rdf:type |
|
lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0031437,
umls-concept:C0162326,
umls-concept:C0185023,
umls-concept:C0185117,
umls-concept:C0205147,
umls-concept:C0205217,
umls-concept:C0208973,
umls-concept:C0237497,
umls-concept:C0278488,
umls-concept:C0331858,
umls-concept:C0905617,
umls-concept:C1314972,
umls-concept:C1517892,
umls-concept:C1704640,
umls-concept:C1704666,
umls-concept:C1706515,
umls-concept:C1947904,
umls-concept:C1999228,
umls-concept:C2825781,
umls-concept:C2911684
|
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
|