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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 (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 (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 (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 (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 (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, et al. "Downregulation of Rap1GAP in Human Tumor Cells Alters Cell/Matrix and Cell/Cell Adhesion." Molecular and Cellular Biology 30, no. 13 (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

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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 (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 (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

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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 (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 filame

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10

Wells, William A. "Exclusion is spreading." Journal of Cell Biology 168, no. 1 (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 (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 (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

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13

Dunn, G. A., and D. Zicha. "Dynamics of fibroblast spreading." Journal of Cell Science 108, no. 3 (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

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14

Adler, E. M. "Spreading AMPylation?" Science Signaling 2, no. 66 (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 (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 (2008): 1017–19. http://dx.doi.org/10.1038/ncb0908-1017.

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17

Fardin, M. A., O. M. Rossier, P. Rangamani, et al. "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 (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 (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 (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 (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 (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 (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 (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 (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, s

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26

KEESE, C. "Substrate mechanics and cell spreading*1." Experimental Cell Research 195, no. 2 (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, et al. "The Universal Dynamics of Cell Spreading." Current Biology 17, no. 8 (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 (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 (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 (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 та 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, № 7 (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

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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 (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

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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 (2009): e7830. http://dx.doi.org/10.1371/journal.pone.0007830.

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35

Li, Yuan, David Lovett, Qiao Zhang, et al. "Moving Cell Boundaries Drive Nuclear Shaping during Cell Spreading." Biophysical Journal 109, no. 4 (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 (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

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37

Kritikou, Ekat. "Restricting the spreading." Nature Reviews Molecular Cell Biology 7, no. 3 (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 (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 transie

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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 (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 p

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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 (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 exogenou

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41

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 (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

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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 (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 plat

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43

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

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44

Pinon, Perrine, Jenita Pärssinen, Patricia Vazquez, et al. "Talin-bound NPLY motif recruits integrin-signaling adapters to regulate cell spreading and mechanosensing." Journal of Cell Biology 205, no. 2 (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 spreadi

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45

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 (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 (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 retractio

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47

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 (2022): 12976–83. http://dx.doi.org/10.1021/acsami.1c22603.

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49

Potter, David A., Jennifer S. Tirnauer, Richard Janssen, et al. "Calpain Regulates Actin Remodeling during Cell Spreading." Journal of Cell Biology 141, no. 3 (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

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50

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

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