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Journal articles on the topic 'Cell spreading'

Author: Grafiati
Published: 4 June 2021
Last updated: 31 January 2023

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1

LeBrasseur, Nicole. "Spreading mitochondria." Journal of Cell Biology 172, no. 4 (February 6, 2006): 482. http://dx.doi.org/10.1083/jcb1724rr4.

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2

Disatnik, Marie-Hélène, and Thomas A. Rando. "Integrin-mediated Muscle Cell Spreading." Journal of Biological Chemistry 274, no. 45 (November 5, 1999): 32486–92. http://dx.doi.org/10.1074/jbc.274.45.32486.

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3

Lavine, Marc S. "Cell spreading affects energy consumption." Science 370, no. 6518 (November 12, 2020): 806.2–806. http://dx.doi.org/10.1126/science.370.6518.806-b.

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4

Stewart, M. G., E. Moy, G. Chang, W. Zingg, and A. W. Neumann. "Thermodynamic model for cell spreading." Colloids and Surfaces 42, no. 2 (January 1989): 215–32. http://dx.doi.org/10.1016/0166-6622(89)80193-3.

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5

Stewart, M. G., E. Moy, G. Chang, W. Zingg, and A. W. Neumann. "Thermodynamic model for cell spreading." Colloids and Surfaces 42, no. 3-4 (December 1989): 215–32. http://dx.doi.org/10.1016/0166-6622(89)80342-7.

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6

Tsygankova, Oxana M., Changqing Ma, Waixing Tang, Christopher Korch, Michael D. Feldman, Yu Lv, Marcia S. Brose, and Judy L. Meinkoth. "Downregulation of Rap1GAP in Human Tumor Cells Alters Cell/Matrix and Cell/Cell Adhesion." Molecular and Cellular Biology 30, no. 13 (May 3, 2010): 3262–74. http://dx.doi.org/10.1128/mcb.01345-09.

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ABSTRACT Rap1GAP expression is decreased in human tumors. The significance of its downregulation is unknown. We show that Rap1GAP expression is decreased in primary colorectal carcinomas. To elucidate the advantages conferred on tumor cells by loss of Rap1GAP, Rap1GAP expression was silenced in human colon carcinoma cells. Suppressing Rap1GAP induced profound alterations in cell adhesion. Rap1GAP-depleted cells exhibited defects in cell/cell adhesion that included an aberrant distribution of adherens junction proteins. Depletion of Rap1GAP enhanced adhesion and spreading on collagen. Silencing of Rap expression normalized spreading and restored E-cadherin, β-catenin, and p120-catenin to cell/cell contacts, indicating that unrestrained Rap activity underlies the alterations in cell adhesion. The defects in adherens junction protein distribution required integrin signaling as E-cadherin and p120-catenin were restored at cell/cell contacts when cells were plated on poly-l-lysine. Unexpectedly, Src activity was increased in Rap1GAP-depleted cells. Inhibition of Src impaired spreading and restored E-cadherin at cell/cell contacts. These findings provide the first evidence that Rap1GAP contributes to cell/cell adhesion and highlight a role for Rap1GAP in regulating cell/matrix and cell/cell adhesion. The frequent downregulation of Rap1GAP in epithelial tumors where alterations in cell/cell and cell/matrix adhesion are early steps in tumor dissemination supports a role for Rap1GAP depletion in tumor progression.
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7

Sadahira, Yoshito, Tadashi Yoshino, and Naoya Kojima. "B16 melanoma cell spreading on activated endothelial cells." In Vitro Cellular & Developmental Biology - Animal 30, no. 10 (October 1994): 648–50. http://dx.doi.org/10.1007/bf02631266.

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8

McInnes, C., P. Knox, and D. J. Winterbourne. "Cell spreading on serum is not identical to spreading on fibronectin." Journal of Cell Science 88, no. 5 (December 1, 1987): 623–29. http://dx.doi.org/10.1242/jcs.88.5.623.

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Adhesion and spreading of cell lines on dishes coated with serum-derived proteins were studied after removal of cell-surface proteoglycans. A mixture of glycosaminoglycans lyases from heparin-induced Flavobacterium heparinum removed 80% of the [35S]sulphate-labelled glycosaminoglycans from the surface of attached cells within 30 min, but this had little effect on cell morphology. The rate of cell attachment to dishes coated with serum was unaffected by prior treatment of cells with this mixture of glycosaminoglycan lyases. While a heparan sulphate lyase preparation abolished cell spreading in response to fibronectin there was no effect of the enzyme on the spreading mediated by vitronectin. These results suggest that, although heparan sulphate is required for spreading on purified fibronectin, the spreading stimulated by serum under routine culture conditions requires neither cellular heparan sulphate nor serum-derived fibronectin.
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9

Cramer, L. P., and T. J. Mitchison. "Myosin is involved in postmitotic cell spreading." Journal of Cell Biology 131, no. 1 (October 1, 1995): 179–89. http://dx.doi.org/10.1083/jcb.131.1.179.

