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Immunocytochemical detection of the microsomal glucose‐6‐phosphatase in human brain astrocytes
Author(s) -
Bell J. E.,
Hume R.,
Busuttil A.,
Burchell A.
Publication year - 1993
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.1365-2990.1993.tb00465.x
Subject(s) - glucose 6 phosphatase , glial fibrillary acidic protein , phosphatase , astrocyte , biology , enzyme , acid phosphatase , neuroglia , biochemistry , immunofluorescence , alkaline phosphatase , glycogen , endocrinology , medicine , central nervous system , antibody , immunohistochemistry , immunology
Using an antibody raised against the catalytic subunit of glucose‐6‐phosphatase, this enzyme was immuno‐localized in many astrocytes in 20 normal human brains. Double immunofluorescence studies showed co‐localization of glial fibrillary acidic protein (GFAP) with glucose‐6‐phosphatase in astrocytes. However, not all GFAP‐positive cells were also glucose‐6‐phosphatase positive, indicating that some astrocytes do not contain demonstrable expression of this enzyme. Reactive astrocytes in a variety of abnormal brains were strongly glucose‐6‐phosphatase positive, but neoplastic astrocytes were often only weakly positive. Expression of the enzyme could not be demonstrated in radial glia, neurons or oligodendroglia. Astrocytes normally contain glycogen and the demonstration that some astrocytes also contain glucose‐6‐phosphatase indicates that they are competent for both glycogenolysis and gluconeogenesis, which may be critical for neuronal welfare.