Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P01185 (
vasopressin
)
23,126
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The apical (luminal) plasma membrane of toad bladder epithelial cells has been labeled with (125I) diazo-diiodo sulfanilic acid (125I-DDISA) as demonstrated by electron-microscopic autoradiography. The silver grains (125I) were localized exclusively to the apical surface. At concentrations of DDISA of 10(-3) M or less, binding to the apical membrane had no significant effect on the fine structure of the epithelium. At concentrations of DDISA of 10(-6) M or less, the baseline short-circuit current (SCC), and the response to cyclic 3',5'-adenosine monophosphate (cAMP) plus theophylline were unimpaired. At 10(-5) M, baseline SCC was unchanged and the response to cyclic AMP plus theophylline was enhanced. At concentrations of 10(-4) M and greater baseline SCC was depressed and the response to the nucleotide inhibited. The basal-lateral epithelial plasma membranes were labeled by exposing the serosal side to
pyridoxal phosphate
and reducing the resultant Schiff base with sodium borotritide (3H-NaBH1). In electron-microscopic autoradiographs, the silver grains (3H) were found over the basal and lateral surfaces of the epithelium. At concentrations of
pyridoxal phosphate
of 10(-4) M and 3H-NaBH1 of 10(-3) M, there were no significant changes in the fine structure of the epithelium. Addition of
pyridoxal phosphate
(10(-4) M) and NaBH4 (10(-3) M) to the serosal side decreased the baseline SCC significantly but not the response to
vasopressin
. Covalent attachment of the 125I and the 3H was indicated by resistance to elution in the preparation of the sections for electron-microscopy and the reagent requirements for binding.
...
PMID:Differential covalent labeling of apical and basal-lateral membranes of the epithelium of the toad bladder. 81 32