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We have investigated a role for myosin in postmitotic Potoroo tridactylis kidney (PtK2) cell spreading by inhibitor studies, time-lapse video microscopy, and immunofluorescence. We have also determined the spatial organization and polarity of actin filaments in postmitotic spreading cells. We show that butanedione monoxime (BDM), a known inhibitor of muscle myosin II, inhibits nonmuscle myosin II and myosin V adenosine triphosphatases. BDM reversibly inhibits PtK2 postmitotic cell spreading. Listeria motility is not affected by this drug. Electron microscopy studies show that some actin filaments in spreading edges are part of actin bundles that are also found in long, thin, structures that are connected to spreading edges and substrate (retraction fibers), and that 90% of this actin is oriented with barbed ends in the direction of spreading. The remaining actin in spreading edges has a more random orientation and spatial arrangement. Myosin II is associated with actin polymer in spreading cell edges, but not retraction fibers. Myosin II is excluded from lamellipodia that protrude from the cell edge at the end of spreading. We suggest that spreading involves myosin, possibly myosin II.
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10

Wells, William A. "Exclusion is spreading." Journal of Cell Biology 168, no. 1 (December 28, 2004): 11. http://dx.doi.org/10.1083/jcb1681rr3.

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11

Heinrichs, Arianne. "Spreading silence." Nature Reviews Molecular Cell Biology 4, no. 11 (November 2003): 823. http://dx.doi.org/10.1038/nrm1248.

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12

Mothes, Walther, Nathan M. Sherer, Jing Jin, and Peng Zhong. "Virus Cell-to-Cell Transmission." Journal of Virology 84, no. 17 (April 7, 2010): 8360–68. http://dx.doi.org/10.1128/jvi.00443-10.

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ABSTRACT Viral infections spread based on the ability of viruses to overcome multiple barriers and move from cell to cell, tissue to tissue, and person to person and even across species. While there are fundamental differences between these types of transmissions, it has emerged that the ability of viruses to utilize and manipulate cell-cell contact contributes to the success of viral infections. Central to the excitement in the field of virus cell-to-cell transmission is the idea that cell-to-cell spread is more than the sum of the processes of virus release and entry. This implies that virus release and entry are efficiently coordinated to sites of cell-cell contact, resulting in a process that is distinct from its individual components. In this review, we will present support for this model, illustrate the ability of viruses to utilize and manipulate cell adhesion molecules, and discuss the mechanism and driving forces of directional spreading. An understanding of viral cell-to-cell spreading will enhance our ability to intervene in the efficient spreading of viral infections.
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13

Dunn, G. A., and D. Zicha. "Dynamics of fibroblast spreading." Journal of Cell Science 108, no. 3 (March 1, 1995): 1239–49. http://dx.doi.org/10.1242/jcs.108.3.1239.

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A new technique of microinterferometry permits cellular growth and motile dynamics to be studied simultaneously in living cells. In isolated chick heart fibroblasts, we have found that the non-aqueous mass of each cell tends to increase steadily, with minor fluctuations, throughout the cell cycle. The spread area of each cell also tends to increase during interphase but fluctuates between wide limits. These limits are dependent on the cell's mass and the upper limit is particularly sharp and directly proportional to mass. From a dynamical point of view, the spread area of a cell is determined by the balance between the rates of two antagonistic processes: protrusion of cellular material into new territory and retraction of material from previously occupied territory. The spatial asymmetry of these processes determines the translocation of the cell. We have found with the chick fibroblasts that the rates of the two processes are generally closely matched to each other and appear to be dependent on the cell's area of spreading. Both continue incessantly in well spread cells, even when there is no net translocation of the cell, and the lower limit of each activity is directly proportional to spread area. The two processes show different behaviour, however, during changes in the spread area of the cell. Both increases and decreases in area appear to be brought about by changes in the rate of retraction, the rate of protrusion remaining relatively constant. A simple stochastic model based on a limited supply of adhesion molecules can simulate all our observations including the mass-limited spreading, the strong correlation between protrusion and retraction and the retraction-dominated changes in area. We conclude that the spread area of the cell is actively regulated, possibly by a simple automatic mechanism that adjusts the area of spreading in relation to the mass of the cell and controls the rate of protrusion to compensate rapidly for spontaneous fluctuations in retraction.
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14

Adler, E. M. "Spreading AMPylation?" Science Signaling 2, no. 66 (April 14, 2009): ec131-ec131. http://dx.doi.org/10.1126/scisignal.266ec131.

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15

Leslie, Mitch. "Talin holds tight during cell spreading." Journal of Cell Biology 205, no. 2 (April 28, 2014): 128. http://dx.doi.org/10.1083/jcb.2052iti3.

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16

Frame, Margaret, and Jim Norman. "A tal(in) of cell spreading." Nature Cell Biology 10, no. 9 (September 2008): 1017–19. http://dx.doi.org/10.1038/ncb0908-1017.

