The demonstration of cholinesterases by the formation of osmium blacks at the sites of Hatchett's brown

Hanker, Jacob S.; Thornburg, L. P.; Yates, Peggy E.; Moore, Horace G.

doi:10.1007/bf00304184

Cited by 73 publications

(19 citation statements)

References 33 publications

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“…5-a Wachsmuth et al, 1969), and the activity of LDH is contained mainly in the soluble fraction obtained by the cell fractionation technique. On the other hand, LDH of the liver was reported to be localized in the amorphous cytoplasm as well as in the mitochondria, when examined by the enzyme histochemical technique (Hecker, 1972;Hanker et al, 1973). Contrary to the reports mentioned above, LDH-M4 was found to exist in the nuclear fraction (Agostoni et al, 1966), and LDH-H4 was proven to be present in the nuclear fraction (Prokovsky et al, 1969).…”

Section: Localization Of Ldh Isozyme By the Immunohistochemical Technmentioning

confidence: 97%

“…Many attempts have been made to show the distribution of LDH in tissues by using enzyme histochemical methods (Fahimi et al, 1964;Wenzel et al, 1971;Hecker 1972;Hanker et al, 1973;Meijer, 1973). Furthermore, paying attention to the difference in heat stability and in resistance against inhibitor reagents among isozymes, the distribution pattern of each isozyme has been examined in heart, skeletal muscle and in kidney by enzyme histochemical methods (Kunge, 1967;McMillan, 1967;Tsygankov et al, 1971;Baba et al, 1971).…”

mentioning

confidence: 99%

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Immunohistochemical Study of Lactate Dehydrogenase Isozymes in Rat Liver

Yamashita

Yamamoto

Yasuda

1979

Acta Histochem. Cytochem

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Section: Localization Of Ldh Isozyme By the Immunohistochemical Technmentioning

confidence: 97%

mentioning

confidence: 99%

Immunohistochemical Study of Lactate Dehydrogenase Isozymes in Rat Liver

Yamashita

Yamamoto

Yasuda

1979

Acta Histochem. Cytochem

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“…Cortical cholinergic axons were visualized with the help of a highly sensitive AChE histochemical method. The principles of this method (incubation in a dilute Karnovsky-Roots medium followed by metal iondiaminobenzidine intensification) have been described by Hanker et al 40 and Tago et al 41 We have introduced a number of changes in this method as described elsewhere. 42 The specific inhibitor Iso-OMPA (Sigma Chemical Company, St. Louis, MO) was used to inhibit butyrylcholinesterase activity.…”

Section: Cholinesterase Histochemistrymentioning

confidence: 99%

Neuronal and Axonal Loss Are Selectively Linked to Fibrillar Amyloid-β within Plaques of the Aged Primate Cerebral Cortex

Shah

Lal

Leung

et al. 2010

The American Journal of Pathology

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The amyloid-␤ peptide (A␤) deposited in plaques in Alzheimer's disease has been shown to cause degeneration of neurons in experimental paradigms in vivo and in vitro. However, it has been difficult to convincingly demonstrate toxicity of native amyloid deposits in the aged and Alzheimer brains. Here we provide evidence that the fibrillar conformation of A␤ (fA␤) deposited in compact plaques is associated with the pathologies observed in Alzheimer brains. fA␤ containing compact but not diffuse plaques in the aged rhesus cortex contained activated microglia and clusters of phosphorylated tau-positive swollen neurites. Scholl's quantitative analysis revealed that the area adjacent to fA␤, containing compact but not diffuse plaques in aged rhesus, aged human, and Alzheimer's disease cortex, displays significant loss of neurons and small but statistically significant reduction in the density of cholinergic axons. These observations suggest that fA␤ toxicity may not be restricted to cultured cells and animal injection models. Rather, fA␤ deposited in native compact plaques in aged and AD brains may exert selective toxic effects on its surrounding neural environment.

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“…To evaluate this association, we determined the expression of AChE in several cell lines by employing a well-established cytochemical staining protocol 28 ± 32 upon induction of apoptosis with specific stimuli. This detection method was originally described by Karnovsky and Roots 28 for the demonstration of acetylcholinesterase (AChE) and modified by Hanker et al 31 and Kobayashi et al 30 It is specific for AChE 32 and has been widely used for years in detecting AChE activity in research and in clinical diagnosis of nerve disorders such as Hirschsprung's disease. 29,31 This protocol is based on the ability of acetylcholinesterase to catalyse the hydrolysis of acetylthiocholine, which contains a sulfur atom substituted for an oxygen in the ester linkage.…”

Section: Ache Activity Is Associated With Apoptosis Induction In Varimentioning

confidence: 99%

Induction of acetylcholinesterase expression during apoptosis in various cell types

et al. 2002

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Acetylcholinesterase (AChE) plays a key role in terminating neurotransmission at cholinergic synapses. AChE is also found in tissues devoid of cholinergic responses, indicating potential functions beyond neurotransmission. It has been suggested that AChE may participate in development, differentiation, and pathogenic processes such as Alzheimer's disease and tumorigenesis. We examined AChE expression in a number of cell lines upon induction of apoptosis by various stimuli. AChE is induced in all apoptotic cells examined as determined by cytochemical staining, immunological analysis, affinity chromatography purification, and molecular cloning. The AChE protein was found in the cytoplasm at the initiation of apoptosis and then in the nucleus or apoptotic bodies upon commitment to cell death. Sequence analysis revealed that AChE expressed in apoptotic cells is identical to the synapse type AChE. Pharmacological inhibitors of AChE prevented apoptosis. Furthermore, blocking the expression of AChE with antisense inhibited apoptosis. Therefore, our studies demonstrate that AChE is potentially a marker and a regulator of apoptosis.

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The demonstration of cholinesterases by the formation of osmium blacks at the sites of Hatchett's brown

Cited by 73 publications

References 33 publications

Immunohistochemical Study of Lactate Dehydrogenase Isozymes in Rat Liver

Immunohistochemical Study of Lactate Dehydrogenase Isozymes in Rat Liver

Neuronal and Axonal Loss Are Selectively Linked to Fibrillar Amyloid-β within Plaques of the Aged Primate Cerebral Cortex

Induction of acetylcholinesterase expression during apoptosis in various cell types

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