gp74 a membrane glycoprotein of the cis-Golgi network that cycles through the endoplasmic reticulum and intermediate compartment
Autor: | J Alcalde, G Egea, IV Sandoval |
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Přispěvatelé: | Universitat de Barcelona |
Rok vydání: | 1994 |
Předmět: |
Fluorescent Antibody Technique
Golgi Apparatus Cyclopentanes Metabolisme cel·lular Biology Endoplasmic Reticulum Kidney Cell Line Fluorides chemistry.chemical_compound symbols.namesake Microtubule Aparell de Golgi Reticle endoplasmàtic Organelle Animals Cis-Golgi network Aluminum Compounds Microscopy Immunoelectron Glycoproteins Organelles Protein Synthesis Inhibitors chemistry.chemical_classification Cell metabolism Brefeldin A Membrane Glycoproteins Endoplasmic reticulum Vesicle Temperature Antibodies Monoclonal Articles Cell Biology Golgi apparatus Rats Cell biology Molecular Weight Kinetics Biochemistry chemistry symbols Glycoprotein Glicoproteïnes |
Zdroj: | Dipòsit Digital de la UB Universidad de Barcelona Recercat. Dipósit de la Recerca de Catalunya instname The Journal of Cell Biology |
ISSN: | 1540-8140 0021-9525 |
DOI: | 10.1083/jcb.124.5.649 |
Popis: | A monoclonal antibody CC92 (IgM), raised against a fraction of rat liver enriched in Golgi membranes, recognizes a novel Endo H-resistant 74-kD membrane glycoprotein (gp74). The bulk of gp74 is confined to the cis-Golgi network (CGN). Outside the Golgi gp74 is found in tubulovesicular structures and ER foci. In cells incubated at 37 degrees C the majority of gp74 is segregated from the intermediate compartment (IC) marker p58. However, in cells treated with organelle perturbants such as low temperature, BFA, and [AIF4]- the patterns of the two proteins become indistinguishable. Both proteins are retained in the Golgi complex at 20 degrees C and in the IC at 15 degrees C. Incubation of cells with BFA results in relocation of gp74 to p58 positive IC elements. [AIF4]- induces the redistribution of gp74 from the Golgi to p58-positive vesicles and does not retard the translocation of gp74 to IC elements in cells treated with BFA. Disruption of microtubules by nocodazol results in the rapid disappearance of the Golgi elements stained by gp74 and redistribution of the protein into vesicle-like structures. The responses of gp74 to cell perturbants are in sharp contrast with those of cis/middle and trans-Golgi resident proteins whose location is not affected by low temperatures or [AIF4]-, are translocated to the ER upon addition of BFA, and stay in slow disintegrating Golgi elements in cells treated with nocodazol. The results suggest that gp74 is an itinerant protein that resides most of the time in the CGN and cycles through the ER/IC following the pathway used by p58. |
Databáze: | OpenAIRE |
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