Pregled bibliografske jedinice broj: 38116
Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract
Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract // American journal of physiology. Renal physiology, 278 (2000), 5; F717-F725 doi:10.1152/ajprenal.2000.278.5.F717 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 38116 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Tetanus toxin-mediated cleavage of cellubrevin inhibits proton secretion in the male reproductive tract
Autori
Breton, Sylvie ; Nsumu, Ndona N. ; Thierry, Galli ; Sabolić, Ivan ; Smith, Peter J.S. ; Brown, Dennis
Izvornik
American journal of physiology. Renal physiology (1931-857X) 278
(2000), 5;
F717-F725
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
vas deferens ; epididymis ; hydrogen-adenosine 3'5'-triphosphatase ; vesicle endocytosis ; soluble N-ethyl maleimide-sensitive factor for attachment protein receptors
Sažetak
Our laboratory has previously shown that the vacuolar H+-ATPase, located in a subpopulation of specialized cells establishes a luminal acidic environment in the epididymis and proximal part of the vas deferens (Breton S, Smith PSJ, Lui B, and Brown D. Nat Med 2:470-472, 1996). Low luminal pH is critical for sperm maturation and maintainance of sperm in a quiescent state during storage in these organs. In the present study we examined the regulation of proton secretion in the epididymis and vas deferens. In vivo microtubule disruption by colchicine induced an almost complete loss of H+-ATPase apical polarity. Endocytotic vesicles, visualized by Texas red-dextran internalization, contain H+-ATPase, indicating active endocytosis of the pump. Cellubrevin, an analog of the vesicle soluble N-ethyl maleimide-sensitive factor attachment protein (SNAP) receptor (v-SNARE) synaptobrevin, is highly enriched in H+-ATPase- rich cells of the epididymis and vas deferens, and tetanus toxin treatment markedly inhibited bafilomycin-sensitive proton secretion by 64.3 ą 9.0% in the proximal vas deferens. Western blotting showed effective cleavage of cellubrevin by tetanus toxin in intact vas deferens, demonstrating that the toxin gained access to cellubrevin in. These results suggest that H+- ATPase is actively endocytosed and exocytosed in proton-secreting cells of the epididymis and vas deferens and that net proton secretion requires the participation of the v-SNARE cellubrevin.
Izvorni jezik
Engleski
Znanstvena područja
Temeljne medicinske znanosti
POVEZANOST RADA
Projekti:
00220101
Ustanove:
Institut za medicinska istraživanja i medicinu rada, Zagreb
Profili:
Ivan Sabolić
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE