Linked Life Data

18980249

Source:http://linkedlifedata.com/resource/pubmed/id/18980249

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2008-11-27
pubmed:abstractText
tNOX (ENOX2), a cancer-specific and growth-related cell surface protein with protein disulfide-thiol interchange and hydroquinone (NADH) oxidase activities was overexpressed in a transgenic mouse model. Female transgenic mice grew faster than wild type as did embryonic fibroblast cells prepared from the transgenic mice. The tissue expression of tNOX mRNA was greatest in heart, lung and liver. When these tissues were analyzed for cell size, the cells from the tissues of transgenic animals were, on average, 20% larger in surface area than cells from corresponding wild-type tissues. Also analyzed were cells of intestine, spleen and kidney in which tNOX overexpression was observed but to a lesser extent. Cell size was increased as well with intestine and kidney but less so with spleen. At the end of the study, carcass weights of the transgenic animals were greater than those of wild type. This increase in carcass weight was reflected in an increase in femur weight and thickness in both male and female transgenic mice but not in femur length. Other carcass parameters such as skin weight and body fat or body fluids were unchanged or changes were insufficient to account for the increased carcass weight. The findings are consistent with the property of tNOX observed in studies with cultured cells as contributing to the enlargement phase of cell growth.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1097-4644
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
105
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1437-42
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Cell size increased in tissues from transgenic mice overexpressing a cell surface growth-related and cancer-specific hydroquinone oxidase, tNOX, with protein disulfide-thiol interchange activity.
pubmed:affiliation
Department of Foods and Nutrition, Purdue University, Stone Hall, 700 W. State Street, West Lafayette, Indiana 47907-2059, USA.
pubmed:publicationType
Journal Article