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17

Fardin, M. A., O. M. Rossier, P. Rangamani, P. D. Avigan, N. C. Gauthier, W. Vonnegut, A. Mathur, J. Hone, R. Iyengar, and M. P. Sheetz. "Cell spreading as a hydrodynamic process." Soft Matter 6, no. 19 (2010): 4788. http://dx.doi.org/10.1039/c0sm00252f.

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18

James, Judith A., and John B. Harley. "B-cell epitope spreading in autoimmunity." Immunological Reviews 164, no. 1 (August 1998): 185–200. http://dx.doi.org/10.1111/j.1600-065x.1998.tb01220.x.

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19

Ryzhkov, Pavel, Marcus Prass, Meike Gummich, Jac-Simon Kühn, Christina Oettmeier, and Hans-Günther Döbereiner. "Adhesion patterns in early cell spreading." Journal of Physics: Condensed Matter 22, no. 19 (April 26, 2010): 194106. http://dx.doi.org/10.1088/0953-8984/22/19/194106.

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20

Frisch, Thomas, and Olivier Thoumine. "Predicting the kinetics of cell spreading." Journal of Biomechanics 35, no. 8 (August 2002): 1137–41. http://dx.doi.org/10.1016/s0021-9290(02)00075-1.

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21

Lydon, M. J., and C. A. Foulger. "Cell-substratum interactions: serum spreading factor." Biomaterials 9, no. 6 (November 1988): 525–27. http://dx.doi.org/10.1016/0142-9612(88)90049-x.

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22

Salsmann, Alexandre, Elisabeth Schaffner-Reckinger, and Nelly Kieffer. "RGD, the Rho’d to cell spreading." European Journal of Cell Biology 85, no. 3-4 (April 2006): 249–54. http://dx.doi.org/10.1016/j.ejcb.2005.08.003.

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23

Norman, Leann, Kheya Sengupta, and Helim Aranda-Espinoza. "Blebbing dynamics during endothelial cell spreading." European Journal of Cell Biology 90, no. 1 (January 2011): 37–48. http://dx.doi.org/10.1016/j.ejcb.2010.09.013.

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24

Adams, Josephine C. "Cell adhesion — spreading frontiers, intricate insights." Trends in Cell Biology 7, no. 3 (March 1997): 107–10. http://dx.doi.org/10.1016/s0962-8924(97)01001-5.

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25

Marignani, Paola A., and Christopher L. Carpenter. "Vav2 is required for cell spreading." Journal of Cell Biology 154, no. 1 (July 9, 2001): 177–86. http://dx.doi.org/10.1083/jcb.200103134.

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Vav2 is a widely expressed Rho family guanine nucleotide exchange factor highly homologous to Vav1 and Vav3. Activated versions of Vav2 are transforming, but the normal function of Vav2 and how it is regulated are not known. We investigated the pathways that regulate Vav2 exchange activity in vivo and characterized its function. Overexpression of Vav2 activates Rac as assessed by both direct measurement of Rac-GTP and cell morphology. Vav2 also catalyzes exchange for RhoA, but does not cause morphologic changes indicative of RhoA activation. Vav2 nucleotide exchange is Src-dependent in vivo, since the coexpression of Vav2 and dominant negative Src, or treatment with the Src inhibitor PP2, blocks both Vav2-dependent Rac activation and lamellipodia formation. A mutation in the pleckstrin homology (PH) domain eliminates exchange activity and this construct does not induce lamellipodia, indicating the PH domain is necessary to catalyze nucleotide exchange. To further investigate the function of Vav2, we mutated the dbl homology (DH) domain and asked whether this mutant would function as a dominant negative to block Rac-dependent events. Studies using this mutant indicate that Vav2 is not necessary for platelet-derived growth factor– or epidermal growth factor–dependent activation of Rac. The Vav2 DH mutant did act as a dominant negative to inhibit spreading of NIH3T3 cells on fibronectin, specifically by blocking lamellipodia formation. These findings indicate that in fibroblasts Vav2 is necessary for integrin, but not growth factor–dependent activation of Rac leading to lamellipodia.
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26

KEESE, C. "Substrate mechanics and cell spreading*1." Experimental Cell Research 195, no. 2 (August 1991): 528–32. http://dx.doi.org/10.1016/0014-4827(91)90406-k.

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27

McEvoy, Eóin, Vikram S. Deshpande, and Patrick McGarry. "Free energy analysis of cell spreading." Journal of the Mechanical Behavior of Biomedical Materials 74 (October 2017): 283–95. http://dx.doi.org/10.1016/j.jmbbm.2017.06.006.

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28

Cuvelier, Damien, Manuel Théry, Yeh-Shiu Chu, Sylvie Dufour, Jean-Paul Thiéry, Michel Bornens, Pierre Nassoy, and L. Mahadevan. "The Universal Dynamics of Cell Spreading." Current Biology 17, no. 8 (April 2007): 694–99. http://dx.doi.org/10.1016/j.cub.2007.02.058.

