Pregled bibliografske jedinice broj: 93341
Variants of human serum esterases reacting with organophosphates, carbamates and pyridinium oximes
Variants of human serum esterases reacting with organophosphates, carbamates and pyridinium oximes // 4th International Chemical and Biological Medical Treatment Symposium (CBMTS IV) Spiez, Švicarska
Spiez, 2002. str. 44-44 (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 93341 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Variants of human serum esterases reacting with organophosphates, carbamates and pyridinium oximes
Autori
Simeon-Rudolf Vera ; Reiner, Elsa
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
4th International Chemical and Biological Medical Treatment Symposium (CBMTS IV) Spiez, Švicarska
/ - Spiez, 2002, 44-44
Skup
4th International Chemical and Biological Medical Treatment Symposium (CBMTS IV) Spiez
Mjesto i datum
Spiez, Švicarska, 28.04.2002. - 03.05.2002
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
butyrylcholinesterase; paraoxonase; genetic variants
Sažetak
Our studies on biochemical properties of genetic variants of butyrylcholinesterase (EC 3.1.1.8) and of paraoxonase (EC 3.1.8.1) in human sera are summarised with respect to possible individual and population differences concerning their interaction with organophosphates (OPs), carbamates or pyridinium oximes. Serum butyrylcholinesterase occurs as the usual, the atypical and several other genetic variants. Butyrylcholinesterase variants differ in their susceptibilities to positively charged organophosphates and carbamates. The atypical variant has a lower affinity for all positively charged compounds and therefore is a less efficient scavenger for these compounds than the usual enzyme. This property of the atypical butyrylcholinesterase is also unfavourable due to its lower affinity for the positively charged oximes PAM-2 and HI-6, used in the therapy after intoxication by OPs. However, individuals with homozygous atypical cholinesterase are very rare. Paraoxonase, the most extensively studied phosphoric triester hydrolase, has two genetic variants, one with low and the other with high catalytic activity for paraoxon and some other OPs. If exposed to OPs, individuals with low paraoxonase activity might be at risk. A higher incidence of low paraoxonase activity has been observed in patients with glucose and lipid metabolism disorders or renal failure. However, to predict the genetic predisposition of an individual to adverse effects of OPs not only esterases reacting with OPs, but the over all detoxification capacity should be examined.
Izvorni jezik
Engleski
Znanstvena područja
Temeljne medicinske znanosti
POVEZANOST RADA
Projekti:
00220104
Ustanove:
Institut za medicinska istraživanja i medicinu rada, Zagreb