Role of the cytoskeleton in laminin induced mammary gene expression
dc.contributor.author | Blum, Joanne L. | en_US |
dc.contributor.author | Wicha, Max S. | en_US |
dc.date.accessioned | 2007-04-06T18:03:50Z | |
dc.date.available | 2007-04-06T18:03:50Z | |
dc.date.issued | 1988-04 | en_US |
dc.identifier.citation | Blum, 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.issn | 0021-9541 | en_US |
dc.identifier.issn | 1097-4652 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/49876 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3366789&dopt=citation | en_US |
dc.description.abstract | The 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.extent | 1066714 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Life and Medical Sciences | en_US |
dc.subject.other | Cell & Developmental Biology | en_US |
dc.title | Role of the cytoskeleton in laminin induced mammary gene expression | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Kinesiology and Sports | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | 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 48109 | en_US |
dc.contributor.affiliationum | 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 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 48109 | en_US |
dc.identifier.pmid | 3366789 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/49876/1/1041350103_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/jcp.1041350103 | en_US |
dc.identifier.source | Journal of Cellular Physiology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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