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29

McGrath, James L. "Cell Spreading: The Power to Simplify." Current Biology 17, no. 10 (May 2007): R357—R358. http://dx.doi.org/10.1016/j.cub.2007.03.057.

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30

Stolarska, Magdalena, and Aravind R. Rammohan. "Spreading Out: Modeling the Physics of Cell-Substrate Interaction in Cell Spreading and Focal Adhesion Evolution." Biophysical Journal 116, no. 3 (February 2019): 122a. http://dx.doi.org/10.1016/j.bpj.2018.11.680.

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31

Tolić-Nørrelykke, Iva Marija, and Ning Wang. "Traction in smooth muscle cells varies with cell spreading." Journal of Biomechanics 38, no. 7 (July 2005): 1405–12. http://dx.doi.org/10.1016/j.jbiomech.2004.06.027.

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32

Berrier, Allison L., Anthony M. Mastrangelo, Julian Downward, Mark Ginsberg, and Susan E. LaFlamme. "Activated R-Ras, Rac1, Pi 3-Kinase and Pkcε Can Each Restore Cell Spreading Inhibited by Isolated Integrin β1 Cytoplasmic Domains." Journal of Cell Biology 151, no. 7 (December 25, 2000): 1549–60. http://dx.doi.org/10.1083/jcb.151.7.1549.

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Attachment of many cell types to extracellular matrix proteins triggers cell spreading, a process that strengthens cell adhesion and is a prerequisite for many adhesion-dependent processes including cell migration, survival, and proliferation. Cell spreading requires integrins with intact β cytoplasmic domains, presumably to connect integrins with the actin cytoskeleton and to activate signaling pathways that promote cell spreading. Several signaling proteins are known to regulate cell spreading, including R-Ras, PI 3-kinase, PKCε and Rac1; however, it is not known whether they do so through a mechanism involving integrin β cytoplasmic domains. To study the mechanisms whereby cell spreading is regulated by integrin β cytoplasmic domains, we inhibited cell spreading on collagen I or fibrinogen by expressing tac-β1, a dominant-negative inhibitor of integrin function, and examined whether cell spreading could be restored by the coexpression of either V38R-Ras, p110α-CAAX, myr-PKCε, or L61Rac1. Each of these activated signaling proteins was able to restore cell spreading as assayed by an increase in the area of cells expressing tac-β1. R-Ras and Rac1 rescued cell spreading in a GTP-dependent manner, whereas PKCε required an intact kinase domain. Importantly, each of these signaling proteins required intact β cytoplasmic domains on the integrins mediating adhesion in order to restore cell spreading. In addition, the rescue of cell spreading by V38R-Ras was inhibited by LY294002, suggesting that PI 3-kinase activity is required for V38R-Ras to restore cell spreading. In contrast, L61Rac1 and myr-PKCε each increased cell spreading independent of PI 3-kinase activity. Additionally, the dominant-negative mutant of Rac1, N17Rac1, abrogated cell spreading and inhibited the ability of p110α-CAAX and myr-PKCε to increase cell spreading. These studies suggest that R-Ras, PI 3-kinase, Rac1 and PKCε require the function of integrin β cytoplasmic domains to regulate cell spreading and that Rac1 is downstream of PI 3-kinase and PKCε in a pathway involving integrin β cytoplasmic domain function in cell spreading.
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33

Runyan, R. B., J. Versalovic, and B. D. Shur. "Functionally distinct laminin receptors mediate cell adhesion and spreading: the requirement for surface galactosyltransferase in cell spreading." Journal of Cell Biology 107, no. 5 (November 1, 1988): 1863–71. http://dx.doi.org/10.1083/jcb.107.5.1863.

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The molecular mechanisms underlying cell attachment and subsequent cell spreading on laminin are shown to be distinct form one another. Cell spreading is dependent upon the binding of cell surface galactosyltransferase (GalTase) to laminin oligosaccharides, while initial cell attachment to laminin occurs independent of GalTase activity. Anti-GalTase IgG, as well as the GalTase modifier protein, alpha-lactalbumin, both block GalTase activity and inhibited B16-F10 melanoma cell spreading on laminin, but not initial attachment. On the other hand, the addition of UDP galactose, which increases the catalytic turnover of GalTase, slightly increased cell spreading. None of these reagents had any effect on cell spreading on fibronectin. When GalTase substrates within laminin were either blocked by affinity-purified GalTase or eliminated by prior galactosylation, cell attachment appeared normal, but subsequent cell spreading was totally inhibited. The laminin substrate for GalTase was identified as N-linked oligosaccharides primarily on the A chain, and to a lesser extent on B chains. That N-linked oligosaccharides are necessary for cell spreading was shown by the inability of cells to spread on laminin surfaces pretreated with N-glycanase, even though cell attachment was normal. Cell surface GalTase was distinguished from other reported laminin binding proteins, most notably the 68-kD receptor, since they were differentially eluted from laminin affinity columns. These data show that surface GalTase does not participate during initial cell adhesion to laminin, but mediates subsequent cell spreading by binding to its appropriate N-linked oligosaccharide substrate. These results also emphasize that some of laminin's biological properties can be attributed to its oligosaccharide residues.
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34

Baldassarre, Massimiliano, Ziba Razinia, Clara F. Burande, Isabelle Lamsoul, Pierre G. Lutz, and David A. Calderwood. "Filamins Regulate Cell Spreading and Initiation of Cell Migration." PLoS ONE 4, no. 11 (November 13, 2009): e7830. http://dx.doi.org/10.1371/journal.pone.0007830.

