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

Harvard

Hansen, GH, Danielsen, EM, Sjöström, H & Norén, O 1989, 'Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity', European Journal of Cell Biology, bind 49, nr. 1, s. 154-61.

APA

Hansen, G. H., Danielsen, E. M., Sjöström, H., & Norén, O. (1989). Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity. European Journal of Cell Biology, 49(1), 154-61.

Vancouver

Hansen GH, Danielsen EM, Sjöström H, Norén O. Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity. European Journal of Cell Biology. 1989;49(1):154-61.

Author

Hansen, Gert Helge ; Danielsen, E M ; Sjöström, H ; Norén, Ove. / Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity. I: European Journal of Cell Biology. 1989 ; Bind 49, Nr. 1. s. 154-61.

Bibtex

@article{dc06df50e31111ddb5fc000ea68e967b,
title = "Organelles involved in the intracellular transport of newly synthesized aminopeptidase N and their acidity",
abstract = "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.",
author = "Hansen, {Gert Helge} and Danielsen, {E M} and H Sj{\"o}str{\"o}m and Ove Nor{\'e}n",
note = "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",
year = "1989",
language = "English",
volume = "49",
pages = "154--61",
journal = "Cytobiologie",
issn = "0724-5130",
publisher = "Elsevier GmbH - Urban und Fischer",
number = "1",

}

RIS

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