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Ubiquitin and heat shock protein expression in amyotrophic lateral sclerosis
Author(s) -
GAROFALO O.,
KENNEDY P. G. E.,
SWASH M.,
MARTIN J. E.,
LUTHERT P.,
ANDERTON B. H.,
LEIGH P. N.
Publication year - 1991
Publication title -
neuropathology and applied neurobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.538
H-Index - 95
eISSN - 1365-2990
pISSN - 0305-1846
DOI - 10.1111/j.1365-2990.1991.tb00692.x
Subject(s) - haematoxylin , amyotrophic lateral sclerosis , ubiquitin , heat shock protein , glial fibrillary acidic protein , pathology , immunostaining , immunocytochemistry , antibody , biology , spinal cord , immunohistochemistry , microbiology and biotechnology , biochemistry , medicine , immunology , neuroscience , disease , gene
The expression of two heat shock proteins, HSP72 and p57, in addition to ubiquitin, has been studied immunocytochemically in nine amyotrophic lateral sclerosis (ALS) cases and 10 agematched controls. HSP72 and p57 antibodies did not identify the characteristic ubiquitinimmunoreactive inclusions present in anterior horn cells in ALS spinal cord. Antibodies to HSP72, but not to p57 or ubiquitin, strongly labelled structures corresponding to polyglucosan bodies in spinal grey matter. Such immunoreactive profiles were more abundant in ALS cases, although they were also present in control material. They were sometimes identified by haematoxylin and eosin and periodic acid Schiff reaction, but were not labelled by phosphotungstic acid haematoxylin or by antibodies to glial fibrillary acidic protein. Although ubiquitin, HSP72 and p57 are stress–induced proteins, they are expressed differently and might therefore have different significance in neuronal degeneration.