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35

Li, Yuan, David Lovett, Qiao Zhang, Srujana Neelam, Ram Anirudh Kuchibhotla, Ruijun Zhu, Gregg G. Gundersen, Tanmay P. Lele, and Richard B. Dickinson. "Moving Cell Boundaries Drive Nuclear Shaping during Cell Spreading." Biophysical Journal 109, no. 4 (August 2015): 670–86. http://dx.doi.org/10.1016/j.bpj.2015.07.006.

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36

Lebakken, C. S., and A. C. Rapraeger. "Syndecan-1 mediates cell spreading in transfected human lymphoblastoid (Raji) cells." Journal of Cell Biology 132, no. 6 (March 15, 1996): 1209–21. http://dx.doi.org/10.1083/jcb.132.6.1209.

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Syndecan-1 is a cell surface proteoglycan containing a highly conserved transmembrane and cytoplasmic domain, and an extracellular domain bearing heparan sulfate glycosaminoglycans. Through these domains, syndecan-1 is proposed to have roles in growth factor action, extracellular matrix adhesion, and cytoskeletal organization that controls cell morphology. To study the role of syndecan-1 in cell adhesion and cytoskeleton reorganization, mouse syndecan-1 cDNA was transfected into human Raji cells, a lymphoblastoid cell line that grows as suspended cells and exhibits little or no endogenous cell surface heparan sulfate. High expressing transfectants (Raji-Sl cells) bind to and spread on immobilized thrombospondin or fibronectin, which are ligands for the heparan sulfate chains of the proteoglycan. This binding and spreading as not dependent on the cytoplasmic domain of the core protein, is mutants expressing core proteins with cytoplasmic deletions maintain the ability to spread. The spreading is mediated through engagement of the syndecan-1 core protein, as the Raji-S 1 cells also bind to and spread on immobilized mAb 281.2, an antibody specific for the ectodomain of the syndecan-1 core protein. Spreading on the antibody is independent of the heparan sulfate glycosaminoglycan chains and can be inhibited by competition with soluble mAb 281.2. The spreading can be inhibited by treatment with cytochalasin D or colchicine. These data suggest that the core protein of syndecan-1 mediates spreading through the formation of a multimolecular signaling complex at the cell surface that signals cytoskeleton reorganization. This complex may form via intramembrane or extracellular interactions with the syndecan core protein.
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37

Kritikou, Ekat. "Restricting the spreading." Nature Reviews Molecular Cell Biology 7, no. 3 (March 2006): 155. http://dx.doi.org/10.1038/nrm1898.

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38

Stockton, Rebecca A., and Bruce S. Jacobson. "Modulation of Cell-Substrate Adhesion by Arachidonic Acid: Lipoxygenase Regulates Cell Spreading and ERK1/2-inducible Cyclooxygenase Regulates Cell Migration in NIH-3T3 Fibroblasts." Molecular Biology of the Cell 12, no. 7 (July 2001): 1937–56. http://dx.doi.org/10.1091/mbc.12.7.1937.

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Adhesion of cells to an extracellular matrix is characterized by several discrete morphological and functional stages beginning with cell-substrate attachment, followed by cell spreading, migration, and immobilization. We find that although arachidonic acid release is rate-limiting in the overall process of adhesion, its oxidation by lipoxygenase and cyclooxygenases regulates, respectively, the cell spreading and cell migration stages. During the adhesion of NIH-3T3 cells to fibronectin, two functionally and kinetically distinct phases of arachidonic acid release take place. An initial transient arachidonate release occurs during cell attachment to fibronectin, and is sufficient to signal the cell spreading stage after its oxidation by 5-lipoxygenase to leukotrienes. A later sustained arachidonate release occurs during and after spreading, and signals the subsequent migration stage through its oxidation to prostaglandins by newly synthesized cyclooxygenase-2. In signaling migration, constitutively expressed cyclooxygenase-1 appears to contribute ∼25% of prostaglandins synthesized compared with the inducible cyclooxygenase-2. Both the second sustained arachidonate release, and cyclooxygenase-2 protein induction and synthesis, appear to be regulated by the mitogen-activated protein kinase extracellular signal-regulated kinase (ERK)1/2. The initial cell attachment-induced transient arachidonic acid release that signals spreading through lipoxygenase oxidation is not sensitive to ERK1/2 inhibition by PD98059, whereas PD98059 produces both a reduction in the larger second arachidonate release and a blockade of induced cyclooxygenase-2 protein expression with concomitant reduction of prostaglandin synthesis. The second arachidonate release, and cyclooxygenase-2 expression and activity, both appear to be required for cell migration but not for the preceding stages of attachment and spreading. These data suggest a bifurcation in the arachidonic acid adhesion-signaling pathway, wherein lipoxygenase oxidation generates leukotriene metabolites regulating the spreading stage of cell adhesion, whereas ERK 1/2-induced cyclooxygenase synthesis results in oxidation of a later release, generating prostaglandin metabolites regulating the later migration stage.
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39

