Prolactin signalling to milk protein secretion but not to gene expression depends on the integrity of the Golgi region

Autor: Michèle Ollivier-Bousquet, M. Lkhider, A. Aubourg, B. Petridou
Přispěvatelé: Unité de biologie cellulaire et moléculaire, Institut National de la Recherche Agronomique (INRA), ProdInra, Migration
Jazyk: angličtina
Rok vydání: 2001
Předmět:
endocrine system
Receptors
Prolactin
[SDV]Life Sciences [q-bio]
Gene Expression
Golgi Apparatus
Biology
In Vitro Techniques
03 medical and health sciences
chemistry.chemical_compound
symbols.namesake
0302 clinical medicine
Gene expression
STAT5 Transcription Factor
Animals
Lactation
Secretion
Breast
Carbon Radioisotopes
Phosphorylation
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
0303 health sciences
Arachidonic Acid
Brefeldin A
Secretory Vesicles
Cell Biology
Golgi apparatus
Milk Proteins
Prolactin
Endocytosis
Anti-Bacterial Agents
[SDV] Life Sciences [q-bio]
DNA-Binding Proteins
Secretory protein
Biochemistry
Transcytosis
chemistry
030220 oncology & carcinogenesis
symbols
Trans-Activators
Arachidonic acid
Female
Endoplasmic Reticulum
Rough
Macrolides
Rabbits
hormones
hormone substitutes
and hormone antagonists
Signal Transduction
Zdroj: Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2001, 114, pp.1883-1891
ISSN: 0021-9533
1477-9137
Popis: Prolactin added to the incubation medium of lactating mammary epithelial cells is transported from the basal to the apical region of cells through the Golgi region and concomitantly stimulates arachidonic acid release and protein milk secretion. We report that when PRL is added after disorganisation of the Golgi apparatus by brefeldin A treatment, prolactin signalling to expression of genes for milk proteins and prolactin endocytosis are not affected. However, prolactin transport to the apical region of cells (transcytosis), as well as prolactin-induced arachidonic acid release and subsequent stimulation of the secretion of caseins, which are located in a post-Golgi compartment, are inhibited. This inhibition was not a consequence of damage to the secretory machinery, as under the same conditions, protein secretion could be stimulated by the addition of arachidonic acid to the incubation medium. Thus, it is possible to discriminate between prolactin-induced actions that are dependent (signalling to milk protein secretion) or independent (signalling to milk gene expression) on the integrity of the Golgi apparatus. These results suggest that these two biological actions may be transduced via distinct intracellular pathways, and support the hypothesis that prolactin signals may be emitted at various cellular sites.
Databáze: OpenAIRE
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