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1709915lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1552596lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1546857lld:lifeskim
pubmed-article:12933801lifeskim:mentionsumls-concept:C1947931lld:lifeskim
pubmed-article:12933801pubmed:issue48lld:pubmed
pubmed-article:12933801pubmed:dateCreated2003-11-24lld:pubmed
pubmed-article:12933801pubmed:abstractTextSurfactant protein C (SP-C) is a lung-specific protein that is synthesized as a 21-kDa integral membrane propeptide (pro-SP-C) and proteolytically processed to a 3.7-kDa secretory product. Previous studies have shown that palmitoylation of pro-SP-C is dependent on two N-terminal juxtamembrane positively charged residues. We hypothesized that these residues influence modification of pro-SP-C by directing transmembrane orientation. Double substitution mutation of these juxtaposed residues from positive to neutral charged species resulted in complete reversal of transmembrane orientation of pro-SP-C and total abrogation of post-translational processing. Mutation of a single residue resulted in mixed orientation. Protein trafficking studies in A549 cells showed that while the double mutant was retained in the endoplasmic reticulum, single mutants produced a mixed pattern of both endoplasmic reticulum (double mutant-like) and vesicular (wild type-like) expression. Our study demonstrates the crucial role juxtamembrane positively charged residues play in establishing membrane topology and their influence on the trafficking and processing of pro-SP-C. Moreover this study provides a likely precedent for a mechanism in disorders associated with mutations in the membrane-flanking region of integral membrane proteins.lld:pubmed
pubmed-article:12933801pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:languageenglld:pubmed
pubmed-article:12933801pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:citationSubsetIMlld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12933801pubmed:statusMEDLINElld:pubmed
pubmed-article:12933801pubmed:monthNovlld:pubmed
pubmed-article:12933801pubmed:issn0021-9258lld:pubmed
pubmed-article:12933801pubmed:authorpubmed-author:MulugetaSuraf...lld:pubmed
pubmed-article:12933801pubmed:authorpubmed-author:BeersMichael...lld:pubmed
pubmed-article:12933801pubmed:issnTypePrintlld:pubmed
pubmed-article:12933801pubmed:day28lld:pubmed
pubmed-article:12933801pubmed:volume278lld:pubmed
pubmed-article:12933801pubmed:ownerNLMlld:pubmed
pubmed-article:12933801pubmed:authorsCompleteYlld:pubmed
pubmed-article:12933801pubmed:pagination47979-86lld:pubmed
pubmed-article:12933801pubmed:dateRevised2007-11-14lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:meshHeadingpubmed-meshheading:12933801...lld:pubmed
pubmed-article:12933801pubmed:year2003lld:pubmed
pubmed-article:12933801pubmed:articleTitleProcessing of surfactant protein C requires a type II transmembrane topology directed by juxtamembrane positively charged residues.lld:pubmed
pubmed-article:12933801pubmed:affiliationLung Epithelial Cell Biology Laboratories, Pulmonary and Critical Care Division, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-4318, USA. mulugeta@mail.med.upenn.edulld:pubmed
pubmed-article:12933801pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12933801pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:12933801pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:6440entrezgene:pubmedpubmed-article:12933801lld:entrezgene
entrez-gene:50683entrezgene:pubmedpubmed-article:12933801lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:12933801lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:12933801lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12933801lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12933801lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12933801lld:pubmed