Open AccessHydrolysis of myelin basic protein by polyclonal catalytic IgGs from the sera of patients with multiple sclerosis
Author(s) -
Polosukhina Darya I.,
Kanyshkova Tatyana G.,
Doronin Boris M.,
Tyshkevich Olga B.,
Buneva Valenti.,
Boiko Alexey N.,
Gusev Evgenii I.,
Favorova Olga O.,
Nevinsky Georgy A.
Publication year - 2004
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/j.1582-4934.2004.tb00325.x
Subject(s) - polyclonal antibodies , myelin basic protein , multiple sclerosis , hydrolysis , myelin , immunology , chemistry , antibody , biochemistry , medicine , central nervous system
Various catalytic antibodies or abzymes have been detected recently in the sera of patients with several autoimmune pathologies, where their presence is most probably associated with autoimmunization. Recently we have shown that DNase, RNase, and polysaccharide‐hydrolyzing activities are associated with IgGs from the sera of patients with multiple sclerosis (MS). Here we present evidence demonstrating that highly purified MS IgGs (but not Igs from the sera of healthy individuals) catalyze specifically hydrolysis of human myelin basic protein (hMBP). In contrast to many known proteases, IgGs do not hydrolyze many other different proteins. Specific inhibitors of acidic and thiol proteases have no remarkable effect on proteolytic activity of IgGs. However, specific inhibitor of serine (PMSF, AEBSF, and benzamidin) and metal‐dependent (EDTA) proteases significantly inhibit activity of proteolytic abzymes. Interestingly, the ratio of serine‐like and metal‐dependent activities of MS IgGs varied very much from patient to patient. The findings speak in favor of the generation by the immune systems of individual MS patients of a variety of polyclonal anti‐MBP IgGs with different catalytic properties.