γ‐Glutamylaminotransferase and Transglutaminase in Subcellular Fractions of Rat Cortex and in Cultured Astrocytes

Reichelt, Karl L.; Poulsen, Eystein

doi:10.1111/j.1471-4159.1992.tb09398.x

Cited by 33 publications

(7 citation statements)

References 31 publications

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“…Also in the previous studies, TGase activity was present ubiquitously in all the fractions of brain tissue, but at the synaptosomal fraction, the highest activity was detected (Gilad and Varon, 1985, Pastuszko et al, 1986, Korner and Bachrach, 1987, Reichelt and Poulsen, 1992, Campisi et al, 1992.…”

Section: Five Different Types Of Tgases From the Mammalian 181mentioning

confidence: 60%

Isolation and characterization of brain-specific transglutaminases from rat

Kwak

Kim²,

Kim³

et al. 1998

Exp Mol Med

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The relevance of transglutaminases with neural function and several disorders has been emphasized recently. Especially, many polypeptides associated with neurodegenerative diseases are suggested to be putative transglutaminase substrates such as amyloid protein of Altzheimer's disease, microtubule-associated proteins and neurofilaments, etc. In addition, the CAG repeated gene products with probable polyglutamine tract, putative transglutami-nase substrates, were identified in several neuro-degenerative disorders. However, the identity of the brain transglutaminase has not been confirmed, because of enzymic stability and low activity. In the present experiment, we have isolated brain-specific transglutaminases, designated as TGase NI and TGase NII, which are different from other types of transglutaminases in respects of molecular weights (mw. 45 kDa, 29 kDa respectively), substrate affinity, elution profile on ion-exchange chromatography, sensitivity to proteases and ethanol, and immuno-logical properties. The enzymes were localized specifically in the brain tissues but not in the liver tissue. And neural cells such as pheochromocytoma cell, glioma cell, primary neuronal and glial cells were shown to be enriched with TGase NI and TGase NII. The possible biological roles of the enzymes were discussed not only on the aspect of crosslinking activity but also of signal transducing capacity of the enzyme in the brain. K e y w o r d s : TGase NI, TGaase NII, brain, rat, localization

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Section: Five Different Types Of Tgases From the Mammalian 181mentioning

confidence: 60%

Isolation and characterization of brain-specific transglutaminases from rat

Kwak

Kim²,

Kim³

et al. 1998

Exp Mol Med

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“…A small amount of tTGase is present in brain relative to liver (41). The activity is present in synaptosomes (42) and astrocytes in culture (42). Brain contains two tTGases, one of which may be unique (43)(44)(45).…”

Section: Discussionmentioning

confidence: 99%

Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and α-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length

Cooper

Sheu

Burke

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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Several adult-onset neurodegenerative diseases are caused by genes with expanded CAG triplet repeats within their coding regions and extended polyglutamine (Q n ) domains within the expressed proteins. Generally, in clinically affected individuals n > 40. Glyceraldehyde 3-phosphate dehydrogenase binds tightly to four Q n disease proteins, but the significance of this interaction is unknown. We now report that purified glyceraldehyde 3-phosphate dehydrogenase is inactivated by tissue transglutaminase in the presence of glutathione S-transferase constructs containing a Q n domain of pathological length (n ‫؍‬ 62 or 81). The dehydrogenase is less strongly inhibited by tissue transglutaminase in the presence of constructs containing shorter Q n domains (n ‫؍‬ 0 or 10). Purified ␣-ketoglutarate dehydrogenase complex also is inactivated by tissue transglutaminase plus glutathione S-transferase constructs containing pathological-length Q n domains (n ‫؍‬ 62 or 81). The results suggest that tissue transglutaminase-catalyzed covalent linkages involving the larger poly-Q domains may disrupt cerebral energy metabolism in CAG͞Q n expansion diseases.

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“…Cellular TGascs have been lacalized and characterized in neuroblastomas (Piacentini et al, 1992;Maccioni andSeeds, 1986), gliomas (Komer andBackrach, 1985;Iwaki et al, 1994). and rat neuronal tissues (Facchiano et al, 1993;Hand et al, 1993b;Reichelt and Poulsen, 1992;Gilad and Varon, 1985). However, the localization and characterization of cellular E a s e in the human brain have not been demonstrated.…”

Section: -1427 19%)mentioning

confidence: 99%

Localization of transglutaminase in hippocampal neurons: implications for Alzheimer's disease.

Appelt¹,

Kopen²,

Boyne³

et al. 1996

J Histochem Cytochem.

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The purpose of this investigation was to identify and localize tissue transglutaminase (TGase) within neurons from the hippocampi of normal aged individuals and of those with confirmed Alzheimer's disease (AD). This enzyme may be a factor in the molecular mechanisms of neurodegeneration and formation of insoluble macromolecular complexes found in the neurons of normal aged and AD brain tissue. An antibody made to the extracellular TGase, coagulation factor XIIIa, was found to be specific for purified intracellular guinea pig liver tissue TGase. The specificity for liver tissue TGase has enabled us to identify tissue TGase(s) within rat hippocampal neurons and within neurons from normal aged and AD hippocampal tissues. Degenerating neurons from the AD hippocampus, compared to neurons from the normal aged hippocampus, exhibited increased immunoreactivity for TGase and demonstrated co-labeling for PHF1 and anti-TGase. Our results suggest that TGase may be associated with the neurofibrillary degeneration observed in AD, thereby implicating TGase as a potential factor in the pathogenesis of Alzheimer's disease.

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γ‐Glutamylaminotransferase and Transglutaminase in Subcellular Fractions of Rat Cortex and in Cultured Astrocytes

Cited by 33 publications

References 31 publications

Isolation and characterization of brain-specific transglutaminases from rat

Isolation and characterization of brain-specific transglutaminases from rat

Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and α-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length

Localization of transglutaminase in hippocampal neurons: implications for Alzheimer's disease.

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