Biosynthesis of intestinal microvillar proteins. Low temperature arrests both processing and intracellular transport
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Biosynthesis of intestinal microvillar proteins. Low temperature arrests both processing and intracellular transport. / Danielsen, E M; Hansen, Gert Helge; Cowell, G M.
I: European Journal of Cell Biology, Bind 49, Nr. 1, 1989, s. 123-7.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Biosynthesis of intestinal microvillar proteins. Low temperature arrests both processing and intracellular transport
AU - Danielsen, E M
AU - Hansen, Gert Helge
AU - Cowell, G M
N1 - Keywords: Animals; Cells, Cultured; Cold Temperature; Intestinal Mucosa; Membrane Proteins; Microscopy, Electron; Microvilli; Organ Culture Techniques; Swine
PY - 1989
Y1 - 1989
N2 - The effect of culture at 20 degrees C on biosynthesis of microvillar enzymes was studied in pig small intestinal mucosal explants. At this temperature, aminopeptidase N (EC 3.4.11.2) and sucrase-isomaltase (EC 3.2.1.48-10) both accumulated intracellularly, predominantly in their transient, high mannose-glycosylated form characteristic of the newly synthesized enzymes prior to the molecular processing taking place in the Golgi complex. The general morphology of the enterocyte was unaffected by culture at low temperature except for the Golgi complex where the cisternae appeared condensed and surrounded by numerous vesicles of 50 to 55 nm. Both molecular processing and microvillar expression could be restored by shifting the temperature to 37 degrees C. Culture at low temperature did not induce any missorting of newly synthesized aminopeptidase N, but both molecular processing and microvillar expression only resumed at a slow rate after increasing the temperature, suggesting that reorganization of the Golgi complex is a time-requiring process.
AB - The effect of culture at 20 degrees C on biosynthesis of microvillar enzymes was studied in pig small intestinal mucosal explants. At this temperature, aminopeptidase N (EC 3.4.11.2) and sucrase-isomaltase (EC 3.2.1.48-10) both accumulated intracellularly, predominantly in their transient, high mannose-glycosylated form characteristic of the newly synthesized enzymes prior to the molecular processing taking place in the Golgi complex. The general morphology of the enterocyte was unaffected by culture at low temperature except for the Golgi complex where the cisternae appeared condensed and surrounded by numerous vesicles of 50 to 55 nm. Both molecular processing and microvillar expression could be restored by shifting the temperature to 37 degrees C. Culture at low temperature did not induce any missorting of newly synthesized aminopeptidase N, but both molecular processing and microvillar expression only resumed at a slow rate after increasing the temperature, suggesting that reorganization of the Golgi complex is a time-requiring process.
M3 - Journal article
C2 - 2759096
VL - 49
SP - 123
EP - 127
JO - Cytobiologie
JF - Cytobiologie
SN - 0724-5130
IS - 1
ER -
ID: 9748508