Linked Life Data

8679656

Source:http://linkedlifedata.com/resource/pubmed/id/8679656

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-8-20
pubmed:abstractText
A concentrative uptake of arginine into brush border membrane vesicles (BBMV) from the midgut of Manduca sexta larvae was driven by an inwardly directed K+ gradient. The pH-dependence of the initial rate of arginine uptake between pH 7 and 10.5 paralleled the titration curve of the amino acid, suggesting that cationic arginine is the principal ionic form that is transported. In the presence of K+, at pH 7.4, arginine uptake was cis-inhibited and trans-stimulated by arginine and lysine but not by any other naturally occurring amino acids; it was also cis-inhibited by homoarginine and ornithine. Taken together, these data argue that arginine, lysine and their analogues share a cationic amino acid:K+ symporter (cotransporter), which we will designate as System R+. This novel symporter has a substrate spectrum similar to that of the uniporter, System y+, in that it accepts arginine+, lysine+, homoarginine+ and ornithine+ and rejects histidine. However, it differs from y+ in that it is cation-dependent and is almost inactive at pH 5.5.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
1282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25-31
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Arginine uptake through a novel cationic amino acid:K+ symporter, System R+, in brush border membrane vesicles from larval Manduca sexta midgut.
pubmed:affiliation
Department of Biology, Temple University, Philadelphia, PA 19122, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.