PMID- 21984379
OWN - NLM
STAT- MEDLINE
DCOM- 20130617
LR  - 20211020
IS  - 1438-2199 (Electronic)
IS  - 0939-4451 (Print)
IS  - 0939-4451 (Linking)
VI  - 44
IP  - 1
DP  - 2013 Jan
TI  - Transglutaminase 6: a protein associated with central nervous system development 
      and motor function.
PG  - 161-77
LID - 10.1007/s00726-011-1091-z [doi]
AB  - Transglutaminases (TG) form a family of enzymes that catalyse various 
      post-translational modifications of glutamine residues in proteins and peptides 
      including intra- and intermolecular isopeptide bond formation, esterification and 
      deamidation. We have characterized a novel member of the mammalian TG family, 
      TG6, which is expressed in a human carcinoma cell line with neuronal 
      characteristics and in mouse brain. Besides full-length protein, alternative 
      splicing results in a short variant lacking the second beta-barrel domain in man and 
      a variant with truncated beta-sandwich domain in mouse. Biochemical data show that 
      TG6 is allosterically regulated by Ca(2+) and guanine nucleotides. Molecular 
      modelling indicates that TG6 could have Ca(2+) and GDP-binding sites related to 
      those of TG3 and TG2, respectively. Localization of mRNA and protein in the mouse 
      identified abundant expression of TG6 in the central nervous system. Analysis of 
      its temporal and spatial pattern of induction in mouse development indicates an 
      association with neurogenesis. Neuronal expression of TG6 was confirmed by 
      double-labelling of mouse forebrain cells with cell type-specific markers. 
      Induction of differentiation in mouse Neuro 2a cells with NGF or dibutyryl cAMP 
      is associated with an upregulation of TG6 expression. Familial ataxia has 
      recently been linked to mutations in the TGM6 gene. Autoantibodies to TG6 were 
      identified in immune-mediated ataxia in patients with gluten sensitivity. These 
      findings suggest a critical role for TG6 in cortical and cerebellar neurons.
FAU - Thomas, Helen
AU  - Thomas H
AD  - Matrix Biology and Tissue Repair Research Unit, School of Dentistry, Cardiff 
      University, Heath Park, Cardiff CF14 4XY, UK.
FAU - Beck, Konrad
AU  - Beck K
FAU - Adamczyk, Magdalena
AU  - Adamczyk M
FAU - Aeschlimann, Pascale
AU  - Aeschlimann P
FAU - Langley, Martin
AU  - Langley M
FAU - Oita, Radu C
AU  - Oita RC
FAU - Thiebach, Lars
AU  - Thiebach L
FAU - Hils, Martin
AU  - Hils M
FAU - Aeschlimann, Daniel
AU  - Aeschlimann D
LA  - eng
SI  - GENBANK/AF540969
SI  - GENBANK/AF540970
SI  - GENBANK/AY159126
SI  - GENBANK/AY177606
SI  - GENBANK/AY177607
GR  - 18461/Arthritis Research UK/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20111008
PL  - Austria
TA  - Amino Acids
JT  - Amino acids
JID - 9200312
RN  - 0 (Coenzymes)
RN  - 0 (Nucleotides)
RN  - EC 2.3.2.13 (TGM6 protein, human)
RN  - EC 2.3.2.13 (Transglutaminases)
SB  - IM
MH  - Animals
MH  - Catalytic Domain
MH  - Cell Differentiation
MH  - Cell Line
MH  - Central Nervous System/cytology/*embryology/*physiology
MH  - Coenzymes
MH  - Evolution, Molecular
MH  - Gene Expression
MH  - Gene Expression Regulation, Developmental
MH  - Humans
MH  - Kinetics
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Neurons/enzymology/*physiology
MH  - Nucleotides/chemistry
MH  - Organ Specificity
MH  - Protein Binding
MH  - Protein Structure, Secondary
MH  - Substrate Specificity
MH  - Transglutaminases/antagonists & inhibitors/*genetics/metabolism
PMC - PMC3535377
EDAT- 2011/10/11 06:00
MHDA- 2013/06/19 06:00
PMCR- 2011/10/08
CRDT- 2011/10/11 06:00
PHST- 2011/06/28 00:00 [received]
PHST- 2011/09/16 00:00 [accepted]
PHST- 2011/10/11 06:00 [entrez]
PHST- 2011/10/11 06:00 [pubmed]
PHST- 2013/06/19 06:00 [medline]
PHST- 2011/10/08 00:00 [pmc-release]
AID - 1091 [pii]
AID - 10.1007/s00726-011-1091-z [doi]
PST - ppublish
SO  - Amino Acids. 2013 Jan;44(1):161-77. doi: 10.1007/s00726-011-1091-z. Epub 2011 Oct 
      8.