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Transglutaminase 3

transglutaminase 3, TGM3
Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Transglutaminase, CAN, HAIR, ACID, fibrillin-1
Papers on transglutaminase 3
The mouse wellhaarig (we) mutations result from defects in epidermal-type transglutaminase 3 (Tgm3).
King et al., New Britain, United States. In Mol Genet Metab, Nov 2015
This analysis restricted the location of we(4J) between sites that flank only one gene known to be expressed in skin: epidermal-type transglutaminase 3 (Tgm3).
Gene and miRNA expression changes in squamous cell carcinoma of larynx and hypopharynx.
Panda et al., Bengaluru, India. In Genes Cancer, Jul 2015
We found that matrix metalloproteinases along with SCEL, CRNN, KRT4, SPINK5, and TGM3 among others have significantly altered expression in these tumors.
Dietary Milk Sphingomyelin Prevents Disruption of Skin Barrier Function in Hairless Mice after UV-B Irradiation.
Sugawara et al., Odawara, Japan. In Plos One, 2014
Furthermore, significantly higher levels of loricrin and transglutaminase-3 mRNA were observed in the SM group.
Exploration of salivary proteins in buffalo: an approach to find marker proteins for estrus.
Gulyas et al., Tiruchchirāppalli, India. In Faseb J, 2014
On the whole, 37 proteins are exclusively expressed in the estrus phase, which include β-enolase, Toll-like receptor (TLR) 4, clusterin, lactoperoxidase, serotransferrin, TGM3, UBA6, and transducin.
Distinctive RNA expression profiles in blood associated with Alzheimer disease after accounting for white matter hyperintensities.
Sharp et al., Beijing, China. In Alzheimer Dis Assoc Disord, 2014
Regulated blood genes included MMP9, MME (Neprilysin), TGFβ1, CA4, OCLN, ATM, TGM3, IGFR2, NOV, RNF213, BMX, LRRN1, CAMK2G, INSR, CTSD, SORCS1, SORL1, and TANC2.
Germline sequence variants in TGM3 and RGS22 confer risk of basal cell carcinoma.
Stefansson et al., Reykjavík, Iceland. In Hum Mol Genet, 2014
We found new BCC susceptibility loci at TGM3 (rs214782[G], P = 5.5 × 10(-17), OR = 1.29) and RGS22 (rs7006527[C], P = 8.7 × 10(-13), OR = 0.77).
Hydrogen peroxide generated by DUOX1 regulates the expression levels of specific differentiation markers in normal human keratinocytes.
Shin et al., South Korea. In J Dermatol Sci, 2014
Knockdown of DUOX1 by RNA interference (RNAi) in NHKs significantly antagonized an increase of ionomycin-induced H2O2 level, and specifically decreased the expressions of several keratinocyte differentiation markers such as keratin 1, transglutaminase 3, desmoglein 1, and aquaporin 9.
Celiac disease as an autoimmune condition.
Deleanu et al., Cluj-Napoca / Kolozsvár, Romania. In Cent Eur J Immunol, 2013
Immune reactivity to tissue transglutaminase targeted autoantibodies and other autoantigens, including transglutaminase 3, actin, ganglioside, collagen, calreticulin or zonulin which have been reported in the celiac disease.
Potential therapeutic targets for oral cancer: ADM, TP53, EGFR, LYN, CTLA4, SKIL, CTGF, CD70.
Bisen et al., Gwalior, India. In Plos One, 2013
In all, 2365 genes were detected to be differentially expressed genes, which includes some of the highly differentially expressed genes like matrix metalloproteinases (MMP-1/3/10/13), chemokine (C-X-C motif) ligands (IL8, CXCL-10/-11), PTHLH, SERPINE1, NELL2, S100A7A, MAL, CRNN, TGM3, CLCA4, keratins (KRT-3/4/13/76/78), SERPINB11 and serine peptidase inhibitors (SPINK-5/7).
Dihydroisoxazole inhibitors of Anopheles gambiae seminal transglutaminase AgTG3.
Baxter et al., New Haven, United States. In Malar J, 2013
CONCLUSIONS: A targeted screen has identified chemical inhibitors of A. gambiae transglutaminase 3 (AgTG3).
Human hair shaft proteomic profiling: individual differences, site specificity and cuticle analysis.
Rice et al., Davis, United States. In Peerj, 2013
The cuticle also exhibited relatively high levels of epidermal transglutaminase (TGM3), accounting for its observed low degree of protein extraction by denaturants.
[Expression of TGM3 protein and its significance in laryngeal carcinoma].
Liu et al., Enshi, China. In Lin Chuang Er Bi Yan Hou Ke Za Zhi, 2012
The low expression of TGM3 may contribute to the carcinogenesis and development of laryngeal carcinoma.
Epidermal transglutaminase (TGase 3) is required for proper hair development, but not the formation of the epidermal barrier.
Smyth et al., Köln, Germany. In Plos One, 2011
Loss of Tgm3 is associated with defective hair development.
Recent advances in dermatitis herpetiformis.
Nakajima, Kōchi, Japan. In Clin Dev Immunol, 2011
Recent studies have demonstrated that IgA and antibodies against epidermal transglutaminase 3 play an important role in the pathogenesis of dermatitis herpetiformis.
Dermatitis herpetiformis sera or goat anti-transglutaminase-3 transferred to human skin-grafted mice mimics dermatitis herpetiformis immunopathology.
Meyer et al., Salt Lake City, United States. In J Immunol, 2011
TGM3 in immunoglobulin A (IgA) and TGM3 immune complexes is responsible for cross-linking and tight binding of IgA to connective tissue in the dermis and explains the IgA deposits in dermatitis herpetiformis skin long after signs of disease are resolved.
Gluten T cell epitope targeting by TG3 and TG6; implications for dermatitis herpetiformis and gluten ataxia.
Sollid et al., Oslo, Norway. In Amino Acids, 2010
findings lend credence to the notion that TG3 and TG6 are involved in the gluten-induced autoimmune responses of dermatitis herpetiformis and gluten ataxia
Identification of a preferred substrate peptide for transglutaminase 3 and detection of in situ activity in skin and hair follicles.
Hitomi et al., Nagoya, Japan. In Febs J, 2010
new information on the specific distribution of TGase 3
Autoantibodies in celiac disease.
Green et al., New York City, United States. In Autoimmunity, 2008
Immune reactivity to other autoantigens, including transglutaminase 3, actin, ganglioside, collagen, calreticulin and zonulin, among others, has also been reported in celiac disease.
The emerging structural understanding of transglutaminase 3.
Rastinejad et al., Bethesda, United States. In J Struct Biol, 2004
Transglutaminases (TGase; protein-glutamine: amine gamma-glutamyl-transferase) are a family of calcium-dependent acyl-transfer enzymes ubiquitously expressed in mammalian cells and responsible for catalyzing covalent cross-links between proteins or peptides.
A model for the reaction mechanism of the transglutaminase 3 enzyme.
Steinert et al., Bethesda, United States. In Exp Mol Med, 2003
Transglutaminase enzymes (TGases) catalyze the calcium dependent formation of an isopeptide bond between protein-bound glutamine and lysine substrates.
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