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Endocytosis inhibitors abolish the active transport of polypeptides in the mucosa of the nasal upper concha of the rabbit

Authors :
Roberta Ghirardelli
Italo Caremi
Claudio Manzoni
Cristina Porta
Dario Cremaschi
Source :
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1280:27-33
Publication Year :
1996
Publisher :
Elsevier BV, 1996.

Abstract

An active absorption of polypeptides (elcatonin = CCT; adrenocorticotropic hormone) had been previously observed in the nasal respiratory mucosa of the rabbit. Its saturation kinetics and the parallel absence of a net transfer of other non-polypeptidic organic markers excluded the involvement of a simple pinocytosis. This absorption has been now better localized and further characterized. Unidirectional CCT fluxes (determined with radioimmunoassay) have been concomitantly monitored with transepithelial electric potential difference (Vms). Although the mucosae covering the ectoturbinal A and the lower and upper conchae displayed similar Vms, the active CCT transport was only evidenced in the upper concha. In this region cytochalasin B (which by disassembling actin microfilaments prevents the apical formation of vesicles in epithelial cells) and monensin (which prevents the split of the ligand-receptor complex in the endosomes) both eliminated the net CCT absorption, however, also permanently increasing the passive CCT junctional permeability. Aluminium fluoride (which prevents the fusion of endocytic vesicles into endosomes) and colchicine (which disrupts microtubules along which vesicles move in the cytoplasm) also permanently abolished net CCT transport, without affecting, or shortly and transiently affecting, passive permeability. On the whole these results are in favor of an active CCT transport supported by a specific vesicular transport.

Details

ISSN :
00052736
Volume :
1280
Database :
OpenAIRE
Journal :
Biochimica et Biophysica Acta (BBA) - Biomembranes
Accession number :
edsair.doi.dedup.....77e8f4f5cab50aa81a79f5280424673f
Full Text :
https://doi.org/10.1016/0005-2736(95)00263-4