scholarly journals On an evolution equation in a cell motility model

2016 ◽  
Vol 318-319 ◽  
pp. 12-25 ◽  
Author(s):  
Matthew S. Mizuhara ◽  
Leonid Berlyand ◽  
Volodymyr Rybalko ◽  
Lei Zhang
Keyword(s):  
Evolution Equation ◽  
Cell Motility ◽  
A Cell

scholarly journals A cell surface chondroitin sulfate proteoglycan, immunologically related to CD44, is involved in type I collagen-mediated melanoma cell motility and invasion.

1992 ◽  
Vol 116 (2) ◽  
pp. 521-531 ◽  
Author(s):  
A E Faassen ◽  
J A Schrager ◽  
D J Klein ◽  
T R Oegema ◽  
J R Couchman ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Motility ◽  
Chondroitin Sulfate ◽  
Melanoma Cell ◽  
Type I Collagen ◽  
Core Protein ◽  
Type I ◽  
Mouse Melanoma ◽  
Mouse Melanoma Cell ◽  
A Cell

The metastatic spread of tumor cells occurs through a complex series of events, one of which involves the adhesion of tumor cells to extracellular matrix (ECM) components. Multiple interactions between cell surface receptors of an adherent tumor cell and the surrounding ECM contribute to cell motility and invasion. The current studies evaluate the role of a cell surface chondroitin sulfate proteoglycan (CSPG) in the adhesion, motility, and invasive behavior of a highly metastatic mouse melanoma cell line (K1735 M4) on type I collagen matrices. By blocking mouse melanoma cell production of CSPG with p-nitrophenyl beta-D-xylopyranoside (beta-D-xyloside), a compound that uncouples chondroitin sulfate from CSPG core protein synthesis, we observed a corresponding decrease in melanoma cell motility on type I collagen and invasive behavior into type I collagen gels. Melanoma cell motility on type I collagen could also be inhibited by removing cell surface chondroitin sulfate with chondroitinase. In contrast, type I collagen-mediated melanoma cell adhesion and spreading were not affected by either beta-D-xyloside or chondroitinase treatments. These results suggest that mouse melanoma CSPG is not a primary cell adhesion receptor, but may play a role in melanoma cell motility and invasion at the level of cellular translocation. Furthermore, purified mouse melanoma cell surface CSPG was shown, by affinity chromatography and in solid phase binding assays, to bind to type I collagen and this interaction was shown to be mediated, at least in part, by chondroitin sulfate. Additionally we have determined that mouse melanoma CSPG is composed of a 110-kD core protein that is recognized by anti-CD44 antibodies on Western blots. Collectively, our data suggests that interactions between a cell surface CD44-related CSPG and type I collagen in the ECM may play an important role in mouse melanoma cell motility and invasion, and that the chondroitin sulfate portion of the proteoglycan seems to be a critical component in mediating this effect.

scholarly journals Lysophospholipids in the limelight

2002 ◽  
Vol 158 (2) ◽  
pp. 197-199 ◽  
Author(s):  
Wouter H. Moolenaar
Keyword(s):  
Growth Factor ◽  
Cell Motility ◽  
Tumor Progression ◽  
G Protein ◽  
Lysophosphatidic Acid ◽  
Cell Types ◽  
G Protein Coupled Receptors ◽  
Serum Phospholipid ◽  
A Cell ◽  
G Protein Coupled

Lysophosphatidic acid (LPA) is a serum phospholipid that evokes growth factor–like responses in many cell types through the activation of its G protein–coupled receptors. Although much is known about LPA signaling, it has remained unclear where and how bioactive LPA is produced. Umezu-Goto et al. (2002)(this issue, page 227) have purified a serum lysophospholipase D that generates LPA from lysophosphatidylcholine and found it to be identical to autotaxin, a cell motility–stimulating ectophosphodiesterase implicated in tumor progression. This result is surprising, as there was previously no indication that autotaxin could act as a phospholipase.

