Linked Life Data

8569078

Source:http://linkedlifedata.com/resource/pubmed/id/8569078

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1996-3-1
pubmed:abstractText
A fundamental property of ion channels is their ability to be modulated by intracellular second messenger systems acting via covalent modifications of the channel protein itself. One such important biochemical reaction is phosphorylation on serine, threonine, and tyrosine residues. Ion channels in the kidney are no exception. Moreover, many ion channels, including many amiloride-sensitive epithelial Na+ channels, are subject to modulation by a multiplicity of inputs. For example, renal Na+ channels are not gated by voltage in their unphosphorylated state. However, upon phosphorylation by PKA plus ATP, these channels become voltage-dependent as well as having their open probability increased. Phosphorylation by PKC inhibits channel activity regardless of whether the channel was previously phosphorylated by PKA. Likewise, Na+ channel ADP-ribosylation by PTX overrides the actions of cAMP-dependent phosphorylation. Consistent with this idea is the fact that the phosphorylation sites for PKA and PKC and the ADP-ribosylation sites occur on different polypeptides comprising the channel complex. Epithelial Na+ channel activity is also regulated by methylation, arachidonic acid metabolites, and by interactions with cytoskeletal components. An exciting new age in understanding renal Na+ channel function has begun. Canessa and collaborators [103, 104] and Lingueglia et al [105] have, for the first time, identified by expression cloning an amiloride-sensitive Na+ channel from rat distal colon. The messenger RNA encoding the subunits comprising this channel are expressed in the distal tubule and cortical collecting tubule of the kidney (Rossier, unpublished observations). In addition, our laboratory has successfully cloned a mammalian homologue of this same channel from bovine renal papillary collecting ducts [106].(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0085-2538
pubmed:author
pubmed:issnType
Print
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1167-79
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Effects of phosphorylation on ion channel function.
pubmed:affiliation
Department of Physiology and Biophysics, University of Alabama at Birmingham, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review