[Conformational disturbances of serum albumin binding sites in schizophrenia].
The properties of serum albumin binding sites were studied using quenching of fluorescence of the molecular probe CAPIDAN (N-carboxyphenylimide of dimethylaminonaphthalic acid) with the nitrate anion. The samples of serum were obtained from 24 patients with paranoid schizophrenia and 24 healthy volunteers. In the absence of quencher the specific probe fluorescence was 1,4 times higher in patients than in volunteers. Fluorescence quenching constant for the probe bound to albumin was (M+/-m) 2,48+/-0,17 l/mol in patients versus 4,65+/-0,37 l/mol (p<0,01) in volunteers (p<0,01). The fluorescence fraction assessable to quenching was significantly (p<0,01) lower in schizophrenic patients as compared to controls (0,60+/-0,03 and 0,76+/-0,03) respectively). Thus, it is shown that in patients with schizophrenia the conformational state of albumin binding sites is significantly changed as compared to controls that can lead to the changes in the protein-ligand interaction and, thus, contribute to the pathogenesis of the disease and patient's response to treatment.
Uzbekov
M G
MG
Smolina
N V
NV
Misionzhnik
E Iu
EIu
Molodetskikh
A V
AV
Dobretsov
G E
GE
Gryzunov
Iu A
IuA
D000293:Adolescent; D000328:Adult; D001665:Binding Sites; D015415:Biomarkers / Q000097:blood; D005500:Follow-Up Studies; D006801:Humans; D008875:Middle Aged; D012563:Schizophrenia, Paranoid / Q000097:blood*; D012709:Serum Albumin / Q000378:metabolism*; D012720:Severity of Illness Index
D015415:Biomarkers; D012709:Serum Albumin