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Biomedical subjects

R Zuckerman

Publications and source records attributed to R Zuckerman.

6 recordsLinked to original sources
PubMed1991

Long-term antimicrobial therapy in the prevention of recurrent soft-tissue infections.

Thirty-six patients who had suffered two or more episodes of erysipelas or cellulitis during the previous year were randomly divided into two equal groups; one group received erythromycin base 250 mg b.i.d. for 18 months, while the other group received no prophylaxis for a similar period. No patients in the treated group developed infection during the 18 months' follow-up but eight of the control group (50%) relapsed and required antibiotic treatment. Prolonged antimicrobial prophylaxis is effective and safe in preventing recurrent episodes of soft-tissue infections.

Cellulitis↗
PubMed1988

Sites of arrestin action during the quench phenomenon in retinal rods.

The target proteins for arrestin (48 kDa protein) action during the quench of cGMP phosphodiesterase (PDE) activation in retinal rod disk membranes were identified by the use of a cross-linking reagent. A heterobifunctional, cleavable, photo-activatable cross-linker (sulfo-SADP) was coupled to purified arrestin. Under precise weak visible light bleach and nucleotide conditions of quench, the cross-linker was UV flash-activated at a time when quench was well established. The target proteins covalently linked to arrestin by cross-linker activation were identified by immunoblotting. In the presence of ATP arrestin cross-linked to both PDE and rhodopsin during the quench phenomenon. Removal of ATP from the reaction mixture essentially abolished the cross-link with PDE, just as ATP omission abolishes quench, but significantly increased the cross-link to rhodopsin. The absence of a cross-link to the plentiful beta-subunit of transductin, as well as the results of competition studies employing arrestin without attached cross-linker, suggest that the observed cross-links are specific and reflect true binding interactions of arrestin during quench. The data are consistent with a model of quench in which photolyzed rhodopsin (R*) catalyzes the formation of an activated form of arrestin, which dissociates from R* in the presence of ATP, and binds to PDEs, thereby deactivating them.

3',5'-Cyclic-GMP Phosphodiesterases↗
PubMed1986

A 48 kDa protein arrests cGMP phosphodiesterase activation in retinal rod disk membranes.

Photolyzed rhodopsin (R) catalyzes GTP-binding to alpha-transducins (T alpha); T alpha X GTPs then activate cGMP phosphodiesterase (PDE). PDE activation is arrested by ATP in two ways: (i) initial velocity is suppressed, and (ii) PDE velocity rapidly returns to preactivation levels (turnoff). Arrestin (a 48 kDa protein) markedly enhances turnoff while not affecting initial velocity. Arrestin in the presence of ATP achieves rapid turnoff by directly inhibiting activated PDE, as indicated by its ability to inhibit the direct activation of PDE by T alpha X GMP--PNP (guanylyl-imidodiphosphate). Double reciprocal plots reveal a competition between arrestins and activated transducins for sites on PDE. Blocking R phosphorylation blocks initial velocity suppression but does not disturb rapid turnoff. Our data suggest a 2-fold mechanism for PDE deactivation: (i) formation of T alpha X GTPs is suppressed by R phosphorylation, while (ii) activation of PDE by T alpha X GTPs is competitively inhibited by arrestins when ATP is present.

3',5'-Cyclic-GMP Phosphodiesterases↗
PubMed1973

Ionic analysis of photoreceptor membrane currents.

1. Membrane current was derived from simultaneous measurements of interstitial ;dark' voltages and conductivities along the radial axis of frog photoreceptor cells. Membrane current was subsequently resolved into its component ionic currents or fluxes by means of ionic substitution and by the use of inhibitors of active transport.2. The plasma membrane of the frog rod outer segment was found to be permeable to Na(+) and Cl(-), with a ratio of Na(+) to K(+) permeabilities higher than that found in most neuronal cells. A net inward flux of 1.5 x 10(8) Na(+)/sec.rod flows across the outer segment plasma membrane in the dark.3. The proximal portion of the rod receptor, extending from the proximal region of the inner segment to the synaptic terminal, is mainly permeable to K(+), although some degree of Na(+) permeability is also presumed.4. A hyperpolarizing electrogenic Na pump was localized to the base of the outer segment and inner segment of the cell. The pump transfers at least 10(8) charges/sec out of the cell at this level, the pump current dividing and re-entering the cell at both the outer segment and proximal portion of the photoreceptor including the synaptic terminal.5. These findings have been incorporated into an ionic model of the photoreceptor, and its implications for cellular functioning considered.

Animals↗