scholarly journals Cationic charge and polyspecificity of an integrin domain regulates infectivity of malaria parasites

2018 ◽  
Author(s):  
Dennis Klug ◽  
Sarah Goellner ◽  
Julia Sattler ◽  
Leanne Strauss ◽  
Jessica Kehrer ◽  
...  
Keyword(s):  
Positive Charge ◽  
Structural Features ◽  
Eukaryotic Evolution ◽  
Apicomplexan Parasites ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
Cell Substrate Adhesion

AbstractCell-cell and cell-substrate adhesion is critical for many functions in life. In eukaryotes, I-domains mediate functions as divergent as tissue traversal by malaria-causing Plasmodium parasites as well as cell adhesion and migration by human leucocytes. The I-domain containing protein TRAP is important for Plasmodium sporozoite motility and invasion. Here we show that the I-domain of TRAP is required to mediate adhesional properties which can be partially preserved when the native I-domain is replaced by I-domains from human integrins or from an apicomplexan parasite that does not infect insects. By putting in vivo data and structural features in perspective we conclude that polyspecificity and positive charge around the ligand binding site of the I-domain are important for TRAP function. Our data suggest a highly preserved functionality of I-domains across eukaryotic evolution that is used by apicomplexan parasites to invade a broad range of tissues in a variety of hosts.

MAb 14C5 against a human cell substrate adhesion molecule for inhibition of tumor growth in-vivo

1997 ◽  
Vol 33 ◽  
pp. S42
Author(s):  
P. Giffels ◽  
S. Köhler ◽  
Ch. DePotter ◽  
E. Coene ◽  
D. Nagel ◽  
...  
Keyword(s):  
Tumor Growth ◽  
Adhesion Molecule ◽  
Human Cell ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Inhibition Of Tumor Growth ◽  
Cell Substrate Adhesion

scholarly journals Novel micropatterning technique reveals dependence of cell-substrate adhesion and migration of social amoebas on parental strain, development, and fluorescent markers

PLoS ONE ◽  
2020 ◽  
Vol 15 (7) ◽  
pp. e0236171
Author(s):  
Richa Karmakar ◽  
Christoph Schich ◽  
Nadine Kamprad ◽  
Vanessa Scheller ◽  
Edgar Gutierrez ◽  
...  
Keyword(s):  
Parental Strain ◽  
Strain Development ◽  
Fluorescent Markers ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
And Migration ◽  
Cell Substrate Adhesion

scholarly journals Enhancement of vinculin synthesis by migrating stratified squamous epithelium.

1989 ◽  
Vol 109 (2) ◽  
pp. 571-576 ◽  
Author(s):  
J D Zieske ◽  
G Bukusoglu ◽  
I K Gipson
Keyword(s):  
Total Protein ◽  
Leading Edge ◽  
Western Blots ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Stratified Squamous Epithelium ◽  
Cell Substrate Adhesion ◽  
And Control ◽  
Cryostat Sections

A 110-115-kD protein is present at levels 27-fold higher in migratory epithelium in the rat cornea than in stationary epithelium. This protein represents 2.7% of the total protein in migratory epithelium 6-h postabrasion wound and 0.1% of the total protein in stationary epithelium. Our findings demonstrate that this 110-115-kD protein is vinculin. In Western blots comparing proteins from migratory and control epithelium, antibody against vinculin cross-reacted with the 110-115-kD protein. Using immunoslot blots, vinculin was determined to be present at maximal levels 6 h postabrasion wound, at levels 22- and 8-fold higher than control at 18 and 48 h, respectively, returning to control levels 72 h postwounding. Vinculin was also localized by indirect immunohistochemistry in migrating corneal epithelium. 3-mm scrape wounds were allowed to heal in vivo for 20 h. In flat mounts of these whole wounded corneas, vinculin was localized as punctate spots in the leading edge of migrating epithelium. In cryostat sections, vinculin was localized as punctate spots along the basal cell membranes of the migrating sheet adjacent to the basement membrane and in patches between cells as well as diffusely throughout the cell. Only very diffuse localization with occasional punctate spots between adjacent superficial cells was present in stationary epithelium. The increased synthesis of vinculin during migration and the localization of vinculin at the leading edge of migratory epithelium suggest that vinculin may be involved in cell-cell and cell-substrate adhesion as the sheet of epithelium migrates to cover a wound.

scholarly journals TMEM87a/Elkin1, a component of a novel mechanoelectrical transduction pathway, modulates melanoma adhesion and migration

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Amrutha Patkunarajah ◽  
Jeffrey H Stear ◽  
Mirko Moroni ◽  
Lioba Schroeter ◽  
Jedrzej Blaszkiewicz ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Melanoma Cells ◽  
Transduction Pathway ◽  
Adhesion Properties ◽  
Mechanoelectrical Transduction ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
And Migration ◽  
Cell Substrate Adhesion ◽  
Cell Cell

Mechanoelectrical transduction is a cellular signalling pathway where physical stimuli are converted into electro-chemical signals by mechanically activated ion channels. We describe here the presence of mechanically activated currents in melanoma cells that are dependent on TMEM87a, which we have renamed Elkin1. Heterologous expression of this protein in PIEZO1-deficient cells, that exhibit no baseline mechanosensitivity, is sufficient to reconstitute mechanically activated currents. Melanoma cells lacking functional Elkin1 exhibit defective mechanoelectrical transduction, decreased motility and increased dissociation from organotypic spheroids. By analysing cell adhesion properties, we demonstrate that Elkin1 deletion is associated with increased cell-substrate adhesion and decreased homotypic cell-cell adhesion strength. We therefore conclude that Elkin1 supports a PIEZO1-independent mechanoelectrical transduction pathway and modulates cellular adhesions and regulates melanoma cell migration and cell-cell interactions.

