Linked Life Data

12783864

Source:http://linkedlifedata.com/resource/pubmed/id/12783864

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2003-8-18
pubmed:abstractText
Autocrine motility factor (AMF)/phosphoglucose isomerase (PGI; EC 5.3.1.9) is a housekeeping cytosolic enzyme that plays a key role in both glycolysis and gluconeogenesis pathways. AMF/PGI is also a multifunctional protein that displays cytokine properties, eliciting mitogenic, motogenic, and differentiation activities, and has been implicated in tumor progression and metastasis. Because little is known about AMF/PGI-dependent signaling in general and during tumorigenesis in particular, we sought to study its effect on the cell cycle. To elucidate the functional role of PGI, we stably transfected its cDNA into NIH/3T3 and BALB/c 3T3-A31 fibroblasts. Ectopic overexpression of PGI results in the acquisition of a transformed phenotype associated with an acceleration of G1 to S cell cycle transition. These were manifested by up-regulation of cyclin D1 expression and cyclin-dependent kinase activity and down-regulation of the cyclin-dependent kinase inhibitor p27Kip1. The reduced p27Kip1 protein expression level in PGI-overexpressing cells could be restored to control levels by treatment with proteasome inhibitor. PGI-overexpressing cells also exhibited elevated expression of Skp2 involved in p27Kip1 ubiquitination and elevation in the levels of retinoblastoma protein hyperphosphorylation. Thus, we may conclude that the overexpression of AMF/PGI enhances cell proliferation together with up-regulation of cyclin/cyclin-dependent kinase activities and down-regulation of p27Kip1, whereas the induction of 3T3 fibroblast transformation by PGI is regulated by the retinoblastoma protein pathway.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32165-72
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:12783864-3T3 Cells, pubmed-meshheading:12783864-Animals, pubmed-meshheading:12783864-Base Sequence, pubmed-meshheading:12783864-Blotting, Western, pubmed-meshheading:12783864-Cell Cycle Proteins, pubmed-meshheading:12783864-Cell Division, pubmed-meshheading:12783864-Cyclin-Dependent Kinase Inhibitor p27, pubmed-meshheading:12783864-Cysteine Endopeptidases, pubmed-meshheading:12783864-DNA Primers, pubmed-meshheading:12783864-Glucose-6-Phosphate Isomerase, pubmed-meshheading:12783864-Hydrolysis, pubmed-meshheading:12783864-Mice, pubmed-meshheading:12783864-Mice, Inbred BALB C, pubmed-meshheading:12783864-Microscopy, Fluorescence, pubmed-meshheading:12783864-Multienzyme Complexes, pubmed-meshheading:12783864-Proteasome Endopeptidase Complex, pubmed-meshheading:12783864-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:12783864-Signal Transduction, pubmed-meshheading:12783864-Tumor Suppressor Proteins
pubmed:year
2003
pubmed:articleTitle
Regulation of cell proliferation by autocrine motility factor/phosphoglucose isomerase signaling.
pubmed:affiliation
Tumor Progression and Metastasis, Karmanos Cancer Institute, The Department of Pathology, Wayne State University, School of Medicine, Detroit, Michigan 48201, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.