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S L Slatin

Publications and source records attributed to S L Slatin.

22 records · Page 2Linked to original sources
PubMed1985

Channels formed by colicin E1 in planar lipid bilayers are large and exhibit pH-dependent ion selectivity.

The E1 subgroup (E1, A, Ib, etc.) of antibacterial toxins called colicins are known to form voltage-dependent channels in planar lipid bilayers. The genes for colicins E1, A and Ib have been cloned and sequenced, making these channels interesting models for the widespread phenomenon of voltage dependence in cellular channels. In this paper we investigate ion selectivity and channel size--properties relevant to model building. Our major finding is that the colicin E1 channel is large, having a diameter of at least 8 A at its narrowest point. We established this from measurements of reversal potentials for gradients formed by salts of large cations or large anions. In so doing, we exploited the fact that the colicin channel is permeable to both cations and anions, and its relative selectivity to them is a function of pH. The channel is anion selective (Cl- over K+) in neutral membranes, and the degree of selectivity is highly dependent on pH. In negatively charged membranes, it becomes cation selective at pH's higher than about 5. Experiments with pH gradients cross the membrane suggest that titratable groups both within the channel lumen and near the channel ends affect the selectivity. Individual E1 channels have more than one open conductance state, all displaying comparable ion selectivity. Colicins A and Ib also exhibit pH-dependent ion selectivity, and appear to have even larger lumens than E1.

Colicins↗
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

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↗