Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 3

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

Search:
in the keywords:  CYSTEINE
help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1
Content available remote

Oxidative DNA damage and level of thiols as related to polymorphisms of MTHFR, MTR, MTHFD1 in Alzheimer's and Parkinson's diseases

100%
Dorszewska J., Florczak J., Rozycka A., Kempisty B., Jaroszewska-Kolecka J., Chojnacka K., Trzeciak W. H., Kozubski W.
Acta Neurobiologiae Experimentalis
|
2007
|
vol. 67
|
issue 2
113-129
EN
Neurodegenerative diseases, such as Alzheimer's disease (AD) and Parkinson's disease (PD), are accompanied by increased levels of 8-oxo-2'-deoxyguanosine (8-oxo2dG) and alterations in levels of homocysteine (Hcy), methionine (Met), and cysteine (Cys). Hcy may undergo remethylation due to involvement of MTHFR, MTR and MTHFD1 proteins. Present studies are aimed at determination of 8-oxo2dG, Hcy, Met, and Cys in AD and PD patients as well as in control groups, using HPLC/EC/UV, as well as estimation, by restriction analysis, frequency of following gene polymorphisms: MTHFR (C677T, A1298C, G1793A), MTHFD1 (G1958A), and MTR (A2756G). In AD there were significant differences of the levels of only Cys (GG, MTHFR, G1793A) and Met/Hcy (AA, MTHFD1, G1958A) whereas in PD there were more significant differences of the levels of thiols: Hcy [MTHFR: CT (C677T) and GG (G1793A); MTR, AG (A2756G)], Met [MTR, AA (A2756G)], Cys [MTR, AG (A2756G)], and Met/Hcy [MTHFR: CC, CT (C677T) and AA (A1298C), and GG (G1793A); MTHFD1 AA(G1958A); MTR AA(A2756G)]. Significant differences in the levels of Cys/Hcy, MTHFD1 GA (G1958) were varied between AD and PD groups. The results indicate that of the enzymes studied only polymorphisms of folate-dependent enzyme MTHFD1 have pointed to significant differences in intensity of turnover of circulating thiols between AD and PD patients.
2

Influence of cysteine on mechlorethamine-induced chromosomal aberrations in cultured human lymphocytes

86%
Blaszczyk A.
Journal of Applied Genetics
|
1995
|
vol. 36
|
issue 4
389-393
EN
The aim of the present paper was to find out by in vitro chromosomal aberration test using human lumphocytes whether cysteine has anticlastogenic properties towards a well-known mutagen - mechlorethamine.The lymphocytes tested were obtained rom three healthy donors.Two doses of cysteine and three doses of mechlorethamine were tested.It was found that cysteine had anticlastogenic properites and that it reduced the number of mrthaphase with chromosomal aberrations induced by mechlorethamine.
3

The effect of cAMP and some sulphur compounds upon the activity of mercaptopyruvate sulphurtransferase and rhodanese in mouse liver

86%
Wrobel M., Frendo J.
|
1992
|
vol. 40
|
issue 1-2
11-14
EN
The aim of the experiments was to evaluate the effect of administration of cysteine, methionine, thiocystine, and thiosulphate upon the activity of mercaptopyruvate sulphurtransferase (MPST) and rhodanese in mouse liver. It was found that rhodanese activity increased following thiocystine and methionine administration and showed a smaller increase after cysteine and thiosulphate. The MPST activity significantly increased after cysteine and to a lesser extent after thiocystine and thiosulphate. On the other hand, methionine seemed to exert no effect upon the enzymatic activity. The results suggested that methionine metabolic cycle in mouse liver proceeded from cysteine to sulphane sulphur as thiocystine and, therefore, these three compounds increased rhodanese activity. Thiosulphate seemed rather to be involved in metabolic changes related to maintaining the stability of the physiological thiosulphate level and activated both the enzymes.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.