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Aluminum inhibits neurofilament protein degradation by multiple cytoskeleton‐associated proteases
Author(s) -
Shea Thomas B.,
Balikian Philip,
Beermann Mary Lou
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80766-a
Subject(s) - proteases , cytoskeleton , chemistry , degradation (telecommunications) , microbiology and biotechnology , neurofilament , proteolysis , biochemistry , protein degradation , biophysics , enzyme , biology , cell , computer science , immunology , immunohistochemistry , telecommunications
The environmental neurotoxin aluminum exerts several distinct biochemical effects on neurofilament proteins, including subunit aggregation, disruption or the normal segregation of phosphorylated subunits within axons leading to abnormal perikaryal accumulation, and inhibition of in vitro degradation by the calcium‐dependent neutral protease, calpain. In the present study, we demonstrate that exposure of mouse CNS cytoskeletal preparations to aluminum chloride inhibits the degradation of neurofilament proteins by both calcium‐dependent and ‐independent proteases that co‐purify with cytoskeletons. Aluminum inhibited both calcium‐dependent and calcium‐independent proteolysis of the high and middle molecular weight neurofilament subunits, but inhibited only calcium‐dependent, and not calcium‐independent proteolysis of the low molecular weight neurofilament subunit. These findings demonstrate that aluminum interferes with multiple aspects or neurofilament protein metabolism.