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Role of the cytoskeleton in laminin induced mammary gene expression

dc.contributor.authorBlum, Joanne L.en_US
dc.contributor.authorWicha, Max S.en_US
dc.date.accessioned2007-04-06T18:03:50Z
dc.date.available2007-04-06T18:03:50Z
dc.date.issued1988-04en_US
dc.identifier.citationBlum, Joanne L.; Wicha, Max S. (1988)."Role of the cytoskeleton in laminin induced mammary gene expression." Journal of Cellular Physiology 135(1): 13-22. <http://hdl.handle.net/2027.42/49876>en_US
dc.identifier.issn0021-9541en_US
dc.identifier.issn1097-4652en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/49876
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3366789&dopt=citationen_US
dc.description.abstractThe differentiation of rat mammary epithelial cells is characterized both by morphologic changes and by the expression of a group of milk protein genes. We have previously shown that by culturing these cells on the basement membrane glycoprotein laminin, the synthesis of the milk proteins, transferrin, Α-casein, and Α-lactalbumin is induced. In order to determine if this effect is mediated through the cytoskeleton, we have treated these cells with cytochalasin D and colchicine. Treatment with cytochalasin D or colchicine for 24 h inhibits the accumulation of Α-casein, transferrin, and Α-lactalbumin without significant effect on general protein synthesis. Pulse chase studies show that cytochalasin D does not alter the intracellular turnover of Α-casein or transferrin. Additionally, treatment with cytochalasin D causes an early (within 1 h) increase in secretion of Α-casein and transferrin suggesting that the actin cytoskeleton provides a meshwork for secretory vesicles. The disruption of this network enhances the secretion of preformed proteins. However, long term (24 h) treatment with cytochalasin D inhibits synthesis of these milk proteins. Northern blot analysis indicates that treatment with cytochalasin D or colchicine inhibits the laminin induced increase in Α-casein, Α-lactalbumin, and transferrin mRNAs. These studies indicate that the major effect of the cytoskeleton on laminin induced milk protein gene expression occurs at the level of accumulation of mRNAs for these proteins. We conclude that the expression of laminin induced milk protein gene expression in primary rat mammary cultures depends on the integrity of the actin and microtubule cytoskeleton.en_US
dc.format.extent1066714 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherWiley Subscription Services, Inc., A Wiley Companyen_US
dc.subject.otherLife and Medical Sciencesen_US
dc.subject.otherCell & Developmental Biologyen_US
dc.titleRole of the cytoskeleton in laminin induced mammary gene expressionen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelKinesiology and Sportsen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDivision of Hematology/Oncology, Department of Internal Medicine and Program in Cell and Molecular Biology, Simpson Memorial Research Institute, University of Michigan, Ann Arbor, Michigan 48109en_US
dc.contributor.affiliationumDivision of Hematology/Oncology, Department of Internal Medicine and Program in Cell and Molecular Biology, Simpson Memorial Research Institute, University of Michigan, Ann Arbor, Michigan 48109 ; Division of Hematology/Oncology, Department of Internal Medicine and Program in Cell and Molecular Biology, Simpson Memorial Research Institute, University of Michigan, Ann Arbor, Michigan 48109en_US
dc.identifier.pmid3366789en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/49876/1/1041350103_ftp.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1002/jcp.1041350103en_US
dc.identifier.sourceJournal of Cellular Physiologyen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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