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Distribution of the proximal tubule cell membrane proteins in control and colchicine treated rats (CROSBI ID 467760)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija

Baus, Mirela ; Međugorac Popovski, Mila ; Heršak, Eva ; Sabolić, Ivan Distribution of the proximal tubule cell membrane proteins in control and colchicine treated rats // Godišnji sastanak hrvatskih biokemicara, HB 98, Sažeci znanstvenih priopćenja / Glavaš-Obrovac, Ljubica (ur.). Zagreb: Hrvatsko biokemijsko društvo, 1998. str. 74-x

Podaci o odgovornosti

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

engleski

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

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.

microtubules; membrane proteins; kidney cortex; rat

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Podaci o prilogu

74-x.

1998.

objavljeno

Podaci o matičnoj publikaciji

Godišnji sastanak hrvatskih biokemicara, HB 98, Sažeci znanstvenih priopćenja

Glavaš-Obrovac, Ljubica

Zagreb: Hrvatsko biokemijsko društvo

Podaci o skupu

Godišnji sastanak hrvatskih biokemičara HB'98

poster

17.09.1998-20.09.1998

Bizovac, Hrvatska

Povezanost rada

Temeljne medicinske znanosti