Polymorphism of transglutaminase 2: Unusually low frequency of genomic variants with deficient functions

Róbert Király, E. Barta, L. Fésüs

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. These unusual multiple roles encoded into one polypeptide chain suggest that genomic variations in the TGM2 gene should be limited. Indeed, the available information in databases shows that unlike in the case of most other transglutaminases there are no common single nucleotide polymorphisms in exons of human TGM2. We collected data on and produced some of the rare genetic variants of TGM2 by site directed mutagenesis and found that some were less stable than the most abundant (wild type) enzyme variant and the majority had deficient transamidating activity. Further studies are required to clarify the pathologic significance of these rare TGM2 alleles in the human population.

Original languageEnglish
Pages (from-to)215-225
Number of pages11
JournalAmino Acids
Volume44
Issue number1
DOIs
Publication statusPublished - Jan 2013

Fingerprint

Polymorphism
Multifunctional Enzymes
Protein Disulfide-Isomerases
Signal transduction
Mutagenesis
Transglutaminases
Enzymes
Site-Directed Mutagenesis
Glutamine
Protein Kinases
Amines
Single Nucleotide Polymorphism
Extracellular Matrix
Exons
Signal Transduction
Membrane Proteins
Nucleotides
Genes
Alleles
Databases

Keywords

  • Deficient activities
  • Human transglutaminase 2
  • No common variants
  • Rare variants
  • SNPs
  • Wild type sequence

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

Cite this

Polymorphism of transglutaminase 2 : Unusually low frequency of genomic variants with deficient functions. / Király, Róbert; Barta, E.; Fésüs, L.

In: Amino Acids, Vol. 44, No. 1, 01.2013, p. 215-225.

Research output: Contribution to journalArticle

@article{cd6515e69ba645099f6d7d5d9d289d5b,
title = "Polymorphism of transglutaminase 2: Unusually low frequency of genomic variants with deficient functions",
abstract = "Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. These unusual multiple roles encoded into one polypeptide chain suggest that genomic variations in the TGM2 gene should be limited. Indeed, the available information in databases shows that unlike in the case of most other transglutaminases there are no common single nucleotide polymorphisms in exons of human TGM2. We collected data on and produced some of the rare genetic variants of TGM2 by site directed mutagenesis and found that some were less stable than the most abundant (wild type) enzyme variant and the majority had deficient transamidating activity. Further studies are required to clarify the pathologic significance of these rare TGM2 alleles in the human population.",
keywords = "Deficient activities, Human transglutaminase 2, No common variants, Rare variants, SNPs, Wild type sequence",
author = "R{\'o}bert Kir{\'a}ly and E. Barta and L. F{\'e}s{\"u}s",
year = "2013",
month = "1",
doi = "10.1007/s00726-011-1194-6",
language = "English",
volume = "44",
pages = "215--225",
journal = "Amino Acids",
issn = "0939-4451",
publisher = "Springer Wien",
number = "1",

}

TY - JOUR

T1 - Polymorphism of transglutaminase 2

T2 - Unusually low frequency of genomic variants with deficient functions

AU - Király, Róbert

AU - Barta, E.

AU - Fésüs, L.

PY - 2013/1

Y1 - 2013/1

N2 - Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. These unusual multiple roles encoded into one polypeptide chain suggest that genomic variations in the TGM2 gene should be limited. Indeed, the available information in databases shows that unlike in the case of most other transglutaminases there are no common single nucleotide polymorphisms in exons of human TGM2. We collected data on and produced some of the rare genetic variants of TGM2 by site directed mutagenesis and found that some were less stable than the most abundant (wild type) enzyme variant and the majority had deficient transamidating activity. Further studies are required to clarify the pathologic significance of these rare TGM2 alleles in the human population.

AB - Transglutaminase 2 (TG2) is a multifunctional member of an enzyme family: it modifies glutamine residues by cross-linking proteins and incorporating primary amines into them, has protein disulphide isomerase and protein kinase activities, mediates trans-membrane signal transduction and interactions between cell surface proteins and the extracellular matrix. These unusual multiple roles encoded into one polypeptide chain suggest that genomic variations in the TGM2 gene should be limited. Indeed, the available information in databases shows that unlike in the case of most other transglutaminases there are no common single nucleotide polymorphisms in exons of human TGM2. We collected data on and produced some of the rare genetic variants of TGM2 by site directed mutagenesis and found that some were less stable than the most abundant (wild type) enzyme variant and the majority had deficient transamidating activity. Further studies are required to clarify the pathologic significance of these rare TGM2 alleles in the human population.

KW - Deficient activities

KW - Human transglutaminase 2

KW - No common variants

KW - Rare variants

KW - SNPs

KW - Wild type sequence

UR - http://www.scopus.com/inward/record.url?scp=84871943950&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84871943950&partnerID=8YFLogxK

U2 - 10.1007/s00726-011-1194-6

DO - 10.1007/s00726-011-1194-6

M3 - Article

C2 - 22160262

AN - SCOPUS:84871943950

VL - 44

SP - 215

EP - 225

JO - Amino Acids

JF - Amino Acids

SN - 0939-4451

IS - 1

ER -