Naslov
Distribution of the proximal tubule cell membrane proteins in control and colchicine treated rats

Autori
Baus, Mirela ; Međugorac Popovski, Mila ; Heršak, Eva ; Sabolić, Ivan

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Godišnji sastanak hrvatskih biokemicara, HB 98, Sažeci znanstvenih priopćenja / Glavaš-Obrovac, Ljubica - Zagreb : Hrvatsko biokemijsko društvo, 1998

Skup
Godišnji sastanak hrvatskih biokemičara, HB 98

Mjesto i datum
Bizovac, Hrvatska, 17.09.1998. - 20.09.1998

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
microtubules; membrane proteins; kidney cortex; rat

Sažetak
The eukariotic cells establish, maintain, and modify their plasma membrane composition by the process of membrane recycling. In polarized cells, membrane components recycle between the specific plasma membrane (PM) domain and intracellular organelles by endo- and exocytosis. These processes depend on intact microtubules (MT) which serve as "tracks" for transporting vesicles that carry the membrane components toward the specific PM domain. In this work we investigated an effect of MT disruption by colchicine in rats in vivo on distribution of some proximal tubule (PT) cell PM proteins that are anchored in the membrane as ecto-, endo-, or transmembrane proteins. To disrupt MT, rats were treated with a single dose of colchicine (3.5 mg/kg B.M., i.p., 12 h before sacrifice). The cellular arrangement of MT, Na/K-ATPase a basolateral membrane (BLM) transmembrane protein, vacuolar proton ATPase V-ATPase, a brush-border membrane (BBM) endoprotein, sodium phosphate co-transporter type 2 (NaPi-2, a BBM transmembrane protein), and cell adhesion molecule CAM-105 (a BBM ectoprotein), was studied immunocytochemically in 4 m thick cryosections of the fixed kidney cortex by using the specific antibodies to these proteins. In the PT cells of colchicine-treated rats we found: a) disappearance of MT, b) marked loss of the V-ATPase and NaPi-2 from the BBM, and their redistribution in randomly scattered intracellular vesicles, and c) unchanged localization of the CAM-105 in the BBM and Na/K-ATPase in the BLM. We conclude that MT disruption affects transporters that exhibit rapid recycling and adaptation to changes in tubular load of the filtered substances (V-ATPase, NaPi-2), whereas the slowly-recycling membrane proteins (Na/K-ATPase, CAM-105) are not significantly affected by MT disruption.

Izvorni jezik
Engleski

Znanstvena područja
Temeljne medicinske znanosti

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