Morrison, R. F., and E. R. Seidel. "Cell spreading and the regulation of ornithine decarboxylase." Journal of Cell Science 108, no. 12 (December 1, 1995): 3787–94. http://dx.doi.org/10.1242/jcs.108.12.3787.

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The aim of this study was to investigate the effect of cell spreading on the induction of ornithine decarboxylase and the rate of putrescine uptake in anchorage-dependent and anchorage-independent cells. Plating non-transformed IEC-6 epithelial cells at high versus low cell density restricted cell spreading from 900 microns 2 to approximately 140 microns 2, blunted the transient induction of ornithine decarboxylase activity from 202 to 32 pmol 14CO2/mg protein per hour and reduced the rate of [14C] putrescine uptake from 46 to 23 pmol/10(5) cells per hour. The mean spreading area of the cell population was controlled by coating tissue culture dishes with the nonadhesive polymer, polyHEMA. Ornithine decarboxylase activity and putrescine uptake correlated with cell spreading with minimal spreading (263 microns 2) corresponding to an 83% decrease in ornithine decarboxylase activity and 51% decrease in the rate of putrescine uptake. Adding the RGD peptide, Gly-Arg-Gly-Glu-Ser-Pro to the medium of sparsely plated cells resulted in rapid reductions in cell spreading concomitant with dose-dependent decreases in ornithine decarboxylase activity and putrescine uptake. Finally, minimizing cell spreading by depriving cells of substratum contact completely abolished serum-induced increases in ornithine decarboxylase and reduced the rate of putrescine uptake by 47%. In contrast to IEC-6 cells, ornithine decarboxylase of neoplastic HTC-116 cells was constitutively expressed with basal and stimulated activity (193 and 982 pmol 14CO2/mg protein per hour, respectively) completely independent of cell adhesion. Putrescine uptake, however, was abolished in the absence of cell adhesion. These data suggest that the induction of ornithine decarboxylase activity and the rate of putrescine uptake correlate with spreading of anchorage-dependent IEC-6 cells and that ornithine decarboxylase activity but not putrescine uptake, appears to be independent of spreading of neoplastic HTC-116 cells.
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40

Chun, J. S., and B. S. Jacobson. "Requirement for diacylglycerol and protein kinase C in HeLa cell-substratum adhesion and their feedback amplification of arachidonic acid production for optimum cell spreading." Molecular Biology of the Cell 4, no. 3 (March 1993): 271–81. http://dx.doi.org/10.1091/mbc.4.3.271.

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Release of arachidonic acid (AA) and subsequent formation of a lipoxygenase (LOX) metabolite(s) is an obligatory signal to induce spreading of HeLa cells on a gelatin substratum (Chun and Jacobson, 1992). This study characterizes signaling pathways that follow the LOX metabolite(s) formation. Levels of diacylglycerol (DG) increase upon attachment and before cell spreading on a gelatin substratum. DG production and cell spreading are insignificant when phospholipase A2 (PLA2) or LOX is blocked. In contrast, when cells in suspension where PLA2 activity is not stimulated are treated with exogenous AA, DG production is turned on, and inhibition of LOX turns it off. This indicates that the formation of a LOX metabolite(s) from AA released during cell attachment induces the production of DG. Consistent with the DG production is the activation of protein kinase C (PKC) which, as with AA and DG, occurs upon attachment and before cell spreading. Inhibition of AA release and subsequent DG production blocks both PKC activation and cell spreading. Cell spreading is also blocked by the inhibition of PKC with calphostin C or sphingosine. The inhibition of cell spreading induced by blocking AA release is reversed by the direct activation of PKC with phorbol ester. However, the inhibition of cell spreading induced by PKC inhibition is not reversed by exogenously applied AA. In addition, inhibition of PKC does not block AA release and DG production. The data indicate that there is a sequence of events triggered by HeLa cell attachment to a gelatin substratum that leads to the initiation of cell spreading: AA release, a LOX metabolite(s) formation, DG production, and PKC activation. The data also provide evidence indicating that HeLa cell spreading is a cyclic feedback amplification process centered on the production of AA, which is the first messenger produced in the sequence of messengers initiating cell spreading. Both DG and PKC activity that are increased during HeLa cell attachment to a gelatin substratum appear to be involved. DG not only activates PKC, which is essential for cell spreading, but is also hydrolyzed to AA. PKC, which is initially activated as consequence of AA production, also increases more AA production by activating PLA2.
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Arthur, William T., Lawrence A. Quilliam, and Jonathan A. Cooper. "Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors." Journal of Cell Biology 167, no. 1 (October 11, 2004): 111–22. http://dx.doi.org/10.1083/jcb.200404068.

