Monoclonal antibody evidence for structural similarities between the central rod regions of actinin and dystrophin.
A monoclonal antibody, MANDYS141, binds to both dystrophin and actinin on Western blots (SDS-denatured), but only to actinin in frozen sections of human muscle (native conformation). It differs from a polyclonal cross-reacting antiserum in that it binds to several muscle isoforms of actinin (smooth, fast and slow) from man, mouse and chicken and recognises a quite different part of the proposed triple-helical region of dystrophin (amino acids 1750-2248). The results suggest that structural homologies between actinin and dystrophin occur more than once in their central helical regions and provide experimental support for an actinin-like central rod model for dystrophin.
Research Division, NE Wales Institute, Deeside, Clwyd, UK.
T M
TM
Nguyen
J M
JM
Ellis
I B
IB
Ginjaar
M M
MM
van Paassen
G J
GJ
van Ommen
A F
AF
Moorman
A J
AJ
Cartwright
G E
GE
Morris
D000185:Actinin / Q000032:analysis* / Q000737:chemistry; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D015153:Blotting, Western; D002645:Chickens; D016189:Dystrophin / Q000032:analysis* / Q000737:chemistry; D000939:Epitopes / Q000276:immunology; D006801:Humans; D051379:Mice; D008856:Microscopy, Fluorescence; D008970:Molecular Weight; D009132:Muscles / Q000737:chemistry; D009137:Muscular Dystrophy, Animal / Q000378:metabolism
D000911:Antibodies, Monoclonal; D016189:Dystrophin; D000939:Epitopes; D000185:Actinin