Linked Life Data

11061429

Source:http://linkedlifedata.com/resource/pubmed/id/11061429

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2001-2-5
pubmed:abstractText
The "tissue" transglutaminase is a multifunctional enzyme that in its cross-linking configuration catalyzes Ca2+ -dependent reactions resulting in post-translational modification of proteins by establishing epsilon(gamma-glutamyl) lysine cross-links and/or covalent incorporation of biogenic amines (di- and poly-amines and histamine) into proteins. Several laboratories have shown that in Vertebrates, "tissue" transglutaminase (tTG) gene expression specifically characterizes cells undergoing apoptosis or programmed cell death (PCD). The Ca2+ -dependent activation of this enzyme leads to the formation of detergent-insoluble cross-linked protein polymers in cells undergoing PCD. This insoluble protein scaffold could stabilize the integrity of the dying cells before their clearance by phagocytosis, preventing the non-specific release of harmful intracellular components (e.g. lysosomal enzymes, nucleic acids, etc.) and consequently inflammatory responses and scar formation in bystander tissues. In this review we attempt to present an overview of the current knowledge on tTG expression and regulation in animal reproduction and development. The data available so far further strengthen the relationship existing between tTG expression and the induction of PCD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0214-6282
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
655-62
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
"Tissue" transglutaminase in animal development.
pubmed:affiliation
Department of Biology, University of Rome Tor Vergata, Italy. mauro.piacentini@uniroma2.it
pubmed:publicationType
Journal Article, Review