Polyamines stimulate D-glucose transport in isolated renal brush-border membrane vesicles.
Polyamines are natural constituents of most living organisms. However, their function in normal or pathological conditions is not fully understood. We have investigated in vitro effects of polyamines on characteristic properties of isolated renal brush-border membrane vesicles in order to determine whether polyamines have a regulatory role in membrane transport processes. The polyamines putrescine, spermidine and spermine were found to stimulate D-glucose uptake. Diffusional L-glucose uptake was not altered, indicating that the polyamines affected the active transport of D-glucose, rather than inducing nonspecific changes in membrane lipid properties. The amiloride-sensitive Na+ /H + exchange was slightly inhibited by polyamines while Mg2+ -ATPase activity was stimulated. The polyamine effects could not be explained solely by the polycationic properties of these agents, since polycationic polypeptides had an opposite effect. For example, lysozyme was found to inhibit D-glucose transport. Spermine was incorporated into the trichloroacetic acid-insoluble fraction of brush-border membrane proteins. Results indicated that this incorporation process consisted of at least two components: a Ca2+ -independent component and a Ca2+ -dependent component, possibly as a result of transglutaminase activity which was present in the isolated renal brush-border membranes. By using SDS-polyacrylamide gel electrophoresis in conjunction with fluorography, [3H]spermine was shown to be incorporated into several brush-border membrane proteins, mainly the 57 kDa, 74 kDa, 100 kDa, a heavy molecular weight band (greater than 200 kDa) and a low molecular weight band (less than 10 kDa). Our results suggest that the polyamine effects on membrane function may be due to a covalent modification of membrane proteins, possibly via a transglutaminase-mediated incorporation of polyamines or to the crosslinking of membrane proteins.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001693:Biological Transport, Active / Q000187:drug effects; D017301:Ca(2+) Mg(2+)-ATPase; D002118:Calcium / Q000494:pharmacology; D002352:Carrier Proteins / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D007687:Kidney Tubules, Proximal / Q000378:metabolism*; D008871:Microvilli / Q000378:metabolism; D011073:Polyamines / Q000494:pharmacology*; D011700:Putrescine / Q000494:pharmacology; D011817:Rabbits; D012964:Sodium / Q000378:metabolism; D017923:Sodium-Hydrogen Exchangers; D013095:Spermidine / Q000494:pharmacology; D013096:Spermine / Q000378:metabolism / Q000494:pharmacology
D002352:Carrier Proteins; D011073:Polyamines; D017923:Sodium-Hydrogen Exchangers; D013096:Spermine; D012964:Sodium; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D005947:Glucose; D002118:Calcium; D013095:Spermidine; D011700:Putrescine