Evidences for a role of protein cross-links in transglutaminase-related disease.

Abstract:

:Transglutaminases (TGs) are a large family of related and ubiquitous enzymes that catalyze the cross-linking of a glutaminyl residue of a protein/peptide substrate to a lysyl residue of a protein/peptide co-substrate. Considerable and intense progress has been made in the understanding of the chemistry, molecular biology and cell biology of TGs. The knowledge that very different physiological and pathological processes are dependent on the presence of adequate levels of these cross-linking enzymes and on the amount of both free and protein-conjugated polyamines by TG, has generated an incredible amount of original research and review articles. It is clear that TG-mediated reactions are essential for some biological processes, such as blood coagulation, skin barrier formation and extracellular matrix assembly, but may also be involved in pathogenetic mechanisms responsible for several human diseases, such as cancer, AIDS, neurodegenerative disorders, celiac disease, and eye lens opacification. We present here a comprehensive review of recent insights into the pathophysiology of TGs related to their protein cross-linking activity.

journal_name

Amino Acids

journal_title

Amino acids

authors

Tabolacci C,Lentini A,Provenzano B,Beninati S

doi

10.1007/s00726-011-1011-2

subject

Has Abstract

pub_date

2012-02-01 00:00:00

pages

975-86

issue

2-3

eissn

0939-4451

issn

1438-2199

journal_volume

42

pub_type

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