Pregled bibliografske jedinice broj: 141384
Molecular response to TBT stress in marine sponge Suberites domuncula: proteolytical cleavage and phosphorylation of KRS_SD protein kinase
Molecular response to TBT stress in marine sponge Suberites domuncula: proteolytical cleavage and phosphorylation of KRS_SD protein kinase // Journal of Experimental Marine Biology and Ecology, 297 (2003), 2; 237-250 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 141384 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Molecular response to TBT stress in marine sponge Suberites domuncula: proteolytical cleavage and phosphorylation of KRS_SD protein kinase
Autori
Fafanđel, Maja ; Muller, Werner E.G. ; Batel, Renato
Izvornik
Journal of Experimental Marine Biology and Ecology (0022-0981) 297
(2003), 2;
237-250
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
KRS_SD; marine sponge; protein kinase; stress; Tributyl-tin
Sažetak
Marine sponges as sessile filter-feeders are inevitably under a constant influence of changes in their environment. Mediation of extracellular signals and regulation of cellular response to environmental stress is a key function of cellular protein kinases. Expression, proteolytical cleavage and phosphorylation of stress-responsive KRS_SD protein kinase, in control and tributyl-tin (TBT) treated sponges was investigated. In control sponge two KRS_SD proteins were expressed: KRS_SD1(54 kDa) corresponding to KRS_SD calculated molecular weight, and KRS-SD2 (50 kDa). Exposure of sponges to TBT resulted in alteration of KRS_SD1 and KRS_SD2 expression levels and their phosphorylation state. KRS_SD1 band disappearance after 4 hours coincides with the appearance of additional 35 kDa immunoreactive protein band (p35) and decrease in number of viable cells. Incubation of recombinant KRS_SD with protein extracts from TBT stressed sponges resulted in cleavage of recombinant KRS_SD protein. The size of the resulting protein fragment suggests caspase-3 recognition-site, present in both recombinant KRS_SD and KRS_SD, as a possible site of cleavage. Phosphorylated KRS_SD bands appear at the same time as p35 and remain after p35 band intensity reached control level. KRS_SD induction, its phosphorylation and proteolytical cleavage during TBT stress suggest that in sponge cells exist mechanism similar to one present in human cells where KRS/MST protein kinase is involved in promotion of apoptosis following oxidative stress.
Izvorni jezik
Engleski
Znanstvena područja
Geologija
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