Transglutaminases: Protein Cross-Linking Enzymes in Tissues and Body Fluids

Aeschlimann, Daniel; Paulsson, Mats

doi:10.1055/s-0038-1642451

Cited by 486 publications

(431 citation statements)

References 138 publications

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“…The destabilase could be reasonably suggested to share homology with transglutaminases. But no math was found, even with the consensus sequence of transglutaminase active centers (YGQCWVFA [4]). …”

Section: The Destabilase Protein Its Precursor and Comparison With Omentioning

confidence: 99%

“…Isopeptide bonds between side chains of Gin and Lys, e-( !-Glu)-Lys, are formed by specific transglutaminases and are important in vital processes such as the final steps of blood coagulation [1][2][3][4]. The presence of transglutaminases in dix erse organisms, organs, tissues and body fluids has long suggested that natural isopeptidases that antagonize the action of t'ansglutaminases might also exist.…”

Section: Introductionmentioning

confidence: 99%

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Enzyme from the medicinal leech (Hirudo medicinalis) that specifically splits endo‐ϵ(‐γ‐Glu)‐Lys isopeptide bonds: cDNA cloning and protein primary structure

et al. 1996

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Earlier we detected a novel enzymatic activity in salivary gland secretion of the medicinal leech, splitting isopeptide bonds between the glutamine T-carboxamide and lysine E-amino group. This activity is due to destabilase. We described its partial amino acid sequence and sequences of two closely related cDNAs, but none of them perfectly matched the protein isolated. Here we report the isolation and sequence peculiarities of the third cDNA of the family as well as the complete sequence of the destabilase protein. The inferred mature protein product of this cDNA matches the independently determined destabilase protein sequence. It contains 115 amino acid residues including 14 highly conserved Cys residues and is formed from a precursor containing specific leader peptide.

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Section: The Destabilase Protein Its Precursor and Comparison With Omentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enzyme from the medicinal leech (Hirudo medicinalis) that specifically splits endo‐ϵ(‐γ‐Glu)‐Lys isopeptide bonds: cDNA cloning and protein primary structure

et al. 1996

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“…Key terms: Apoptosis, cell cycle, laser scanning cytometry, transglutaminase, protein cross-linking, hyperthermia, tumor necrosis factor, onconase, camptothecin, detergents Transglutaminases (TGases) catalyze transferring acyl groups from the ␣-carboxamide moiety of protein glutamines to the ⑀-amino groups of the same or another protein molecule. Thus, these Ca ϩ -activated enzymes cause intramolecular and/or intermolecular protein crosslinking, thereby altering their physicochemical structure and mechanical properties (1)(2)(3). The polyamines spermidine and spermine and their precursor, putrescine, are natural substrates for TGases.…”

mentioning

confidence: 99%

“…The cross-linking in this cell system generates the "cornified envelope" of keratinocytes, thereby ensur-ing their rigidity and resistance to mechanical and chemical stresses. Seven distinct TGases have been identified in humans (1)(2)(3)(4)(5)(6).…”

mentioning

confidence: 99%

Detection of in situ activation of transglutaminase during apoptosis: Correlation with the cell cycle phase by multiparameter flow and laser scanning cytometry

et al. 2002

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Background:One of the hallmarks of apoptosis is activation of tissue transglutaminase (Tgase; also called transglutaminase type 2 [TGase 2]). Its activation causes cross-linking of cytoplasmic proteins, making them insoluble and presumably less immunogenic. Several biochemical and cytochemical methods to detect activity of TGase 2 exist, but none has been adapted for multiparameter flow or image cytometry. Methods: Apoptosis of HL-60 or U-937 leukemic cells was induced by camptothecin, tumor necrosis factor ␣, hyperthermia, or the cytotoxic RNase onconase. Two different approaches to detect TGase 2 activation were developed: (a) the unfixed cells were treated with 4Ј,6Ј-diamidino-2-phenylindole, and sulforhodamine 101 in solutions of nonionic detergents; (b) the TGase 2 substrate fluoresceinated polyamine cadaverine (F-CDV) was administered into the cultures for several hours before cell harvesting. The cells were then fixed and their DNA counterstained with propidium. Cellular fluorescence was measured by flow or laser scanning cytometry. Results: (a) Exposure of nonapoptotic cells to detergents caused their full lysis, resulting in preparation of isolated nuclei devoid of cytoplasm. Conversely, the cross-linking of cytoplasmic protein by activated TGase 2 in apoptotic cells provided resistance to detergents: the nuclei or nuclear (chromatin) fragments of apoptotic cells remained

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“…[14][15][16] The TGases comprise a family of enzymes that catalyze the formation of isopeptide bonds between the g-carboxamide groups of peptidebound glutamine residues and the e-amino groups of lysine residues. [17][18][19][20] Seven diŠerent TGase gene products in higher animals have been characterized. 21) The primary structures of these TGases required for TGase and calcium binding activities are well conserved.…”

mentioning

confidence: 99%