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Biomedical subjects

I M Reich

Publications and source records attributed to I M Reich.

8 recordsLinked to original sources
PubMed1981

Insulin-induced proteins in the toad urinary bladder.

Insulin increases active sodium transport by the toad urinary bladder within 15 min, an effect which persists for an least 20 h. In tissues pre-treated with inhibitors of transcription or translation, sodium transport briefly increases after insulin addition but returns to basal levels within 60-90 min. We have studied the effects of insulin on the incorporation of radioactive amino acids into mucosal cell proteins. Insulin had no detectable effect on the uptake of amino acids nor on their incorporation into total protein; however, using a dual label technique, we found that insulin increases the incorporation of amino acids into specific soluble and plasma membrane proteins of the granular mucosal cell. The time course and dose-response relationship of the induction of protein synthesis by insulin suggest that these proteins may play a role in the sustained elevation of sodium transport by insulin.

Amino Acids↗
PubMed1981

Mechanisms of hormonal modulation of ion transport in the toad's urinary bladder. Subcellular localization of aldosterone-induced proteins.

A dual-label isotope technique was used to study the effects of aldosterone upon the incorporation of amino acids into proteins of the in vitro toad urinary bladder. Following labeling, the mucosal cells were disaggregated and the mitochondria-rich and granular cells were separated. Proteins with an elevated isotope ratio were found in a plasma membrane fraction (170 000, 110 000 and 85 000 daltons) and in the cytosol (36 000 and 6 000 daltons) of the preparations enriched in mitochondria-rich cells. These effects of aldosterone were blocked by cycloheximide. There was no evidence that aldosterone had induced the incorporation of labeled amino acids into carbonic anhydrase isolated from the soluble fraction by affinity chromatography. The results suggest that the physiologic response of the toad bladder to aldosterone is related to the synthesis of both soluble and plasma membrane proteins.

Aldosterone↗
PubMed1981

Insulin-induced alterations in the lactoperoxidase-catalyzed radioiodination of membrane proteins of the toad bladder epithelium.

Insulin-stimulated sodium transport in the toad urinary bladder consists of two components, a brief element of rapid onset that is independent of protein synthesis, and a sustained increase, slower in onset, that is dependent upon RNA and protein synthesis. The mucosal epithelium of the toad bladder was labeled by lactoperoxidase-catalyzed radioiodination (125I) following 15 min and 3 h exposure to insulin. The membrane of "mitochondria-rich" and "granular" mucosal cells from these tissues were analyzed by electrophoresis in SDS-urea. Compared to untreated tissues, membranes of "granular" mucosal cells from tissues exposed to insulin for 15 min contained a band (Mr = 15,000) with significantly increased labeling. Bladders exposed to insulin for 3 h showed no consistent increase in labeling. These data suggest that there are differences in the conformation of apical membrane proteins during the two phases of hormone-induced sodium transport. The technique may also offer an opportunity to identify "effector" proteins mediating this and other insulin responses.

Animals↗
PubMed1979

Inhibition of fatty acid synthesis prevents the incorporation of aldosterone-induced proteins into membranes.

2-Methyl-2-[p-(1,2,3,4-tetrahydro-1-naphthyl)phenoxy]propionic acid (TPIA), an acetyl coenzyme A carboxylase inhibitor, blocks the aldosterone-induced increase in transepithelial sodium transport. To examine the requirement for ongoing fatty acid synthesis and/or elongation in the aldosterone-induced alteration of cellular protein metabolism in the toad's urinary bladder, the effect of TPIA has been examined in double-labeled amino acid incorporation experiments. TPIA itself has no effect on the pattern of protein labeling in either the "soluble" or a plasma membrane-enriched fraction. However, inhibition of fatty acid synthesis selectively inhibits the aldosterone-induced incorporation of membrane proteins without altering the labeling of soluble cell protein. These results indicate that ongoing fatty acid synthesis is required for the hormone-induced changes in plasma membrane protein metabolism.

Aldosterone↗
PubMed1978

Comparison of toad bladder aldosterone-induced proteins and proteins synthesized in vitro using aldosterone-induced messenger RNA as template.

Using double-labeled isotope techniques, it can be shown that aldosterone induces the synthesis of several proteins in the mitochondria-rich (MR) cells of the toad's urinary bladder. Induced proteins have been identified both in the plasma membrane (mol wt = 170,000, 85,000 and 12,000) and the cytosol (mol wt = 36,000, 12,000 and 6,000) fractions of these mucosal cells. We have also shown that aldosterone (Aldo) induces the synthesis of a class of RNA having the properties of messenger RNA (mRNA). mRNA isolated from Aldo-treated mucosal cells was used as template in a cell-free protein-synthesis system prepared from rabbit reticulocytes. Preparations charged with mRNA from Aldo-treated cells synthesized two proteins that were not labeled when mRNA from control tissues was used as template. The electrophoretic mobility of one of these proteins was similar to an Aldo-induced membrane protein (mol wt = 70,000) found in the intact tissue.

Aldosterone↗