Linked Life Data

12360406

Source:http://linkedlifedata.com/resource/pubmed/id/12360406

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2002-10-2
pubmed:abstractText
p95 is a putative signal transduction protein of approximately 95 kDa that contains multiple tyrosine residues that are conserved from yeast to human, a Src phosphorylation consensus sequence and a proline-rich C-terminus that binds SH3-domains. Previous studies have established that mammalian p95 is physically associated with proteins that regulate apoptotic induction and cell transformation; however, it is unclear whether p95 is a positive or negative regulator in these processes. Moreover, a p95 partner protein has been localized at both focal adhesions and actin-cytoskeletons in rat astrocytes. However, there is no evidence that mammalian p95 has roles in regulating cell adhesion or morphology. In this study, we examined the effects of p95 on the anchorage-independent growth and tumorigenicity of malignant HeLa cells, and on the growth and morphology of non-transformed NIH3T3 cells. In HeLa cells, p95 overexpression promoted detachment-induced apoptosis (anoikis), inhibited detachment of viable cells from substratum and reduced tumorigenicity. In NIH3T3 cells, p95 overexpression promoted flat cell morphology and slowed cell proliferation, whereas p95 downregulation had opposite effects. These findings indicate that the mammalian p95 is a positive regulator in apoptotic signaling and a negative regulator in cell transformation. They also suggest that p95 has roles in regulating cell adhesion and morphology.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6801-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12360406-3T3 Cells, pubmed-meshheading:12360406-Animals, pubmed-meshheading:12360406-Anoikis, pubmed-meshheading:12360406-Apoptosis, pubmed-meshheading:12360406-Calcium-Binding Proteins, pubmed-meshheading:12360406-Carrier Proteins, pubmed-meshheading:12360406-Cell Adhesion, pubmed-meshheading:12360406-Cell Cycle Proteins, pubmed-meshheading:12360406-Cell Division, pubmed-meshheading:12360406-Endosomal Sorting Complexes Required for Transport, pubmed-meshheading:12360406-G1 Phase, pubmed-meshheading:12360406-HeLa Cells, pubmed-meshheading:12360406-Humans, pubmed-meshheading:12360406-Mice, pubmed-meshheading:12360406-Mice, Nude, pubmed-meshheading:12360406-Neoplasms, Experimental, pubmed-meshheading:12360406-Phosphoproteins, pubmed-meshheading:12360406-Signal Transduction
pubmed:year
2002
pubmed:articleTitle
Hp95 promotes anoikis and inhibits tumorigenicity of HeLa cells.
pubmed:affiliation
Department of Experimental Therapeutics, The University of Texas, M.D. Anderson Cancer Center, Houston, Texas, TX 77030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't