The role of cell-cell contact in ?contact? inhibition of cell division: A review and new evidence

1972 ◽  
Vol 79 (2) ◽  
pp. 189-210 ◽  
Author(s):  
Eric Martz ◽  
Malcolm S. Steinberg
Keyword(s):  
Cell Division ◽  
Contact Inhibition ◽  
Cell Contact ◽  
New Evidence ◽  
Cell Cell

scholarly journals Non-junctional role of Cadherin3 in cell migration and contact inhibition of locomotion via domain-dependent, opposing regulation of Rac1

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Takehiko Ichikawa ◽  
Carsten Stuckenholz ◽  
Lance A. Davidson
Keyword(s):  
Cell Migration ◽  
Contact Inhibition ◽  
Cell Contact ◽  
Collective Cell Migration ◽  
Rac1 Activity ◽  
Classical Cadherins ◽  
Migration Assays ◽  
Spatio Temporal ◽  
Cell Cell

Abstract Classical cadherins are well-known adhesion molecules responsible for physically connecting neighboring cells and signaling this cell–cell contact. Recent studies have suggested novel signaling roles for “non-junctional” cadherins (NJCads); however, the function of cadherin signaling independent of cell–cell contacts remains unknown. In this study, mesendodermal cells and tissues from gastrula stage Xenopus laevis embryos demonstrate that deletion of extracellular domains of Cadherin3 (Cdh3; formerly C-cadherin in Xenopus) disrupts contact inhibition of locomotion. In both bulk Rac1 activity assays and spatio-temporal FRET image analysis, the extracellular and cytoplasmic Cdh3 domains disrupt NJCad signaling and regulate Rac1 activity in opposing directions. Stabilization of the cytoskeleton counteracted this regulation in single cell migration assays. Our study provides novel insights into adhesion-independent signaling by Cadherin3 and its role in regulating single and collective cell migration.

Low-affinity LFA-1/ICAM-3 interactions augment LFA-1/ICAM-1-mediated T cell adhesion and signaling by redistribution of LFA-1

2000 ◽  
Vol 113 (3) ◽  
pp. 391-400 ◽  
Author(s):  
D.A. Bleijs ◽  
M.E. Binnerts ◽  
S.J. van Vliet ◽  
C.G. Figdor ◽  
Y. van Kooyk
Keyword(s):  
T Cell ◽  
Cell Interactions ◽  
T Cell Proliferation ◽  
Cell Contact ◽  
Surface Distribution ◽  
Affinity Ligand ◽  
Large Clusters ◽  
High Affinity Ligand ◽  
Cell Cell

Although ICAM-3 is implicated in both adhesion and signal transduction events of leukocytes, its low affinity for LFA-1 compared to other ligands of LFA-1 has puzzled many investigators. Here we investigated the role of ICAM-3 in supporting LFA-1-mediated ICAM-1 binding and subsequently cell signaling. We observed that although ICAM-3 binds poorly to LFA-1 expressed on resting T cells, it specifically facilitates and increases LFA-1-mediated adhesion to the high affinity ligand of LFA-1, ICAM-1. We demonstrate that low-affinity binding of LFA-1 to ICAM-3 together with ICAM-1 alters the cell surface distribution of LFA-1 dramatically, inducing large clusters of LFA-1 that facilitate ICAM-1 binding after LFA-1 activation. We found that LFA-1-mediated ICAM-1 cell-cell interactions such as T cell proliferation greatly depend on low affinity LFA-1/ICAM-3 interactions that enhance stable LFA-1/ICAM-1 cell-cell contact. Taken together, these data demonstrate that low affinity LFA-1 binding to ICAM-3 regulates strong LFA-1/ICAM-1-mediated adhesion by driving LFA-1 into clusters to facilitate cell-cell interactions that take place in the immune system.

scholarly journals Endocannabinoid Signaling in Embryonic Neuronal Motility and Cell–Cell Contact – Role of mGluR5 and TRPC3 Channels

Neuroscience ◽  
2018 ◽  
Vol 375 ◽  
pp. 135-148 ◽  
Author(s):  
Pauli M. Turunen ◽  
Lauri M. Louhivuori ◽  
Verna Louhivuori ◽  
Jyrki P. Kukkonen ◽  
Karl E. Åkerman
Keyword(s):  
Cell Contact ◽  
Cell Cell

Role of cell–cell contact in the preservation of differentiation and response to thyrotrophin in cultured porcine thyroid cells

1987 ◽  
Vol 113 (2) ◽  
pp. 223-NP ◽  
Author(s):  
A. S. Yap ◽  
J. R. Bourke ◽  
S. W. Manley
Keyword(s):  
Follicular Development ◽  
Seeding Density ◽  
Cell Contact ◽  
Culture Dish ◽  
Thyroid Cells ◽  
A Cell ◽  
Free Membrane ◽  
Zero Time ◽  
Cell Cell

ABSTRACT Cultured porcine thyroid cells did not reassociate into functional follicles in the presence of TSH unless the initial seeding density was adequate. At 0·2 × 106 cells/35 mm diameter culture dish the cells rapidly formed a monolayer even in the presence of TSH (128 μu./ml), and radioiodide uptake was not significantly increased compared with that in control cells. Seeding densities of 1–3 × 106 cells/dish resulted in cultures which responded to TSH with follicular development and increased radioiodide uptake. A cell-free membrane fraction of thyroid homogenate restored the ability of cultures seeded at low densities to respond to TSH with development of follicular morphology and increased radioiodide uptake. Delaying the addition of TSH by 48 h markedly reduced the stimulation of follicular development and radioiodide uptake of cultures. Addition of membrane fractions, or an alkali-soluble fraction of membranes, at zero time improved the responses to TSH added after a 48-h delay. It was concluded that maintenance of differentiation and of TSH-responsiveness in cultured thyroid cells was influenced by cell–cell contact. J. Endocr. (1987) 113, 223–229

scholarly journals Role of Fat1 in cell-cell contact formation of podocytes in puromycin aminonucleoside nephrosis and neonatal kidney