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The Ras-related GTPase Rap1 stimulates integrin-mediated adhesion and spreading in various mammalian cell types. Here, we demonstrate that Rap1 regulates cell spreading by localizing guanine nucleotide exchange factors (GEFs) that act via the Rho family GTPase Rac1. Rap1a activates Rac1 and requires Rac1 to enhance spreading, whereas Rac1 induces spreading independently of Rap1. Active Rap1a binds to a subset of Rac GEFs, including VAV2 and Tiam1 but not others such as SWAP-70 or COOL-1. Overexpressed VAV2 and Tiam1 specifically require Rap1 to promote spreading, even though Rac1 is activated independently of Rap1. Rap1 is necessary for the accumulation of VAV2 in membrane protrusions at the cell periphery. In addition, if VAV2 is artificially localized to the cell edge with the subcellular targeting domain of Rap1a, it increases cell spreading independently of Rap1. These results lead us to propose that Rap1 promotes cell spreading by localizing a subset of Rac GEFs to sites of active lamellipodia extension.
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42

Roll, Richard L., Eve Marie Bauman, Joel S. Bennett, and Charles S. Abrams. "Phosphorylated Pleckstrin Induces Cell Spreading via an Integrin-Dependent Pathway." Journal of Cell Biology 150, no. 6 (September 18, 2000): 1461–66. http://dx.doi.org/10.1083/jcb.150.6.1461.

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Pleckstrin is a 40-kD phosphoprotein containing NH2- and COOH-terminal pleckstrin homology (PH) domains separated by a disheveled-egl 10-pleckstrin (DEP) domain. After platelet activation, pleckstrin is rapidly phosphorylated by protein kinase C. We reported previously that expressed phosphorylated pleckstrin induces cytoskeletal reorganization and localizes in microvilli along with glycoproteins, such as integrins. Given the role of integrins in cytoskeletal organization and cell spreading, we investigated whether signaling from pleckstrin cooperated with signaling pathways involving the platelet integrin, αIIbβ3. Pleckstrin induced cell spreading in both transformed (COS-1 & CHO) and nontransformed (REF52) cell lines, and this spreading was regulated by pleckstrin phosphorylation. In REF52 cells, pleckstrin-induced spreading was matrix dependent, as evidenced by spreading of these cells on fibrinogen but not on fibronectin. Coexpression with αIIbβ3 did not enhance pleckstrin-mediated cell spreading in either REF52 or CHO cells. However, coexpression of the inactive variant αIIbβ3 Ser753Pro, or β3 Ser753Pro alone, completely blocked pleckstrin-induced spreading. This implies that αIIbβ3 Ser753Pro functions as a competitive inhibitor by blocking the effects of an endogenous receptor that is used in the signaling pathway involved in pleckstrin-induced cell spreading. Expression of a chimeric protein composed of the extracellular and transmembrane portion of Tac fused to the cytoplasmic tail of β3 completely blocked pleckstrin-mediated spreading, whereas chimeras containing the cytoplasmic tail of β3 Ser753Pro or αIIb had no effect. This suggests that the association of an unknown signaling protein with the cytoplasmic tail of an endogenous integrin β-chain is also required for pleckstrin-induced spreading. Thus, expressed phosphorylated pleckstrin promotes cell spreading that is both matrix and integrin dependent. To our knowledge, this is the first example of a mutated integrin functioning as a dominant negative inhibitor.
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43

Hurtley, S. M. "Spreading the Word." Science Signaling 1, no. 27 (July 8, 2008): ec248-ec248. http://dx.doi.org/10.1126/scisignal.127ec248.

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Pinon, Perrine, Jenita Pärssinen, Patricia Vazquez, Michael Bachmann, Rolle Rahikainen, Marie-Claude Jacquier, Latifeh Azizi, et al. "Talin-bound NPLY motif recruits integrin-signaling adapters to regulate cell spreading and mechanosensing." Journal of Cell Biology 205, no. 2 (April 28, 2014): 265–81. http://dx.doi.org/10.1083/jcb.201308136.

