Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.

Yee, Vivien C.; Pedersen, Lars C.; Trong, I. Le; Bishop, Paul D.; Stenkamp, Ronald E.; Teller, David C.

doi:10.1073/pnas.91.15.7296

Cited by 337 publications

(333 citation statements)

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“…Transglutaminases (TGMs) form a family of structurally-and functionally related enzymes that posttranslationally modify proteins by catalyzing a Ca 21 -dependent transferase reaction between the ccarboxamide group of a peptide-bound glutamine residue and various primary amines (Yee et al, 1994). Nine distinctly expressed TGM genes are present in mammals (Fesus and Piacentini, 2002).…”

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confidence: 99%

Distribution of Transglutaminase 6 in the Central Nervous System of Adult Mice

Liu

Tang

Lan

et al. 2013

The Anatomical Record

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Our previous study identified a new form of spinocerebellar ataxia (SCA), in which mutations in the gene coding for transglutaminase 6 (TG6) were suggested to be causative. However, the data concerning cellular distribution of TG6 in the brain is still fragmentary. Therefore, we now report a comprehensive immunohistochemical examination of the expression profile of TG6 in adult mouse brain. TG6 was abundantly expressed in the septal region, basal ganglia, hypothalamus and brainstem. Notably, numerous TG6-positive neurons were found in the key brain regions involved in regulating locomotion activity, including the globus pallidus, subthalamic nucleus, substantia nigra, cerebellum, some precerebellar nuclei, and spinal motor neurons. Double immunostaining showed that the vast majority of TG6-positive neurons in the reticular nigra were GABAergic and those in the compact nigra were not dopaminergic. In addition, double staining for TG6 with either anti-NeuN or glial fibrillary acidic protein (GFAP) antibodies demonstrated exclusive NeuN-TG6 co-localization. This study presents a comprehensive overview of TG6 expression in the mouse brain, and provides insight for investigating the role of TG6 in the development of SCA. Anat Rec, 296:1576Rec, 296: -1587Rec, 296: , 2013. V C 2013 Wiley Periodicals, Inc.Key words: spinocerebellar ataxia; transglutaminase 6; immunohistochemistry; brain; distribution Abbreviations used: CNS 5 central nervous system; GABA 5 gammaaminobutyric acid; GAD67 5 glutamate acid decarboxylase 67; GFAP 5 glial fibrillary acidic protein; GFP 5 green fluorescent protein; NeuN 5 neuron specific nuclear protein; SCA 5 spinocerebellar ataxia; TGM 5 transglutaminase; TH 5 tyrosine hydroxylase.

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confidence: 99%

Distribution of Transglutaminase 6 in the Central Nervous System of Adult Mice

Liu

Tang

Lan

et al. 2013

The Anatomical Record

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“…They are calcium-dependent enzymes that contain an active site consisting of a catalytic triad (Cys, His, Asp) (3)(4)(5). The six different classes of transglutaminases are participating in a wide variety of physiological processes (3,6,7).…”

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confidence: 99%

Consequences of Seven Novel Mutations on the Expression and Structure of Keratinocyte Transglutaminase

Huber¹,

Yee²,

Burri³

et al. 1997

Journal of Biological Chemistry

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“…Therefore, assuming that a similar cysteine-based epoxide opening mechanism to that observed with FAS was present, molecular modelling was performed in order to deduce a likely binding pose for the pre-covalent attack complex of cerulenin within the FXIII-A active site and to also aid in the design of analogues. For these in silico studies, in the absence of a crystal structure of the activated form of the enzyme, a model of FXIII-A was created from the published zymogen crystal structure (1GGT.pdb) [4], by manually deleting the 'blocking' barrel domains (involving deletion of 229 residues between W500 -P729 inclusive) to reveal the active site. Cerulenin was then manually positioned into this active site model of FXIII-A.…”

Section: Resultsmentioning

confidence: 99%

“…Several crystal structures of human zymogen FXIII have been solved and consistently reveal the presence of a C314, H373, D396 triad [3]. Zymogen FXIII has no transglutaminase activity as the catalytic triad is buried deep in the core domain of the enzyme surrounded by two barrel domains, which block the entrance to the active site of the enzyme [4]. Conversion into the active transglutaminase (FXIII-A) is mediated by thrombin and Ca 2+ and involves a large conformational change, which removes the barrel domains from the core region thus allowing the substrates access to the active site [5].…”

Section: Introductionmentioning

confidence: 99%

(±) cis-bisamido epoxides: A novel series of potent FXIII-A inhibitors

Avery

Pease

Smith

et al. 2015

European Journal of Medicinal Chemistry

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A novel class of potent FXIII-A inhibitors containing a (±) cis-bisamido epoxide pharmacophore is described. The compounds display highly potent inhibition of FXIII-A (IC 50 = 5-500 nM) in an in vitro assay. In contrast to other types of previously described covalent transglutaminase inhibitors, the bis-amido epoxides exhibited no measurable reactivity with glutathione, therefore possibly rendering this class of compounds suitable for future in vivo investigations. Additionally, the compounds show selective inhibition for FXIII-A against the cysteine protease, cathepsin S although they proved to have similar potency with a closely related transglutaminase, TGII, to that observed for FXIII-A.

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Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII.

Cited by 337 publications

References 40 publications

Distribution of Transglutaminase 6 in the Central Nervous System of Adult Mice

Distribution of Transglutaminase 6 in the Central Nervous System of Adult Mice

Consequences of Seven Novel Mutations on the Expression and Structure of Keratinocyte Transglutaminase

(±) cis-bisamido epoxides: A novel series of potent FXIII-A inhibitors

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