Transglutaminase activity is increased in Alzheimer's disease brain

Johnson, Gail V.W.; Cox, Teresa M.; Lockhart, Jason; Zinnerman, Marcus; Miller, Michael L.; Powers, Richard E.

doi:10.1016/s0006-8993(96)01431-x

Cited by 175 publications

(135 citation statements)

References 46 publications

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“…Tissue transglutaminase has been proposed to be implicated in a vast array of cellular processes, including the suppression of cell proliferation, differentiation, and signal transduction (30)(31)(32)(33)(34).…”

Section: Discussionmentioning

confidence: 99%

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

Cerchia

D’Alessio

Amabile

et al. 2006

Molecular Cancer Research

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Section: Discussionmentioning

confidence: 99%

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

Cerchia

D’Alessio

Amabile

et al. 2006

Molecular Cancer Research

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“…DISCUSSION Tissue TG has been shown to be both pro-and anti-apoptotic (15,16,21). Indeed tTG is increased both in conditions such as neurodegenerative disorders where there is increased cell death in specific brain regions (51)(52)(53), and in some tumors which are characterized by a lack of apoptosis (54,55). Therefore it is of critical importance to investigate the role of tTG in the process of apoptosis.…”

Section: The Interaction Of Ttg With Rb In the Nucleus Does Not Altermentioning

confidence: 99%

Intracellular Localization and Activity State of Tissue Transglutaminase Differentially Impacts Cell Death

Milaković

Tucholski

McCoy

et al. 2004

Journal of Biological Chemistry

118

141

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Tissue transglutaminase (tTG) is a unique member of the transglutaminase family as it is both a transamidating enzyme and a GTPase. In the cell tTG is mostly cytosolic, however it is also found in the nucleus and associated with the plasma membrane. tTG can be proapoptotic, however anti-apoptotic activities of the enzyme have also been reported. To determine how the intracellular localization and transamidating activity of tTG modulates its effects on apoptosis, HEK293 cells were transiently transfected with tTG or [C277S]tTG (which lacks transamidating activity) constructs that were targeted to different intracellular compartments. Apoptosis was induced by thapsigargin treatment, which results in increased intracellular calcium concentrations. Cytosolic tTG was pro-apoptotic, while nuclear localization of [C277S]tTG attenuated apoptosis. Membrane-targeted tTG had neither pro-nor anti-apoptotic functions. This finding indicates for the first time that intracellular localization is an important determinant of the effect of tTG on apoptosis. Previous studies have suggested that tTG may modulate retinoblastoma (Rb) protein, an important suppressor of apoptosis. tTG interacted with Rb and after induction of apoptosis, the interaction of nuclear-targeted [C277S]tTG with Rb was increased significantly concomitant with an attenuation of apoptosis. In contrast, the interaction of nucleartargeted tTG with Rb was significantly decreased and apoptosis was not attenuated. These data suggest that tTG protects cells against apoptosis in response to stimuli that do not result in increased transamidating activity by translocating to the nucleus, and that complexing with Rb may be an important aspect of the protective effects of tTG.

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“…In Alzheimer's disease (AD), tTGase catalyzes the cross-linking of neurofilament, amyloid precursor protein, tau, and non-A␤ component (29)(30)(31)(32). In addition, TGase activity and expression are elevated in affected areas of AD brains compared with normal controls (33). Studies have also stressed the role of tTGase in polyglutamine expansion neurodegenerative disorders such as Huntington's disease (HD).…”

Section: P Arkinson's Disease (Pd) Is a Neurodegenerative Disordermentioning

confidence: 99%

Tissue transglutaminase-induced aggregation of α-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies

Junn

Ronchetti

Quezado

et al. 2003

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

236

179

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Transglutaminase activity is increased in Alzheimer's disease brain

Cited by 175 publications

References 46 publications

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

An Autocrine Loop Involving Ret and Glial Cell–Derived Neurotrophic Factor Mediates Retinoic Acid–Induced Neuroblastoma Cell Differentiation

Intracellular Localization and Activity State of Tissue Transglutaminase Differentially Impacts Cell Death

Tissue transglutaminase-induced aggregation of α-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies

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