1983
DOI: 10.1016/0020-711x(83)90100-3
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The binding and degradation of 125I-labelled insulin by rat kidney brush-border membranes

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Cited by 8 publications
(5 citation statements)
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“…However, here we demonstrate a direct effect on the phospholipid metabolism, possibly mediated by active insulin receptors. This finding would suggest one metabolic role for papillary insulin receptors, which differs from the insulin degradating role attributed to the renal cortex receptors (Kurokawa et al 1979;Meezan and Freychet 1982;Talor, Emmanouel and Katz 1982;Thomas et al 1983;Meezan, Pillion and Elgavish 1988;Rabkin, Ryan and Duckworth 1984). The precise biochemical pathway by which insulin exerted its effect cannot be elucidated from these results.…”
Section: Discussionmentioning
confidence: 91%
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“…However, here we demonstrate a direct effect on the phospholipid metabolism, possibly mediated by active insulin receptors. This finding would suggest one metabolic role for papillary insulin receptors, which differs from the insulin degradating role attributed to the renal cortex receptors (Kurokawa et al 1979;Meezan and Freychet 1982;Talor, Emmanouel and Katz 1982;Thomas et al 1983;Meezan, Pillion and Elgavish 1988;Rabkin, Ryan and Duckworth 1984). The precise biochemical pathway by which insulin exerted its effect cannot be elucidated from these results.…”
Section: Discussionmentioning
confidence: 91%
“…The presence of specific high-affinity insulin receptors in both isolated renal glomeruli and tubules has been demonstrated (Kurokawa, Silverblatt, Klein, Wang and Lemer 1979;Meezan and Freychet 1982). Subsequently, it has been reported that purified renal tubular brush border and basolateral membrane have insulin receptors with similar binding properties (Talor, Emmanouel and Katz 1982;Thomas, Jenkins, Davey and Papachristodoulou 1983). More recently, it has been reported that insulin association with isolated renal brush border membrane vesicles almost totally represents low-affinity, high-capacity binding sites (Meezan, Pillion and Elgavish 1988).…”
Section: Introductionmentioning
confidence: 99%
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“…Luminal membranes degrade insulin at twice the rate that the contraluminal membranes do, and contain several peptidases, including a neutral metalloendopeptidase which degrades the isolated B chain of insulin but not intact insulin [31,55]. The isolated luminal membrane does not contain GIT activity [30] and does not produce intact A chains from insulin [20,58]. Thus, as a result of interacting with luminal membranes, insulin may be degraded by the membrane-associated neutral metalloendopeptidase, which, in concert with insulin protease, degrades insulin synergistically to trichloroacetic-acid-soluble products [31,55].…”
Section: Enzymatic Mechanisms Of Renal Insulin Degradationmentioning
confidence: 99%
“…Together, GIT and lysosomal proteases could catalyze the initial, specific and later, non-specific steps, respectively, of insulin degradation by proximal tubular cells. However, several studies have presented evidence that GIT plays, at best, a minor role in renal insulin degradation [2,30,58].…”
Section: Enzymatic Mechanisms Of Renal Insulin Degradationmentioning
confidence: 99%