Multiple Signaling Pathways are Activated During Insulin-like Growth Factor-I (IGF-I) Stimulated Breast Cancer Cell Migration
dc.contributor.author | Zhang, Xihong | en_US |
dc.contributor.author | Lin, Min | en_US |
dc.contributor.author | Golen, Kenneth L. | en_US |
dc.contributor.author | Yoshioka, Kiyoko | en_US |
dc.contributor.author | Itoh, Kazuyuki | en_US |
dc.contributor.author | Yee, Douglas | en_US |
dc.date.accessioned | 2006-09-11T14:28:40Z | |
dc.date.available | 2006-09-11T14:28:40Z | |
dc.date.issued | 2005-09 | en_US |
dc.identifier.citation | Zhang, Xihong; Lin, Min; Golen, Kenneth L.; Yoshioka, Kiyoko; Itoh, Kazuyuki; Yee, Douglas; (2005). "Multiple Signaling Pathways are Activated During Insulin-like Growth Factor-I (IGF-I) Stimulated Breast Cancer Cell Migration." Breast Cancer Research and Treatment 93(2): 159-168. <http://hdl.handle.net/2027.42/44233> | en_US |
dc.identifier.issn | 1573-7217 | en_US |
dc.identifier.issn | 0167-6806 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/44233 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=16187236&dopt=citation | en_US |
dc.description.abstract | In order to display the full metastatic phenotype, the cancer cell must acquire the ability to migrate. In breast cancer, we have previously shown that insulin-like growth factor I (IGF-I) enhances cell motility in the highly metastatic MDA-231BO cell line by activating the type I IGF receptor (IGF1R). This motility response requires activation of IRS-2 and integrin ligation. In order to identify the key molecules downstream of IRS-2, we examined several signaling pathways known to be involved in cell motility. Focal adhesion kinase (FAK) was not activated by IGF-I, but IGF-I caused redistribution of FAK away from focal adhesion plaques. IGF-I treatment of MDA-231BO cells activated RhoA and inhibition of Rho-kinase (ROCK) inhibited the IGF-mediated motility response. The mitogen activated protein kinase (MAPK), p38, was also activated by IGF-I and inhibition of p38 by SB203580 blocked IGF-I induced cell motility. ROCK inhibition with Y-27632 also inhibited p38 phosphorylation suggesting that p38 lies downstream of ROCK. Both Erk1,2 and phosphatidyl-3 kinase (PI3K) were required for IGF-I stimulated cell motility, but only PI3K appeared to be directly downstream of IGF-I. Thus, IGF-I activation of its receptor coordinates multiple signaling pathways required for cell motility. Defining the key molecules downstream of the type I IGF receptor may provide a basis for optimizing therapies directed at this target. | en_US |
dc.format.extent | 346920 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; Springer | en_US |
dc.subject.other | Cell Motility | en_US |
dc.subject.other | Rho | en_US |
dc.subject.other | Medicine & Public Health | en_US |
dc.subject.other | Oncology | en_US |
dc.subject.other | Breast Neoplasms | en_US |
dc.subject.other | Focal Adhesion Kinase | en_US |
dc.subject.other | Insulin-like Growth Factor-I | en_US |
dc.subject.other | Mitogen Activated Protein Kinase | en_US |
dc.subject.other | Type I IGF Receptor | en_US |
dc.title | Multiple Signaling Pathways are Activated During Insulin-like Growth Factor-I (IGF-I) Stimulated Breast Cancer Cell Migration | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Ophthalmology | en_US |
dc.subject.hlbsecondlevel | Obstetrics and Gynecology | en_US |
dc.subject.hlbsecondlevel | Oncology and Hematology | en_US |
dc.subject.hlbsecondlevel | Internal Medicine and Specialties | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Otolaryngology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Internal Medicine, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationum | Department of Internal Medicine, University of Michigan, Ann Arbor, MI, USA | en_US |
dc.contributor.affiliationother | Laboratory of Tumor Biology, Osaka Medical Center for Cancer, Osaka, Japan | en_US |
dc.contributor.affiliationother | Department of Medicine, University of Minnesota Cancer Center, Minneapolis, MN, 55455, USA; Department of Medicine, University of Minnesota Cancer Center, Minneapolis, MN, 55455, USA | en_US |
dc.contributor.affiliationother | Department of Medicine, University of Minnesota Cancer Center, Minneapolis, MN, 55455, USA | en_US |
dc.contributor.affiliationother | Laboratory of Tumor Biology, Osaka Medical Center for Cancer, Osaka, Japan | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 16187236 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/44233/1/10549_2005_Article_4626.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/s10549-005-4626-8 | en_US |
dc.identifier.source | Breast Cancer Research and Treatment | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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