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Conformation of Albumin Binding Sites are Disturbed in Schizophrenia

Published online by Cambridge University Press:  16 April 2020

M. Uzbekov ,
Y. Gryzunov ,
E. Misionzhnik ,
T. Syrejshchikova ,
G. Dobretsov ,
N. Smolina ,
T. Sokolova  and
A. Molodetskich
M. Uzbekov
Affiliation:
Research Institute of Psychiatry, Moscow, Russia
Y. Gryzunov
Affiliation:
Research Institute for Physical Chemical Medicine, Moscow, Russia
E. Misionzhnik
Affiliation:
Research Institute of Psychiatry, Moscow, Russia
T. Syrejshchikova
Affiliation:
Lebedev Physical Insitute, Moscow, Russia
G. Dobretsov
Affiliation:
Research Institute for Physical Chemical Medicine, Moscow, Russia
N. Smolina
Affiliation:
Research Institute for Physical Chemical Medicine, Moscow, Russia
T. Sokolova
Affiliation:
Research Institute of Psychiatry, Moscow, Russia
A. Molodetskich
Affiliation:
Research Institute of Psychiatry, Moscow, Russia

Abstract

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Aim:

Investigate some properties of albumin binding sites in schizophrenic patients.

Methods:

Properties of serum albumin binding sites were studied using quenching of fluorescence of probe K-35 (N-carboxyphenylimide of dimethylaminonaphthalic acid) with nitrate anion. Serum samples were collected from 24 schizophrenic patients and 24 healthy volunteers.

Results:

In the absence of quencher specific probe fluorescence in patients was 1,4 times higher than in controls. Fluorescent quenching constant for probe bound to albumin was 2,5 L/mol in patients versus 4,6 L/mol in volunteers (p< 0,01). Fluorescent fraction assessable to quenching was significantly lower in patients than in volunteers. Fluorescent decay studies on S-60 synchrotron have revealed in patient's albumin the redistribution between long-lived and short-lived molecules of the probe with increase of the latter. There were found decrease of albumin accessible SH-groups in schizophrenic patients as compared with volunteers.

Conclusions:

In schizophrenic patients conformational state of albumin binding sites is significantly disturbed that can lead to changes in protein-ligand interaction and to damage of main albumin functions (transport and detoxification) and aggravation of endotoxicosis.

Type
P03-210
Information
European Psychiatry , Volume 24 , Issue S1: 17th EPA Congress - Lisbon, Portugal, January 2009, Abstract book , January 2009 , 24-E1209
Copyright
Copyright © European Psychiatric Association 2009
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