Binding of an aldose reductase inhibitor to renal glomeruli. 1985

M P Cohen, and H Klepser

The aldose reductase inhibitor Sorbinil affects several membrane-associated complexes including Na/K-ATPase activity, transport processes, and impulse propagation. These considerations, coupled with the drug's aromatic nature, suggested the possibility of direct interaction with cell membranes. In the present study, binding of [3H]-Sorbinil to isolated glomeruli was demonstrated. Binding is dose-dependent and saturable, and can be inhibited by increasing concentrations of unlabeled Sorbinil. These results may help explain the compound's diverse effects on membrane-associated processes.

UI MeSH Term Description Entries
D007093 Imidazoles Compounds containing 1,3-diazole, a five membered aromatic ring containing two nitrogen atoms separated by one of the carbons. Chemically reduced ones include IMIDAZOLINES and IMIDAZOLIDINES. Distinguish from 1,2-diazole (PYRAZOLES).
D007678 Kidney Glomerulus A cluster of convoluted capillaries beginning at each nephric tubule in the kidney and held together by connective tissue. Glomerulus, Kidney
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008297 Male Males
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D000449 Aldehyde Reductase An enzyme that catalyzes reversibly the oxidation of an aldose to an alditol. It possesses broad specificity for many aldoses. EC 1.1.1.21. Aldose Reductase,Aldose Reductase Ia,Aldose Reductase Ib,Erythrose Reductase,Xylose Reductase,Reductase Ia, Aldose,Reductase Ib, Aldose,Reductase, Aldehyde,Reductase, Aldose,Reductase, Erythrose,Reductase, Xylose
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013401 Sugar Alcohol Dehydrogenases Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99. Sugar Alcohol Oxidoreductases,Alcohol Dehydrogenases, Sugar,Alcohol Oxidoreductases, Sugar,Dehydrogenases, Sugar Alcohol,Oxidoreductases, Sugar Alcohol
D013402 Sugar Alcohols Polyhydric alcohols having no more than one hydroxy group attached to each carbon atom. They are formed by the reduction of the carbonyl group of a sugar to a hydroxyl group. (From Dorland, 28th ed) Alcohols, Sugar,Alditol,Sugar Alcohol,Alditols,Alcohol, Sugar

Related Publications

M P Cohen, and H Klepser
November 2010, Nihon rinsho. Japanese journal of clinical medicine,
M P Cohen, and H Klepser
January 1997, Neurobiology (Budapest, Hungary),
M P Cohen, and H Klepser
December 1995, The British journal of ophthalmology,
M P Cohen, and H Klepser
November 1992, Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology,
M P Cohen, and H Klepser
May 1988, Pharmaceutical research,
M P Cohen, and H Klepser
April 1986, Metabolism: clinical and experimental,
M P Cohen, and H Klepser
November 1997, Nihon rinsho. Japanese journal of clinical medicine,
M P Cohen, and H Klepser
April 1986, Metabolism: clinical and experimental,
M P Cohen, and H Klepser
November 1990, The American journal of physiology,
Copied contents to your clipboard!