A Role for Transglutaminase in Neurotransmitter Release by Rat Brain Synaptosomes

Pastuszko, Anna; Wilson, David F.; Erecińska, Maria

doi:10.1111/j.1471-4159.1986.tb12996.x

Cited by 63 publications

(31 citation statements)

References 38 publications

(39 reference statements)

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“…In other studies, TGase expression in human brain tissue has revealed that not only the expression of TGase 2 but of TGases 1 and TGases 3 are commonly found in stratified squamous epithelia [17,18]. In brain, TGase was demonstrated to be involved in various signal transduction pathways, particularly in the regulation of neurotransmitter release [19]. Our results agree with the presence of TGM3 and its important roles in mouse brain.…”

Section: Discussionsupporting

confidence: 82%

Transglutaminase 3 expression in C57BL/6J mouse embryo epidermis and the correlation with its differentiation

et al. 2005

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Epidermal-type transglutaminase 3 (TGM3) is involved in the cross-linking of structural proteins to form the cornified envelope in the epidermis. In the present study, we detected the expression of TGM3 in the mouse embryo using RT-PCR. TGM3 mRNA is weakly presented from E11.5 to E14.5 and increases significantly from E15.5 to birth. Then we determined the spatial and temporal expression pattern of TGM3 in the skin and other organs by in situ hybridization. We found a deprivation of TGM3 in skin at E11.5, while a rich supply in periderm cells and a weak expression in basal cells from E12.5 to E14.5. From the period of E15.5 to E16.5, after keratinization in the epidermis, TGM3 was expressed in the granular and cornified layers. The electron microscopic observation of the C57BL/6J mouse limb bud skin development provided several morphological evidences for the epidermal differentiation. The above findings suggest that the expression of TGM3 plays a important role in the epidermis differentiation in embryogenesis.

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Section: Discussionsupporting

confidence: 82%

Transglutaminase 3 expression in C57BL/6J mouse embryo epidermis and the correlation with its differentiation

et al. 2005

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“…Finally, tTGase has been suggested to play a role in neurotransmitter release from synaptosomes (43,44,55), crosslinking of neurofilaments, glial filaments and myelin basic protein (56), crosslinking of filaments into insoluble polymers during aging (57), and the formation of paired helical filaments in Alzheimer disease (57). [See Lorand (58) for a recent commentary.]…”

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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“…In all the experiments described above, we used a commercial preparation of tissue type transglutaminase (type II) purified from guinea pig liver. The brain contains the same enzyme (33) but also an uncharacterized transglutaminase associated with synaptic vesicles (34,35). Since the two brain transglutaminases may be different, we determined whether either could act on the DRPLA Q 12 peptide.…”

Section: Reactivity Of Model Fibronectin Peptide Containing Smallmentioning

confidence: 99%

Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system

Kahlem

Terré

Green

et al. 1996

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

185

132

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Many proteins contain reiterated glutamine residues, but polyglutamine of excessive length may result in human disease by conferring new properties on the protein containing it. One established property of a glutamine residue, depending on the nature of the flanking residues, is its ability to act as an amine acceptor in a transglutaminase-catalyzed reaction and to make a glutamyl-lysine cross-link with a neighboring polypeptide. To learn whether glutamine repeats can act as amine acceptors, we have made peptides with variable lengths of polyglutamine flanked by the adjacent amino acid residues in the proteins associated with spinocerebellar ataxia type 1 (SCA1), Machado-Joseph disease (SCA3), or dentato-rubral pallidoluysian atrophy (DRPLA) or those residues adjacent to the preferred cross-linking site of involucrin, or solely by arginine residues. The polyglutamine was found to confer excellent substrate properties on any soluble peptide; under optimal conditions, virtually all the glutamine residues acted as amine acceptors in the reaction with glycine ethyl-ester, and lengthening the sequence of polyglutamine increased the reactivity of each glutamine residue. In the presence of transglutaminase, peptides containing polyglutamine formed insoluble aggregates with the proteins of brain extracts and these aggregates contained glutamyl-lysine cross-links. Repeated glutamine residues exposed on the surface of a neuronal protein should form cross-linked aggregates in the presence of any transglutaminase activated by the presence of Ca 2؉ .

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A Role for Transglutaminase in Neurotransmitter Release by Rat Brain Synaptosomes

Cited by 63 publications

References 38 publications

Transglutaminase 3 expression in C57BL/6J mouse embryo epidermis and the correlation with its differentiation

Transglutaminase 3 expression in C57BL/6J mouse embryo epidermis and the correlation with its differentiation

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

Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system

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