An enzymically catalyzed incorporation of amines into proteins

Sarkar, Nirmal Kumar; Clarke, Donald D.; Waelsch, Heinrich

doi:10.1016/0006-3002(57)90512-7

Cited by 116 publications

(59 citation statements)

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“…TG2 is a calcium-dependent enzyme and represents the most ubiquitous isoform, being expressed in many organs. Since the discovery of TG2 in 1957, 7 a large number of its substrates have been identified in intracellular compartments as well as on the cell surface and in the extracellular matrix. 8,9 A peculiar aspect of TG2 biology is its multifunctionality, this being dictated by marked changes in the enzyme's 3-D structure.…”

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confidence: 99%

Transglutaminase 2 ablation leads to mitophagy impairment associated with a metabolic shift towards aerobic glycolysis

et al. 2014

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Macroautophagy selectively degrades dysfunctional mitochondria by a process known as mitophagy. Here we demonstrate the involvement of transglutaminase 2 (TG2) in the turnover and degradation of damaged mitochondria. In TG2-ablated cells we observed the presence of a large number of fragmented mitochondria that display decreased membrane potential, downregulation of IF1 along with increased Drp1 and PINK1 levels, two key proteins regulating the mitochondrial fission. Of note, we demonstrate that in healthy mitochondria, TG2 interacts with the dynamic proteins Drp1 and Fis1; interestingly, their interaction is largely reduced upon induction of the fission process by carbonyl cyanide m-chlorophenyl hydrazine (CCCP). In keeping with these findings, mitochondria lacking TG2 are more susceptible to CCCP treatment. As a consequence of accumulation of damaged mitochondria, cells lacking TG2 increased their aerobic glycolysis and became sensitive to the glycolytic inhibitor 2-deoxy-D-glucose (2-DG). In contrast, TG2-proficient cells are more resistant to 2-DG-induced apoptosis as the caspase 3 is inactivated through the enzyme's crosslinking activity. The data presented in this study show that TG2 plays a key role in cellular dynamics and consequently influences the energetic metabolism.

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confidence: 99%

Transglutaminase 2 ablation leads to mitophagy impairment associated with a metabolic shift towards aerobic glycolysis

et al. 2014

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“…substrate and enzyme protein are two different entities cannot be stated at present. The activity of the amide groups in amine incorporation may be of considerable biological significance as pointed out previously (1), not only as concerns the fixation and metabolism of biologically important amines but also because of t he possibility of the formation of modified proteins. The Ca++_activated liberation of ammonia from proteins supports the recent claim that some unassigned tissue ammonia originates in the amide groups of proteins (6) .…”

Section: Metabolic Activity Of Protein Amide Groupsmentioning

confidence: 94%

“…Recently an enzymically catalyzed, Ca++ -activated incorporation of aliphatic amines, such as cadaverine or ethanolamine, into a protein fraction of liver, kidney, and brain was described (1). To the list of amines acting as substrates for incorporation may now be added putrescine, spermine, and histamine which were tested as C 14 -labeled compounds.…”

Section: Metabolic Activity Of Protein Amide Groupsmentioning

confidence: 99%

“…The incorporation of spermine and putrescine suggests an explanation for the inhibition of cadaverine incorporation by these amines reported previously. In addition it was shown that ammonia acted as an inhibitor of cadaverine incorporation (1). Therefore, the incorporation of N 15 -ammonia into the protein fraction active in amine fixation was tested.…”

Section: Metabolic Activity Of Protein Amide Groupsmentioning

confidence: 99%

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Metabolic activity of protein amide groups

Clarke

Neidle

Sarkar

et al. 1957

Archives of Biochemistry and Biophysics

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“…Transglutaminase research started more than five decades ago when Waelsch and co-workers observed a Ca 2+ -dependent activity in liver extracts incorporating primary amines into proteins (Sarkar et al 1957;Mycek et al 1959). In the sixties there were two important developments.…”

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confidence: 99%

Polymorphism of transglutaminase 2: unusually low frequency of genomic variants with deficient functions

2011

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Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. These unusual multiple roles encoded into one polypeptide chain suggest that genomic variations in the TGM2 gene should be limited. Indeed, the available information in databases shows that unlike in the case of most other transglutaminases there are no common single nucleotide polymorphisms in exons of human TGM2. We collected data on and produced some of the rare genetic variants of TGM2 by site directed mutagenesis and found that some were less stable than the most abundant (wild type) enzyme variant and the majority had deficient transamidating activity. Further studies are required to clarify the pathologic significance of these rare TGM2 alleles in the human population.

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An enzymically catalyzed incorporation of amines into proteins

Cited by 116 publications

References 2 publications

Transglutaminase 2 ablation leads to mitophagy impairment associated with a metabolic shift towards aerobic glycolysis

Transglutaminase 2 ablation leads to mitophagy impairment associated with a metabolic shift towards aerobic glycolysis

Metabolic activity of protein amide groups

Polymorphism of transglutaminase 2: unusually low frequency of genomic variants with deficient functions

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