Linked Life Data

1281159

Source:http://linkedlifedata.com/resource/pubmed/id/1281159

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1993-1-12
pubmed:abstractText
The effect of a cAMP-dependent secretogogue (VIP) on the phosphorylation of an endogenous, membrane-bound protein (pp170) was assessed in an intact cell preparation from the avian salt gland. The addition of VIP, in the presence of 100 microM isobutylmethylxanthine, resulted in a concentration-dependent increase in phosphorylation of pp170. This effect was rapid and transient with a 3-5-fold increase in phosphorylation occurring 1 min after the addition of VIP. Under similar incubation conditions, VIP stimulated a 4.6-fold increase in cAMP accumulation that paralleled phosphorylation. Exposure of cells to either forskolin or 8-Br-cAMP resulted in a 5-8-fold increase in the phosphorylation of pp170. The effect of forskolin was dose dependent with an EC50 similar to that for stimulation of secretion (35 nM). These results implicate an involvement for a cAMP-dependent protein kinase in the phosphorylation of pp170. The identity of pp170 was assessed utilizing a monoclonal antibody (Q3) directed against pp170. Q3 recognized a single 170-kDa band on Western blots of salt gland membrane protein. Immunoprecipitation of pp170 from salt gland cells resulted in the selective extraction of a single protein whose phosphorylation state was increased approximately 5-fold in response to carbachol or VIP. The identity of pp170 was established using two criteria. First, Q3 recognized affinity-purified Na:K:Cl cotransporter preparations from shark rectal gland membranes. Second, pp170 was selectively immunoprecipitated by monoclonal antibodies (J3, J4, and J7) that recognize different epitopes of the shark transport protein. These results suggest that pp170 is homologous to the shark rectal gland Na-K-Cl cotransporter, and thus the proteins may be functionally similar.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25444-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1281159-1-Methyl-3-isobutylxanthine, pubmed-meshheading:1281159-8-Bromo Cyclic Adenosine Monophosphate, pubmed-meshheading:1281159-Animals, pubmed-meshheading:1281159-Blotting, Western, pubmed-meshheading:1281159-Calcium, pubmed-meshheading:1281159-Carbachol, pubmed-meshheading:1281159-Carrier Proteins, pubmed-meshheading:1281159-Cell Membrane, pubmed-meshheading:1281159-Cyclic AMP, pubmed-meshheading:1281159-Ducks, pubmed-meshheading:1281159-Forskolin, pubmed-meshheading:1281159-Kinetics, pubmed-meshheading:1281159-Membrane Proteins, pubmed-meshheading:1281159-Phosphates, pubmed-meshheading:1281159-Phosphorylation, pubmed-meshheading:1281159-Salt Gland, pubmed-meshheading:1281159-Sodium-Potassium-Chloride Symporters, pubmed-meshheading:1281159-Time Factors, pubmed-meshheading:1281159-Vasoactive Intestinal Peptide
pubmed:year
1992
pubmed:articleTitle
The Na-K-Cl cotransporter of avian salt gland. Phosphorylation in response to cAMP-dependent and calcium-dependent secretogogues.
pubmed:affiliation
Department of Pharmacology, University of Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't