Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity
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Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity. / Hansen, Gert Helge; Danielsen, E M; Sjöström, H; Norén, Ove.
I: European Journal of Cell Biology, Bind 49, Nr. 1, 1989, s. 154-61.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity
AU - Hansen, Gert Helge
AU - Danielsen, E M
AU - Sjöström, H
AU - Norén, Ove
N1 - Keywords: Aminopeptidases; Animals; Antigens, CD13; Cycloheximide; Exocytosis; Golgi Apparatus; Hydrogen-Ion Concentration; Jejunum; Lysosomes; Microscopy, Electron; Microvilli; Organ Culture Techniques; Organelles; Protein Synthesis Inhibitors; Swine
PY - 1989
Y1 - 1989
N2 - The intracellular routes taken by aminopeptidase N, an apically expressed enzyme in the enterocyte, was followed in small intestinal cultures of pig using either immunoelectron microscopy (immunogold labeling) or continuous labeling with [35S]methionine. Aminopeptidase N was found in the microvillar membrane, the Golgi complex, apical small smooth vesicles, and various acidic lysosomal/endosomal-like organelles. By culturing mucosal explants in the presence of either cycloheximide or (3-(2,4-dinitroanilino)-3-amino-N-methylpropylamine) (DAMP) it was demonstrated that the apical small smooth vesicles are exocytotic and that the low pH in the acid compartments is of no importance for intracellular transport and correct sorting of aminopeptidase N. Furthermore, our results show that the majority of the aminopeptidase N in the lysosomal/endosomal-like compartments is newly synthesized.
AB - The intracellular routes taken by aminopeptidase N, an apically expressed enzyme in the enterocyte, was followed in small intestinal cultures of pig using either immunoelectron microscopy (immunogold labeling) or continuous labeling with [35S]methionine. Aminopeptidase N was found in the microvillar membrane, the Golgi complex, apical small smooth vesicles, and various acidic lysosomal/endosomal-like organelles. By culturing mucosal explants in the presence of either cycloheximide or (3-(2,4-dinitroanilino)-3-amino-N-methylpropylamine) (DAMP) it was demonstrated that the apical small smooth vesicles are exocytotic and that the low pH in the acid compartments is of no importance for intracellular transport and correct sorting of aminopeptidase N. Furthermore, our results show that the majority of the aminopeptidase N in the lysosomal/endosomal-like compartments is newly synthesized.
M3 - Journal article
C2 - 2569397
VL - 49
SP - 154
EP - 161
JO - Cytobiologie
JF - Cytobiologie
SN - 0724-5130
IS - 1
ER -
ID: 9748481