2005 ◽  
Vol 68 (2) ◽  
pp. 542-551 ◽  
Author(s):  
Eishin Yaoita ◽  
Hidetake Kurihara ◽  
Yutaka Yoshida ◽  
Tsutomu Inoue ◽  
Asako Matsuki ◽  
...  
Keyword(s):  
Cell Contact ◽  
Puromycin Aminonucleoside ◽  
Contact Formation ◽  
Neonatal Kidney ◽  
Aminonucleoside Nephrosis ◽  
Puromycin Aminonucleoside Nephrosis ◽  
Cell Cell

Polymorphonuclear Leukocyte-Platelet Interaction: Role of P-Selectin in Thromboxane B2 and Leukotriene C4 Cooperative Synthesis

1994 ◽  
Vol 72 (03) ◽  
pp. 450-456 ◽  
Author(s):  
Norma Maugeri ◽  
Virgilio Evangelista ◽  
Antonio Celardo ◽  
Giuseppe Dell’Elba ◽  
Nicola Martelli ◽  
...  
Keyword(s):  
Cell Aggregation ◽  
Inhibitory Effect ◽  
Cathepsin G ◽  
Cell Contact ◽  
Mixed Cell ◽  
Platelet Surface ◽  
Mixed Aggregates ◽  
Transcellular Metabolism ◽  
Cell Cell

SummaryIn PMN/platelet suspensions stimulated by fMLP giant mixed aggregates are formed and TxB2 and LTC4 are synthesized as the result of the cooperation in the arachidonic acid (AA) metabolism during cell/cell contact. PMN-derived cathepsin G induced the expression of P-selectin on platelet surface. GE12, an antibody against P-selectin, significantly reduced mixed cell aggregates. GE12 did not affect platelet aggregation induced by PMN-derived supernatants, indicating that the inhibitory effect of GE12 on mixed cell aggregation depends on inhibition of PMN/platelet adhesion. GE12 significantly reduced TxB2 and LTC4 production in PMN/platelet mixed cell suspensions stimulated by fMLP. As previously reported, synthesis of 3H-TxB2 in 3H-AA-labeled PMN/unlabeled platelets indicates that platelets utilize 3H-AA from PMN. 3H-LTC4 production in unlabeled PMN/3H-AA-labeled platelets indicates that bidirectional routes are utilized in this system for LTC4 synthesis. GE12 significantly reduced 3H-TxB2 and 3H-LTC4 synthesis. These results show that cathepsin G released by activated PMN induces the expression of P-selectin on platelet membrane: this adhesive glycoprotein modulates cell-cell contact and transcellular metabolism of AA.

scholarly journals Hydrodynamics of transient cell-cell contact: The role of membrane permeability and active protrusion length

2019 ◽  
Vol 15 (4) ◽  
pp. e1006352 ◽  
Author(s):  
Kai Liu ◽  
Brian Chu ◽  
Jay Newby ◽  
Elizabeth L. Read ◽  
John Lowengrub ◽  
...  
Keyword(s):  
Membrane Permeability ◽  
Cell Contact ◽  
Cell Cell

scholarly journals The role of spectrin in cell adhesion and cell–cell contact

2019 ◽  
Vol 244 (15) ◽  
pp. 1303-1312 ◽  
Author(s):  
Beata Machnicka ◽  
Renata Grochowalska ◽  
Dżamila M Bogusławska ◽  
Aleksander F Sikorski
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Biology ◽  
Membrane Integrity ◽  
Cell Contact ◽  
Surface Activities ◽  
New Findings ◽  
Cell Cell

Spectrins are proteins that are responsible for many aspects of cell function and adaptation to changing environments. Primarily the spectrin-based membrane skeleton maintains cell membrane integrity and its mechanical properties, together with the cytoskeletal network a support cell shape. The occurrence of a variety of spectrin isoforms in diverse cellular environments indicates that it is a multifunctional protein involved in numerous physiological pathways. Participation of spectrin in cell–cell and cell–extracellular matrix adhesion and formation of dynamic plasma membrane protrusions and associated signaling events is a subject of interest for researchers in the fields of cell biology and molecular medicine. In this mini-review, we focus on data concerning the role of spectrins in cell surface activities such as adhesion, cell–cell contact, and invadosome formation. We discuss data on different adhesion proteins that directly or indirectly interact with spectrin repeats. New findings support the involvement of spectrin in cell adhesion and spreading, formation of lamellipodia, and also the participation in morphogenetic processes, such as eye development, oogenesis, and angiogenesis. Here, we review the role of spectrin in cell adhesion and cell–cell contact.Impact statementThis article reviews properties of spectrins as a group of proteins involved in cell surface activities such as, adhesion and cell–cell contact, and their contribution to morphogenesis. We show a new area of research and discuss the involvement of spectrin in regulation of cell–cell contact leading to immunological synapse formation and in shaping synapse architecture during myoblast fusion. Data indicate involvement of spectrins in adhesion and cell–cell or cell–extracellular matrix interactions and therefore in signaling pathways. There is evidence of spectrin’s contribution to the processes of morphogenesis which are connected to its interactions with adhesion molecules, membrane proteins (and perhaps lipids), and actin. Our aim was to highlight the essential role of spectrin in cell–cell contact and cell adhesion.

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