Anti-tubulin antibodies in a sensorimotor neuropathy patient alter tubulin polymerization.
The effect of anti-tubulin antibodies present in the serum of a patient with a progressive sensorimotor neuropathy on microtubule assembly was examined. The patient's serum was reactive on immunoblots with a single band of proteins of 55-kDa from homogenates of neural tissues. Tubulin was identified as the quantitatively major component of these 55-kDa proteins. Polymerization of tubulin in vitro was significantly enhanced by the patient's serum. A monoclonal antibody to nerve-specific class III beta-tubulin precisely duplicated the immunoreactive profile of the patient's serum, while an antibody to class (I + II) beta-tubulins also reacted with tubulins in non-neural tissues. The results indicate for the first time that human antisera reactive with nerve specific beta-tubulin can alter tubulin polymerization-depolymerization dynamics.
Stubbs
E B
EB
Neurology Service, Edward Hines, Jr. VA Hospital, Hines, IL 60141, USA. estubbs@orion.it.luc.edu
Fisher
M A
MA
Siegel
G J
GJ
D000368:Aged; D000918:Antibody Specificity; D001323:Autoantibodies / Q000097:blood*; D015417:Hereditary Sensory and Motor Neuropathy / Q000276:immunology* / Q000378:metabolism*; D006801:Humans; D007075:Immunoglobulin M / Q000097:blood; D008297:Male; D010525:Peripheral Nerves / Q000737:chemistry / Q000276:immunology / Q000473:pathology; D011108:Polymers; D014404:Tubulin / Q000276:immunology* / Q000378:metabolism*
D001323:Autoantibodies; D007075:Immunoglobulin M; D011108:Polymers; D014404:Tubulin