Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1999-12-14
pubmed:abstractText
Base-unpairing regions (BURs) contain a specialized DNA context with an exceptionally high unwinding propensity, and are typically identified within various matrix attachment regions. A BUR affinity column was used to purify a doublet of Mr 20,000 proteins from human breast carcinoma cells. These proteins were identified as the high-mobility group (HMG) protein, HMG-I, and its splicing variant, HMG-Y. We show that HMG-I(Y) specifically binds BURs. Mutating BURs so as to abrogate their unwinding property greatly reduced their binding affinity to HMG-I(Y). Numerous studies have indicated that elevated HMG-I(Y) expression is correlated with more advanced cancers and with increased metastatic potential. We studied whether the expression of HMG-I(Y) responds to signaling through the heregulin (HRG)-erbB pathway and the extracellular matrix. HMG-I(Y) expression was increased in MCF-7 cells after stable transfection with an HRG expression construct that led cells to acquire estrogen independence and metastasizing ability. A high level of HMG-I(Y) expression was detected in metastatic MDA-MB-231 cells, but the expression was virtually diminished, and the metastasizing ability was lost after cells were stably transfected with an antisense HRG cDNA construct. HMG-I(Y) was also decreased in MDA-MB-231 cells when treated with a chemical inhibitor for matrix metalloproteinase-9 that led to a reduction of invasive capability in vitro. The level of HMG-I(Y) expression, therefore, is dynamically regulated in human breast cancer cells in response to varying types of signaling that affect metastatic ability, including the HRG-erbB pathway and those from the extracellular matrix.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antisense Elements (Genetics), http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Estrogens, http://linkedlifedata.com/resource/pubmed/chemical/HMGA1a Protein, http://linkedlifedata.com/resource/pubmed/chemical/Heterogeneous-Nuclear..., http://linkedlifedata.com/resource/pubmed/chemical/High Mobility Group Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 9, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neuregulin-1, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5695-703
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10582687-Antisense Elements (Genetics), pubmed-meshheading:10582687-Blotting, Southern, pubmed-meshheading:10582687-Blotting, Western, pubmed-meshheading:10582687-Breast Neoplasms, pubmed-meshheading:10582687-DNA-Binding Proteins, pubmed-meshheading:10582687-Estrogens, pubmed-meshheading:10582687-Female, pubmed-meshheading:10582687-HMGA1a Protein, pubmed-meshheading:10582687-Heterogeneous-Nuclear Ribonucleoproteins, pubmed-meshheading:10582687-High Mobility Group Proteins, pubmed-meshheading:10582687-Humans, pubmed-meshheading:10582687-Matrix Metalloproteinase 9, pubmed-meshheading:10582687-Molecular Weight, pubmed-meshheading:10582687-Neoplasm Metastasis, pubmed-meshheading:10582687-Neoplasm Proteins, pubmed-meshheading:10582687-Neuregulin-1, pubmed-meshheading:10582687-Phenotype, pubmed-meshheading:10582687-Ribonucleoproteins, pubmed-meshheading:10582687-Transcription Factors, pubmed-meshheading:10582687-Transfection, pubmed-meshheading:10582687-Tumor Cells, Cultured
pubmed:year
1999
pubmed:articleTitle
HMG-I(Y) recognizes base-unpairing regions of matrix attachment sequences and its increased expression is directly linked to metastatic breast cancer phenotype.
pubmed:affiliation
Lawrence Berkeley National Laboratory, University of California, Berkeley 94720, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't