Structure of the enterocyte transcytosis compartments during lipid absorption.


Journal

Histochemistry and cell biology
ISSN: 1432-119X
Titre abrégé: Histochem Cell Biol
Pays: Germany
ID NLM: 9506663

Informations de publication

Date de publication:
Jun 2020
Historique:
accepted: 04 02 2020
pubmed: 13 3 2020
medline: 15 12 2020
entrez: 13 3 2020
Statut: ppublish

Résumé

In spite of tremendous progress in deciphering the molecular mechanisms involved in intracellular transport in cell culture and in the test tube, many aspects of this process in situ remain unclear. Here, we examined lipid transcytosis in enterocytes in adult rats. Apical clathrin-coated buds and the ER exit sites were not found. After starvation, the Golgi complex was in a non-transporting state and contained many vesicles, but no intercisternal connections and typical the cis-most and the trans-most cisternae. Following the addition of the lipids in the form of chyme, pre-chylomicrons (pre-ChMs) were initially found in the tubules of the smooth SER attached to the basolateral plasmalemma below the belt composed of adhesive junctions (AJ) and always connected with other cisternae. However, the ER exit sites were still absent. Pre-ChMs moved into the cis-most cisterna and were concentrated in cisternal distensions at the trans-side of the Golgi complex. This induced attachment of the cis-most and the trans-most cisternae to the Golgi complex. Post-Golgi carriers fused with the basolateral plasmalemma and delivered ChMs outside. Overloading of enterocytes with lipids resulted in an accumulation of lipid droplets, an increase of the diameter of ChMs, and shift of the Golgi complex to the transporting state with the formation of intercisternal connections, attachment of the cis-most and the trans-most cisternae and disappearance of vesicles. These data are discussed from the functional point of view. In spite of tremendous progress in deciphering the molecular mechanisms involved in intracellular transport in cell culture and in the test tube, many aspects of this process in situ remain unclear. Here, we examined lipid transcytosis in enterocytes in adult rats. Apical clathrin-coated buds and the ER exit sites were not found. After starvation, the Golgi complex was in a non-transporting state and contained many vesicles, but no intercisternal connections and typical the cis-most and the trans-most cisternae. Following the addition of the lipids in the form of chyme, pre-chylomicrons (pre-ChMs) were initially found in the tubules of the smooth SER attached to the basolateral plasmalemma below the belt composed of adhesive junctions (AJ) and always connected with other cisternae. However, the ER exit sites were still absent. Pre-ChMs moved into the cis-most cisterna and were concentrated in cisternal distensions at the trans-side of the Golgi complex. This induced attachment of the cis-most and the trans-most cisternae to the Golgi complex. Post-Golgi carriers fused with the basolateral plasmalemma and delivered ChMs outside. Overloading of enterocytes with lipids resulted in an accumulation of lipid droplets, an increase of the diameter of ChMs, and shift of the Golgi complex to the transporting state with the formation of intercisternal connections, attachment of the cis-most and the trans-most cisternae and disappearance of vesicles. These data are discussed from the functional point of view.

Identifiants

pubmed: 32162136
doi: 10.1007/s00418-020-01851-3
pii: 10.1007/s00418-020-01851-3
doi:

Substances chimiques

Lipids 0

Types de publication

Comparative Study Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

413-429

Auteurs

Irina S Sesorova (IS)

Department of Anatomy, Ivanovo State Medical Academy, Ivanovo, Russia.

Natalia R Karelina (NR)

Department of Anatomy, Saint Petersburg State Paediatric Medical University, St. Petersburg, Russia.

Tatiana E Kazakova (TE)

Department of Anatomy, Ivanovo State Medical Academy, Ivanovo, Russia.

Seetharaman Parashuraman (S)

Institute of Protein Biochemistry, Consiglio Nazionale Delle Ricerche (CNR-IBP), Naples, Italy.

Maria A Zdorikova (MA)

Department of Anatomy, Ivanovo State Medical Academy, Ivanovo, Russia.

Ivan D Dimov (ID)

The FIRC Institute of Molecular Oncology, Via Adamello 16, 20139, Milan, Italy.

Elena V Seliverstova (EV)

Laboratory of Renal Physiology, Sechenov Institute of Evolutionary Physiology and Biochemistry of the Russian Academy of Sciences, Torez Avenue, 44, 194223, St. Petersburg, Russia.

Galina V Beznoussenko (GV)

The FIRC Institute of Molecular Oncology, Via Adamello 16, 20139, Milan, Italy. galina.beznusenko@ifom.eu.

Alexander A Mironov (AA)

The FIRC Institute of Molecular Oncology, Via Adamello 16, 20139, Milan, Italy. alexandre.mironov@ifom.eu.

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Classifications MeSH