Cell-Adhesion to Crystal Surfaces: Adhesion-Induced Physiological Cell Death

Abstract During development signaling pathways coordinate cell fates and regulate the choice between cell survival or programmed cell death. The well-conserved Wingless/Wnt pathway is required for many developmental decisions in all animals. One transducer of the Wingless/Wnt signal is Armadillo/β-catenin. Drosophila Armadillo not only transduces Wingless signal, but also acts in cell-cell adhesion via its role in the epithelial adherens junction. While many components of both the Wingless/Wnt signaling pathway and adherens junctions are known, both processes are complex, suggesting that unknown components influence signaling and junctions. We carried out a genetic modifier screen to identify some of these components by screening for mutations that can suppress the armadillo mutant phenotype. We identified 12 regions of the genome that have this property. From these regions and from additional candidate genes tested we identified four genes that suppress arm: dTCF, puckered, head involution defective (hid), and Dpresenilin. We further investigated the interaction with hid, a known regulator of programmed cell death. Our data suggest that Wg signaling modulates Hid activity and that Hid regulates programmed cell death in a dose-sensitive fashion.

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Protein Synthesis during Programmed (Physiological) Cell Death

Chemical Carcinogenesis 2 ◽

10.1007/978-1-4615-3694-9_45 ◽

1991 ◽

pp. 451-459

Author(s):

R. A. Lockshin ◽

Z. F. Zakeri ◽

L. M. Yesner

Keyword(s):

Cell Death ◽

Protein Synthesis ◽

Physiological Cell Death

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Cathepsin D gene expression outlines the areas of physiological cell death during embryonic development

Developmental Dynamics ◽

10.1002/dvdy.21076 ◽

2007 ◽

Vol 236 (3) ◽

pp. 880-885 ◽

Cited By ~ 21

Author(s):

V. Zuzarte-Luis ◽

J.A. Montero ◽

N. Torre-Perez ◽

J.A. Garcia-Porrero ◽

J.M. Hurle

Keyword(s):

Gene Expression ◽

Cell Death ◽

Embryonic Development ◽

Cathepsin D ◽

Physiological Cell Death

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Role of LFA-1/ICAM-1-dependent cell adhesion in CD40-mediated inhibition of anti-IgM antibody-induced B-cell death

Journal of Allergy and Clinical Immunology ◽

10.1016/s0091-6749(95)70198-2 ◽

1995 ◽

Vol 96 (6) ◽

pp. 1136-1144 ◽

Cited By ~ 3

Author(s):

M MAYUMI ◽

S SUMIMOTO ◽

Y OHSHIMA ◽

K KATAMURA ◽

T HEIKE ◽

...

Keyword(s):

Cell Death ◽

Cell Adhesion ◽

B Cell ◽

Igm Antibody ◽

Dependent Cell

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Selective interactions of cells with crystal surfaces. Implications for the mechanism of cell adhesion

Journal of Cell Science ◽

10.1242/jcs.104.2.275 ◽

1993 ◽

Vol 104 (2) ◽

pp. 275-288

Author(s):

D. Hanein ◽

H. Sabanay ◽

L. Addadi ◽

B. Geiger

Keyword(s):

