Identification of human salivary transglutaminases

Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with t...

Full description

Saved in:
Bibliographic Details
Published in:Amino acids 2013, Vol.44 (1), p.245-250
Main Authors: Perez Alea, Mileidys, Thomas, Vincent, Martin, Guillaume, El Alaoui, Saïd
Format: Article
Language:English
Subjects:
Amino acids
Analytical Chemistry
Antibodies
Biochemical Engineering
Biochemistry
Biomedical and Life Sciences
Deregulation
Diseases
Enzyme Inhibitors - chemistry
Female
GTP-Binding Proteins
Holes
Human
Humans
Isoenzymes - antagonists & inhibitors
Isoenzymes - chemistry
Isoenzymes - metabolism
Life Sciences
Male
Neurobiology
Original Article
Peptide Fragments - chemistry
Proteomics
Saliva
Saliva - enzymology
Transglutaminases - antagonists & inhibitors
Transglutaminases - chemistry
Transglutaminases - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Transglutaminases (TGs) expression and enzymatic activities in human saliva were investigated. Specific antibodies showed the co-existence of TG1, TG2, TG3 and TG4. TG2 and TG3 were found in native and multiple proteolytic forms. Our data indicate that TG1 and TG2 isoenzymes are highly active with the major activity attributed to TG1. These findings pave the way for future studies on the physiological role of TG in the oral cavity and the potential impact of their deregulation in TG-associated oral diseases.
ISSN:0939-4451
1438-2199
DOI:10.1007/s00726-011-1142-5