Modulation of fibronectin synthesis and fibronectin binding during transformation and differentiation of mouse AKR fibroblasts
dc.contributor.author | Varani, James | en_US |
dc.contributor.author | Chakrabarty, Subhas | en_US |
dc.date.accessioned | 2007-04-06T18:04:02Z | |
dc.date.available | 2007-04-06T18:04:02Z | |
dc.date.issued | 1990-06 | en_US |
dc.identifier.citation | Varani, James; Chakrabarty, Subhas (1990)."Modulation of fibronectin synthesis and fibronectin binding during transformation and differentiation of mouse AKR fibroblasts." Journal of Cellular Physiology 143(3): 445-454. <http://hdl.handle.net/2027.42/49878> | en_US |
dc.identifier.issn | 0021-9541 | en_US |
dc.identifier.issn | 1097-4652 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/49878 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2141611&dopt=citation | en_US |
dc.description.abstract | In previous studies it was shown that transformation of AKR fibroblasts with 3-methylcholanthrene was associated with a loss of surface fibronectin and that induction of differentiation of the transformed cells with N,N-dimethylformamide (DMF) was associated with reacquisition of surface fibronectin (Chakrabarty et al., J. Cell. Physiol. 133:415, 1987). It is shown in the present study that changes in surface fibronectin reflect altered fibronectin synthesis and altered fibronectin binding. Both the nontransformed cells (AKR-2B) and their transformed counterparts (AKR-MCA) bound 125 I-fibronectin in a receptor-like fashion, but the AKR-MCA cells had only 20% of the receptors found on the AKR-2B cells. Whole cell extracts prepared from the AKR-2B cells and separated by sodium dodecyl sufate-polyacrylamide gel electrophoresis under reducing conditions were examined for 125 I-fibronectin binding. Under these conditions, the majority of binding occurred to moieties with molecular weights of 180 kD, 150 kD, and 97 kD. Binding to similar moieties on the AKR-MCA cells was virtually absent but occurred rapidly after treatment with DMF. The appearance of these moieties paralleled the acquisition of 125 I-fibronectin binding activity by whole cells. Antibodies to the fibronectin receptor isolated from human placenta reacted with the DMF-sensitive moieties in immunoblot assays. Both the appearance of the fibronectin binding moieties and the acquisition of 125 I-fibronectin binding activity by whole cells occurred within 6 hr of DMF treatment and increased over the suosequent 4 day period. The time course of these events paralleled closely the time course for induction of fibronectin biosynthesis by DMF. These changes in fibronectin binding and fibronectin production were associated with alterations in cell-substrate adhesion. The AKR-2B cells rapidly attached and spread on bovine serum albumin-coated dishes and on fibronectin-coated dishes, whereas the AKR-MCA cells were less adhesive on both substrates. Capacity to attach and spread was regained concomitantly with the induction of fibronectin binding and fibronectin production. Adhesion on both substrates was partially inhibited by antibodies to the fibronectin receptor and by RGDS. These studies suggest that fibronectin production and fibronectin binding are coregulated in AKR fibroblasts and that they function together to bring about changes in cell-substrate adhesion. | en_US |
dc.format.extent | 1198883 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 | Modulation of fibronectin synthesis and fibronectin binding during transformation and differentiation of mouse AKR fibroblasts | 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 | Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109 ; Department of Pathology, University of Michigan Medical School, Ann Arbor, Michigan 48109 | en_US |
dc.contributor.affiliationother | Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030 | en_US |
dc.identifier.pmid | 2141611 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/49878/1/1041430307_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/jcp.1041430307 | en_US |
dc.identifier.source | Journal of Cellular Physiology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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