Premium
Activation of Complement by Myelin: Identification of C1‐Binding Proteins of Human Myelin from Central Nervous Tissue
Author(s) -
Vanguri Padmavathy,
Shin Moon L.
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb01773.x
Subject(s) - myelin , immunostaining , blot , complement system , western blot , complement membrane attack complex , polyacrylamide gel electrophoresis , kilodalton , gel electrophoresis , biology , myelin basic protein , microbiology and biotechnology , chemistry , central nervous system , biochemistry , antibody , immunology , immunohistochemistry , neuroscience , enzyme , gene
Myelin isolated from central nervous tissue activates the classic pathway of complement by directly activating C1. Activation of C1 can proceed to form membrane attack complex, C5b‐9, in the myelin. Such an interaction between myelin and complement may be important in diseases involving myelin damage, in view of the role of complement in membrane attack and inflammation. To identify the C1‐activating protein, myelin was subjected to sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) and Western blot. The blots were incubated with C1 or with whole serum complement, followed by immunostaining for C1 or C3, respectively. A duplicate strip was stained with amido black or anti‐myelin antibody to visualize the myelin proteins. The results showed that two major protein bands were capable of activating C1. An approximately 56–58‐kilodalton band comigrated with the W2 protein and an approximately 45–47‐kilodalton band migrated along with, but slightly behind, the W1 Wolfgram doublet.