Linked Life Data

9013726

Source:http://linkedlifedata.com/resource/pubmed/id/9013726

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-4-17
pubmed:abstractText
Polarized transport of proteins is contingent on the presence of specific protein structures or motifs that function as sorting signals. Our model protein to analyze and to identify such signals is that of lactase-phlorizin hydrolase (LPH), a strictly polarized brush border membrane protein of small intestinal epithelial cells. It is synthesized as a large pro-LPH precursor molecule, which is proteolytically processed to yield the mature brush border enzyme (LPHbeta). Pro-LPH as well as LPHbeta are correctly sorted to the brush border membrane. In this paper we examine the location of putative sorting signals in the pro-LPH molecule. Expression of a cDNA encoding the LPHbeta mature form in the absence of the LPHalpha species in Madin-Darby canine kidney (MDCK) cells reveal an LPHbeta molecule that is not as transport-competent as wild type pro-LPH. The proportion of complex glycosylated LPHbeta constitutes not more than 10% of the total synthesized protein. This form displays a similar trypsin sensitive pattern as wild type intestinal LPHbeta suggesting comparable folding patterns of the two species. Complex glycosylated LPHbeta is sorted to the apical membrane more efficiently than wild type pro-LPH. We conclude that the apical sorting signals for pro-LPH are exclusively found in the LPHbeta mature domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0171-9335
pubmed:author
pubmed:issnType
Print
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
54-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The apical sorting of lactase-phlorizin hydrolase implicates sorting sequences found in the mature domain.
pubmed:affiliation
Institute of Microbiology, Heinrich Heine University of Düsseldorf, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't