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Integrin-dependent cell adhesion and spreading are critical for morphogenesis, tissue regeneration, and immune defense but also tumor growth. However, the mechanisms that induce integrin-mediated cell spreading and provide mechanosensing on different extracellular matrix conditions are not fully understood. By expressing β3-GFP-integrins with enhanced talin-binding affinity, we experimentally uncoupled integrin activation, clustering, and substrate binding from its function in cell spreading. Mutational analysis revealed Tyr747, located in the first cytoplasmic NPLY747 motif, to induce spreading and paxillin adapter recruitment to substrate- and talin-bound integrins. In addition, integrin-mediated spreading, but not focal adhesion localization, was affected by mutating adjacent sequence motifs known to be involved in kindlin binding. On soft, spreading-repellent fibronectin substrates, high-affinity talin-binding integrins formed adhesions, but normal spreading was only possible with integrins competent to recruit the signaling adapter protein paxillin. This proposes that integrin-dependent cell–matrix adhesion and cell spreading are independently controlled, offering new therapeutic strategies to modify cell behavior in normal and pathological conditions.
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Chandrasekaran, S., M. L. Tanzer, and M. S. Giniger. "Oligomannosides initiate cell spreading of laminin-adherent murine melanoma cells." Journal of Biological Chemistry 269, no. 5 (February 1994): 3356–66. http://dx.doi.org/10.1016/s0021-9258(17)41870-9.

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46

Flevaris, Panagiotis, Aleksandra Stojanovic, Haixia Gong, Athar Chishti, Emily Welch, and Xiaoping Du. "A molecular switch that controls cell spreading and retraction." Journal of Cell Biology 179, no. 3 (October 29, 2007): 553–65. http://dx.doi.org/10.1083/jcb.200703185.

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Integrin-dependent cell spreading and retraction are required for cell adhesion, migration, and proliferation, and thus are important in thrombosis, wound repair, immunity, and cancer development. It remains unknown how integrin outside-in signaling induces and controls these two opposite processes. This study reveals that calpain cleavage of integrin β3 at Tyr759 switches the functional outcome of integrin signaling from cell spreading to retraction. Expression of a calpain cleavage–resistant β3 mutant in Chinese hamster ovary cells causes defective clot retraction and RhoA-mediated retraction signaling but enhances cell spreading. Conversely, a calpain-cleaved form of β3 fails to mediate cell spreading, but inhibition of the RhoA signaling pathway corrects this defect. Importantly, the calpain-cleaved β3 fails to bind c-Src, which is required for integrin-induced cell spreading, and this requirement of β3-associated c-Src results from its inhibition of RhoA-dependent contractile signals. Thus, calpain cleavage of β3 at Tyr759 relieves c-Src–mediated RhoA inhibition, activating the RhoA pathway that confines cell spreading and causes cell retraction.
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Kovaleva, A. V., A. V. Tvorogova, and A. A. Saidova. "SPREADING MECHANISMS OF CATTLE MESHENYMAL STEM CELL." International Journal of Applied and Fundamental Research (Международный журнал прикладных и фундаментальных исследований) 1, no. 12 2018 (2018): 70–79. http://dx.doi.org/10.17513/mjpfi.12524.

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48

Wu, Di, Yong Hou, Zhiqin Chu, Qiang Wei, Wei Hong, and Yuan Lin. "Ligand Mobility-Mediated Cell Adhesion and Spreading." ACS Applied Materials & Interfaces 14, no. 11 (March 13, 2022): 12976–83. http://dx.doi.org/10.1021/acsami.1c22603.

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49

Potter, David A., Jennifer S. Tirnauer, Richard Janssen, Dorothy E. Croall, Christina N. Hughes, Kerry A. Fiacco, James W. Mier, Masatoshi Maki, and Ira M. Herman. "Calpain Regulates Actin Remodeling during Cell Spreading." Journal of Cell Biology 141, no. 3 (May 4, 1998): 647–62. http://dx.doi.org/10.1083/jcb.141.3.647.

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Previous studies suggest that the Ca2+-dependent proteases, calpains, participate in remodeling of the actin cytoskeleton during wound healing and are active during cell migration. To directly test the role that calpains play in cell spreading, several NIH-3T3– derived clonal cell lines were isolated that overexpress the biological inhibitor of calpains, calpastatin. These cells stably overexpress calpastatin two- to eightfold relative to controls and differ from both parental and control cell lines in morphology, spreading, cytoskeletal structure, and biochemical characteristics. Morphologic characteristics of the mutant cells include failure to extend lamellipodia, as well as abnormal filopodia, extensions, and retractions. Whereas wild-type cells extend lamellae within 30 min after plating, all of the calpastatin-overexpressing cell lines fail to spread and assemble actin-rich processes. The cells genetically altered to overexpress calpastatin display decreased calpain activity as measured in situ or in vitro. The ERM protein ezrin, but not radixin or moesin, is markedly increased due to calpain inhibition. To confirm that inhibition of calpain activity is related to the defect in spreading, pharmacological inhibitors of calpain were also analyzed. The cell permeant inhibitors calpeptin and MDL 28, 170 cause immediate inhibition of spreading. Failure of the intimately related processes of filopodia formation and lamellar extension indicate that calpain is intimately involved in actin remodeling and cell spreading.
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50

Chenette, Emily J. "Talin shifts cell spreading into high gear." Nature Reviews Molecular Cell Biology 9, no. 10 (September 17, 2008): 738. http://dx.doi.org/10.1038/nrm2517.

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