Linked Life Data

1673452

Source:http://linkedlifedata.com/resource/pubmed/id/1673452

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-5-28
pubmed:abstractText
A monoclonal antibody (MAb) 81D1c2, which recognizes the N epsilon (gamma glutamyl) lysine isopeptide produced by the action of transglutaminase activity was prepared. Its reactivity towards the homologous isopeptide was about 3-fold greater than that with either N alpha (alpha glutamyl) lysine (a naturally occurring heterologous dipeptide) or N alpha (gamma glutamyl) lysine, another heterologous peptide not described so far in naturally occurring proteins. When used in an immunohistochemical study on cells in culture derived from human carcinoma of the larynx (HEp2) and from chicken embryo cells (CEC), both fixed in acetone, this MAb detected N epsilon (gamma glutamyl) lysine residues in the nucleus. The amount of N epsilon (gamma glutamyl) lysine isopeptides follows closely transglutaminase activity during the lag phase of growth of both CEC and HEp2 cells. However, during exponential growth, the 2 parameters decrease concomitantly in HEp2 cells, whereas in CEC, transglutaminase activity increases but isopeptide bond levels drop. Compared with other reported methods for measuring isopeptides, this immunohistological approach permits the localization and at least the semi-quantitative determination of N epsilon (gamma glutamyl) lysine in cells in situ.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0020-7136
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
221-6
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Transglutaminase activity and N epsilon (gamma glutamyl) lysine isopeptide levels during cell growth: an enzymic and immunological study.
pubmed:affiliation
Laboratoire d'Immunochimie INSERM C.J.F., Faculté de Médecine Lyon Sud, Oullins, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't