Cell Adhesion ◽

Protein S ◽

Surface Topology ◽

Water Molecules ◽

Cell Binding ◽

Crystal Surfaces ◽

Limited Effect ◽

Surface Distribution ◽

Adsorbed Proteins ◽

Adhesive Interactions

In this study we have characterized the mode of cell adhesion to calcite and calcium (R,R)-tartrate tetrahydrate crystals. The use of crystals as adhesion substrata was motivated by their well-established chemical nature and structurally defined surfaces. We show that calcite binds A6 Xenopus laevis epithelial cells rapidly and efficiently, most likely via surface-adsorbed proteins. Surface topology had only a limited effect on the adhesive interactions. Calcium (R,R)-tartrate tetrahydrate crystals exhibits two chemically equivalent, yet structurally distinct faces that differ mainly in the surface distribution of their lattice water molecules and charges. However, despite the gross similarity between the two faces striking differences were noted in their adhesive behavior. One of the faces was highly adhesive for cells, leading to protein-independent attachment and spreading followed by cell death. In contrast, cell adhesion to the other surface of tartrate was slow (> 24 h) and apparently mediated by RGD-containing protein(s). It was further shown that the latter face of tartrate crystals could be “conditioned” by long (24 h) incubation with serum-containing medium, after which it becomes highly adhesive. The results presented here indicate that crystal surfaces may serve as excellent, structurally defined, substrata for cell adhesion, that cell binding may occur directly or via RGD-containing proteins and that cell adhesion may be dramatically modulated by variations in surface structure. The implications of the results to the mechanism of cell-substratum adhesion are discussed.

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Morphogenesis: Shaping by Active Cell Movement, Differential Cell Adhesion and Cell Death

Development and Reproduction in Humans and Animal Model Species ◽

10.1007/978-3-662-43784-1_14 ◽

2014 ◽

pp. 433-442

Author(s):

Werner A. Mueller ◽

Monika Hassel ◽

Maura Grealy

Keyword(s):

Cell Death ◽

Cell Adhesion ◽

Cell Movement ◽

Active Cell ◽

Differential Cell

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The medical significance of physiological cell death

Medicinal Research Reviews ◽

10.1002/med.2610150404 ◽

1995 ◽

Vol 15 (4) ◽

pp. 299-311 ◽

Cited By ~ 14

Author(s):

Georg Häucker ◽

David L. Vaux

Keyword(s):

Cell Death ◽

Physiological Cell Death

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FRL, a Novel Formin-Related Protein, Binds to Rac and Regulates Cell Motility and Survival of Macrophages

Molecular and Cellular Biology ◽

10.1128/mcb.20.18.6872-6881.2000 ◽

2000 ◽

Vol 20 (18) ◽

pp. 6872-6881 ◽

Cited By ~ 71

Author(s):

Shinri Yayoshi-Yamamoto ◽

Ichiro Taniuchi ◽

Takeshi Watanabe

Keyword(s):

Cell Death ◽

Cell Adhesion ◽

Bone Marrow Cells ◽

Apoptotic Cell ◽

Small Gtpases ◽

Apoptotic Cell Death ◽

Cell Adhesion And Migration ◽

Rho Family ◽

And Migration ◽

Related Proteins

ABSTRACT We have isolated a cDNA, frl(formin-related gene in leukocytes), a novel mammalian member of the formin gene family. The frlcDNA encodes a 160-kDa protein, FRL, that possesses FH1, FH2, and FH3 domains that are well conserved among other Formin-related proteins. An FRL protein is mainly localized in the cytosol and is highly expressed in spleen, lymph node, and bone marrow cells. Formin-related genes and proteins have been reported to play crucial roles in morphogenesis, cell polarity, and cytokinesis through interaction with Rho family small GTPases. FRL binds to Rac at its N-terminal region including the FH3 domain and associates with profilin at the FH1 domain. In a macrophage cell line, P388D1, overexpression of a truncated form of FRL containing only the FH3 domain (FH3-FRL) strongly inhibited cell adhesion to fibronectin and migration upon stimulation with a chemokine. Moreover, expression of the truncated FH3-FRL protein resulted in apoptotic cell death of P388D1 cells, suggesting that the truncated FH3-FRL protein may interfere with signals of FRL. Overexpression in the P388D1 cells of full-length FRL or of the truncated protein containing the FH3 and FH1 domains, with simultaneous expression of the truncated FH3-FRL protein, blocked apoptotic cell death and inhibition of cell adhesion and migration. These results suggest that FRL may play a role in the control of reorganization of the actin cytoskeleton in association with Rac and also in the regulation of the signal for cell survival.

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