Benzofuran-Derived Cyclic β-Amino Acid Scaffold for Building a Diverse Set of Flavonoid-Like Probes and the Discovery of a Cell Motility Inhibitor

2008 ◽  
Vol 10 (6) ◽  
pp. 1143-1146 ◽  
Author(s):  
Jyoti P. Nandy ◽  
Bojana Rakic ◽  
Bugga V. N. B. Sarma ◽  
Nallareddy Babu ◽  
Marc Lefrance ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Motility ◽  
A Cell

scholarly journals A cell number-counting factor regulates the cytoskeleton and cell motility in Dictyostelium

2002 ◽  
Vol 99 (3) ◽  
pp. 1371-1376 ◽  
Author(s):  
L. Tang ◽  
T. Gao ◽  
C. McCollum ◽  
W. Jang ◽  
M. G. Vicker ◽  
...  
Keyword(s):  
Cell Motility ◽  
Cell Number ◽  
A Cell

2P2-J13 A development of a 3D cell tracking and fluorescence microscope system and its application to a cell motility research

2008 ◽  
Vol 2008 (0) ◽  
pp. _2P2-J13_1-_2P2-J13_4
Author(s):  
Takeshi OBARA ◽  
Yasunobu IGARASHI ◽  
Daisuke WAKO ◽  
Hiroshi TSUBOKAWA ◽  
Yasuo NAKAOKA ◽  
...  
Keyword(s):  
Cell Motility ◽  
Cell Tracking ◽  
Fluorescence Microscope ◽  
A Cell

scholarly journals Ena/Vasp: Solving a Cell Motility Paradox

2002 ◽  
Vol 12 (12) ◽  
pp. R417-R419 ◽  
Author(s):  
Louise P Cramer
Keyword(s):  
Cell Motility ◽  
A Cell

scholarly journals Cell-intrinsic activation of Orai1 regulates human T cell motility

2017 ◽  
Author(s):  
Tobias X. Dong ◽  
Milton L. Greenberg ◽  
Sabrina Leverrier ◽  
Ying Yu ◽  
Ian Parker ◽  
...  
Keyword(s):  
T Cells ◽  
T Cell ◽  
Lymph Nodes ◽  
Cell Motility ◽  
Cell Function ◽  
Immune Surveillance ◽  
Dominant Negative ◽  
Human T Cell ◽  
A Cell

AbstractCa2+ signaling through the store-operated Ca2+ channel, Orai1, is crucial for T cell function, but a role in regulating T cell motility in lymph nodes has not been previously reported. Tracking human T cells in immunodeficient mouse lymph nodes and in microfabricated PDMS channels, we show that inhibition of Orai1 channel activity with a dominant-negative Orai1-E106A construct increases average T cell velocities by reducing the frequency of pauses in motile T cells. Orai1-dependent motility arrest occurs spontaneously during confined motility in vitro, even in the absence of extrinsic cell contacts or antigen recognition. Utilizing a novel ratiometric genetically encoded cytosolic Ca2+ indicator, Salsa6f, we show these spontaneous pauses during T cell motility in vitro coincide with episodes of spontaneous cytosolic Ca2+ signaling. Our results demonstrate that Orai1, activated in a cell-intrinsic manner, regulates T cell motility patterns that accompany immune surveillance.

Cellular adhesiveness, contractility, and traction: stick, grip, and slip control

1995 ◽  
Vol 73 (7-8) ◽  
pp. 311-316 ◽  
Author(s):  
Michal Opas
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Motility ◽  
Motive Force ◽  
Slip Control ◽  
Focal Contacts ◽  
A Cell ◽  
Tractional Forces ◽  
Structural Connection ◽  
Fine Tune

Translocation of cells over solid substrata depends on generation of motive force, in crawling tissue cells, brought about by regulated contractility of intracellular actomyosin. Intracellular contractile machinery has a direct, structural connection to the cell surface. Hence, regulated adhesiveness of the cell surface provides a mechanism whereby a cell can fine tune the extent of tractional forces that are necessary for effective translocation. Cells are able to control adhesiveness of surfaces (stick), contractility (grip), and the extent of traction exerted on the substratum (slip). Here, I discuss several aspects of local (subcellular) regulation of adhesiveness and contractility and speculate on how cells, given a choice of the substratum, decide on how and where to apply traction.Key words: cell adhesion, focal contacts, cell motility, traction, cytomechanics.

Sign in / Sign up

Export Citation Format

Share Document