PMID- 10567386
OWN - NLM
STAT- MEDLINE
DCOM- 19991229
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 48
DP  - 1999 Nov 26
TI  - Transglutaminase type 1 and its cross-linking activity are concentrated at
      adherens junctions in simple epithelial cells.
PG  - 34148-54
AB  - Transglutaminase type 1 was identified as a tyrosine-phosphorylated protein from 
      the isolated junctional fraction of the mouse liver. This enzyme was reported to 
      be involved in the covalent cross-linking of proteins in keratinocytes, but its
      expression and activity in other cell types have not been examined. Northern
      blotting revealed that transglutaminase type 1 was expressed in large amounts in 
      epithelial tissues (lung, liver, and kidney), which was also confirmed by
      immunoblotting with antibodies raised against mouse recombinant protein.
      Immunoblotting of the isolated junctional fraction revealed that transglutaminase
      type 1 was concentrated in the fraction not only as a 97-kDa form but also as
      forms of various molecular masses cross-linked to other proteins. In agreement
      with this finding, endogenous transglutaminase type 1 was immunofluorescently
      colocalized with E-cadherin in cultured simple epithelial cells. In the liver and
      kidney, immunoelectron microscopy revealed that transglutaminase type 1 was
      concentrated, albeit not exclusively, at cadherin-based adherens junctions.
      Furthermore, by in vitro and in vivo labeling, transglutaminase cross-linking
      activity was also shown to be concentrated at intercellular junctions of simple
      epithelial cells. These findings suggested that the formation of covalently
      cross-linked multimolecular complexes by transglutaminase type 1 is an important 
      mechanism for maintenance of the structural integrity of simple epithelial cells,
      especially at cadherin-based adherens junctions.
FAU - Hiiragi, T
AU  - Hiiragi T
AD  - Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku,
      Kyoto 606-8501, Japan.
FAU - Sasaki, H
AU  - Sasaki H
FAU - Nagafuchi, A
AU  - Nagafuchi A
FAU - Sabe, H
AU  - Sabe H
FAU - Shen, S C
AU  - Shen SC
FAU - Matsuki, M
AU  - Matsuki M
FAU - Yamanishi, K
AU  - Yamanishi K
FAU - Tsukita, S
AU  - Tsukita S
LA  - eng
SI  - GENBANK/AF186373
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Cadherins)
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (DNA, Complementary)
RN  - 0 (Phosphoproteins)
RN  - 0 (RNA, Messenger)
RN  - 21820-51-9 (Phosphotyrosine)
RN  - EC 2.3.2.13 (Transglutaminases)
RN  - EC 2.3.2.13 (transglutaminase 1)
SB  - IM
MH  - 3T3 Cells
MH  - Amino Acid Sequence
MH  - Animals
MH  - Blotting, Northern
MH  - Cadherins/metabolism
MH  - Cell Adhesion
MH  - Cell Line
MH  - Cross-Linking Reagents/*metabolism
MH  - DNA, Complementary/chemistry/genetics
MH  - Epithelial Cells/cytology/*metabolism
MH  - Gene Expression
MH  - Humans
MH  - Intercellular Junctions/*enzymology
MH  - L Cells
MH  - Liver/enzymology
MH  - Male
MH  - Mice
MH  - Microscopy, Confocal
MH  - Microscopy, Fluorescence
MH  - Molecular Sequence Data
MH  - Phosphoproteins/metabolism
MH  - Phosphotyrosine
MH  - RNA, Messenger/genetics/metabolism
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
MH  - Transglutaminases/genetics/*metabolism
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1074/jbc.274.48.34148 [doi]
AID - S0021-9258(19)53513-X [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 26;274(48):34148-54. doi: 10.1074/jbc.274.48.34148.