scholarly journals A New Member of the Rho Family, Rnd1, Promotes Disassembly of Actin Filament Structures and Loss of Cell Adhesion

1998 ◽  
Vol 141 (1) ◽  
pp. 187-197 ◽  
Author(s):  
Catherine D. Nobes ◽  
Inger Lauritzen ◽  
Marie-Geneviève Mattei ◽  
Sonia Paris ◽  
Alan Hall ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Rho Gtpase ◽  
Focal Adhesions ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Rho Family ◽  
Cell Substrate Adhesion ◽  
Distinct Branch

Members of the Rho GTPase family regulate the organization of the actin cytoskeleton in response to extracellular growth factors. We have identified three proteins that form a distinct branch of the Rho family: Rnd1, expressed mostly in brain and liver; Rnd2, highly expressed in testis; and Rnd3/RhoE, showing a ubiquitous low expression. At the subcellular level, Rnd1 is concentrated at adherens junctions both in confluent fibroblasts and in epithelial cells. Rnd1 has a low affinity for GDP and spontaneously exchanges nucleotide rapidly in a physiological buffer. Furthermore, Rnd1 lacks intrinsic GTPase activity suggesting that in vivo, it might be constitutively in a GTP-bound form. Expression of Rnd1 or Rnd3/RhoE in fibroblasts inhibits the formation of actin stress fibers, membrane ruffles, and integrin-based focal adhesions and induces loss of cell–substrate adhesion leading to cell rounding (hence Rnd for “round”). We suggest that these proteins control rearrangements of the actin cytoskeleton and changes in cell adhesion.

scholarly journals Shear force-based genetic screen reveals negative regulators of cell adhesion and protrusive activity

2017 ◽  
Vol 114 (37) ◽  
pp. E7727-E7736 ◽  
Author(s):  
Thomas J. Lampert ◽  
Nadine Kamprad ◽  
Marc Edwards ◽  
Jane Borleis ◽  
Ayende J. Watson ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Model Organism ◽  
Network Activity ◽  
Filamentous Actin ◽  
Migratory Activity ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Human Genes ◽  
And Migration ◽  
Cell Substrate Adhesion

The model organism Dictyostelium discoideum has greatly facilitated our understanding of the signal transduction and cytoskeletal pathways that govern cell motility. Cell–substrate adhesion is downstream of many migratory and chemotaxis signaling events. Dictyostelium cells lacking the tumor suppressor PTEN show strongly impaired migratory activity and adhere strongly to their substrates. We reasoned that other regulators of migration could be obtained through a screen for overly adhesive mutants. A screen of restriction enzyme-mediated integration mutagenized cells yielded numerous mutants with the desired phenotypes, and the insertion sites in 18 of the strains were mapped. These regulators of adhesion and motility mutants have increased adhesion and decreased motility. Characterization of seven strains demonstrated decreased directed migration, flatness, increased filamentous actin-based protrusions, and increased signal transduction network activity. Many of the genes share homology to human genes and demonstrate the diverse array of cellular networks that function in adhesion and migration.

scholarly journals Regulation of cell-substrate adhesion by proteoglycans immobilized on extracellular substrates

1989 ◽  
Vol 264 (14) ◽  
pp. 8012-8018 ◽  
Author(s):  
M Yamagata ◽  
S Suzuki ◽  
S K Akiyama ◽  
K M Yamada ◽  
K Kimata
Keyword(s):  
Substrate Adhesion ◽  
Cell Substrate ◽  
Cell Substrate Adhesion

scholarly journals A GTPase controls cell-substrate adhesion in Xenopus XTC fibroblasts.

1992 ◽  
Vol 118 (5) ◽  
pp. 1235-1244 ◽  
Author(s):  
M H Symons ◽  
T J Mitchison
Keyword(s):  
Control Cell ◽  
Response To Treatment ◽  
Nucleotide Analogs ◽  
Cell Contractility ◽  
Cell Rounding ◽  
Substrate Adhesion ◽  
Cell Substrate ◽  
Adhesive Interactions ◽  
Cell Substrate Adhesion ◽  
Gamma S

Cell-substrate adhesion is crucial at various stages of development and for the maintenance of normal tissues. Little is known about the regulation of these adhesive interactions. To investigate the role of GTPases in the control of cell morphology and cell-substrate adhesion we have injected guanine nucleotide analogs into Xenopus XTC fibroblasts. Injection of GTP gamma S inhibited ruffling and increased spreading, suggesting an increase in adhesion. To further investigate this, we made use of GRGDSP, a peptide which inhibits binding of integrins to vitronectin and fibronectin. XTC fibroblasts injected with non-hydrolyzable analogs of GTP took much more time to round up than mock-injected cells in response to treatment with GRGDSP, while GDP beta S-injected cells rounded up in less time than controls. Injection with GTP gamma S did not inhibit cell rounding induced by trypsin however, showing that cell contractility is not significantly affected by the activation of GTPases. These data provide evidence for the existence of a GTPase which can control cell-substrate adhesion from the cytoplasm. Treatment of XTC fibroblasts with the phorbol ester 12-o-tetradecanoylphorbol-13-acetate reduced cell spreading and accelerated cell rounding in response to GRGDSP, which is essentially opposite to the effect exerted by non-hydrolyzable GTP analogs. These results suggest the existence of at least two distinct pathways controlling cell-substrate adhesion in XTC fibroblasts, one depending on a GTPase and another one involving protein kinase C.

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