title: STIM1-regulated Ca2+ influx across the apical and the basolateral membrane in colonic epithelium.
abstract: In nonexcitable cells, store-operated Ca(2+) entry is the most important pathway for influx of extracellular Ca(2+) serving as a second messenger in the cytoplasm. The present study investigated the expression, localization and polar distribution of two key components of store-operated Ca(2+) entry identified, e.g., in lymphocytes or epithelial cell lines-STIM1 (stromal interacting molecule 1), working as a Ca(2+) sensor in the endoplasmic reticulum, and Orai1, working as the (or part of the) store-operated Ca(2+) channel in the plasma membrane-in a native intestinal epithelium, i.e., rat colon. Immunohistochemical investigations revealed expression of STIM1 and Orai1 in the rat colonic epithelium. Ca(2+) store depletion led to a translocation of STIM1 both to the basolateral as well as to the apical cell pole as observed by confocal microscopy. A Ca(2+) depletion/repletion protocol was used in Ussing chamber experiments to investigate the contribution of basolateral and apical store-operated Ca(2+) entry to the induction of anion secretion. These experiments revealed that Ca(2+)-dependent anion secretion was induced not only by basolateral Ca(2+) repletion but also, to a lesser extent, by apical Ca(2+) repletion. Both responses were suppressed by La(3+). The effect of basolateral Ca(2+) repletion was significantly inhibited by brefeldin A, a blocker of vesicular transport from the endoplasmic reticulum to the Golgi apparatus. In a final series of experiments, fura-2-loaded HT29/B6 cells were used. A carbachol-induced increase in the cytosolic Ca(2+) concentration was significantly reduced when cells were pretreated with siRNA against STIM1. In conclusion, these results demonstrate that STIM1 as a key component of intracellular Ca(2+) signaling is expressed by rat colonic epithelium and is involved in the regulation not only of basolateral but also of apical Ca(2+) influx.
authors: Institute for Veterinary Physiology and Biochemistry, Justus-Liebig-University, Giessen, Germany.
authors: Kaoru
authors: K
authors: Onodera
authors: Ervice
authors: E
authors: Pouokam
authors: Martin
authors: M
authors: Diener
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism*; D015220:Calcium Channels / Q000235:genetics / Q000378:metabolism; D045744:Cell Line, Tumor; D003106:Colon / Q000166:cytology / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D005260:Female; D019073:HT29 Cells; D006801:Humans; D007150:Immunohistochemistry; D008297:Male; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D000071740:ORAI1 Protein; D034741:RNA, Small Interfering; D051381:Rats; D017208:Rats, Wistar; D000071737:Stromal Interaction Molecule 1
chemical_list: D015220:Calcium Channels; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009363:Neoplasm Proteins; D000071740:ORAI1 Protein; C532493:Orai1 protein, rat; D034741:RNA, Small Interfering; C103530:STIM1 protein, human; C518857:Stim1 protein, rat; D000071737:Stromal Interaction Molecule 1; D002118:Calcium
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