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- W2080325723 abstract "The inositol 1,4,5‐trisphosphate (IP 3 )‐sensitive Ca 2+ store role of the secretory vesicles of adrenal medullary chromaffin cells is attributed to the presence of high capacity, low affinity Ca 2+ binding protein chromogranin A. Chromogranin A has recently been shown to interact with the protein component(s) on the intraluminal side of the secretory vesicle membrane at the intravesicular pH of 5.5 but to dissociate from them at the near physiological pH of 7.5. Further, one of the chromogranin A‐interacting membrane proteins was tentatively identified as the IP 3 receptor. Therefore, the pH‐dependent potential interaction of the intraluminal loop domains of the IP 3 receptor with chromogranin A was studied by analytical ultracentrifugation utilizing synthetic intraluminal loop peptides of the IP 3 receptor labeled with 5‐hydroxy‐tryptophan at the N‐terminus as a chromophore. One of the intraluminal loop domains was found to interact with chromogranin A at pH 5.5 but not at pH 7.5, suggesting the importance of the intraluminal loop domain in transmitting Ca 2+ mobilization signals to chromogranin A." @default.
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- W2080325723 date "1994-03-14" @default.
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- W2080325723 title "pH-dependent interaction of an intraluminal loop of inositol 1,4,5-trisphosphate receptor with chromogranin A" @default.
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- W2080325723 doi "https://doi.org/10.1016/0014-5793(94)80234-3" @default.
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