scholarly journals Localization of the Laminin α4 Chain in the Skin and Identification of a Heparin-Dependent Cell Adhesion Site Within the Laminin α4 Chain C-Terminal LG4 Module

2004 ◽  
Vol 122 (3) ◽  
pp. 614-620 ◽  
Author(s):  
Hiroshi Matsuura ◽  
Yutaka Momota ◽  
Kaoru Murata ◽  
Hironori Matsushima ◽  
Hiroshi Shinkai ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Dependent Cell ◽  
Adhesion Site

scholarly journals Affinity and Kinetic Analysis of L-selectin (CD62L) Binding to Glycosylation-dependent Cell-adhesion Molecule-1

1998 ◽  
Vol 273 (2) ◽  
pp. 763-770 ◽  
Author(s):  
Martin W. Nicholson ◽  
A. Neil Barclay ◽  
Mark S. Singer ◽  
Steven D. Rosen ◽  
P. Anton van der Merwe
Keyword(s):  
Cell Adhesion ◽  
Kinetic Analysis ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Dependent Cell ◽  
Cell Adhesion Molecule 1

scholarly journals α4β1Integrin-dependent Cell Adhesion Is Regulated by a Low Affinity Receptor Pool That Is Conformationally Responsive to Ligand

1995 ◽  
Vol 270 (48) ◽  
pp. 28740-28750 ◽  
Author(s):  
Ted A. Yednock ◽  
Catherine Cannon ◽  
Christopher Vandevert ◽  
Erich G. Goldbach ◽  
Gray Shaw ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Dependent Cell ◽  
Affinity Receptor ◽  
Receptor Pool

Integrin-like RGD-dependent cell adhesion mechanism is involved in the rapid killing of Onchocerca microfilariae during early infection of Simulium damnosum s.l.

Parasitology ◽  
2001 ◽  
Vol 122 (4) ◽  
pp. 433-438 ◽  
Author(s):  
H. E. HAGEN ◽  
S. L. KLÄGER
Keyword(s):  
Cell Adhesion ◽  
Intermediate Host ◽  
Blocking Agent ◽  
Early Infection ◽  
Adhesion Mechanism ◽  
Simulium Damnosum ◽  
Dependent Cell ◽  
Species Specific

Injection trials with compatible and non-compatible Onchocerca species into S. damnosum s.l., the vector of human and bovine onchocerciasis, demonstrated that the rapid killing of microfilariae within the blackfly's haemocoel is species specific. In the presence of the peptide RGDS as a blocking agent for integrin-like receptors of haemocytes, the survival of O. ochengi microfilariae in its natural intermediate host was significantly increased. This increased survival 24 h p.i. correlated with a significant decrease of apoptosis levels in the microfilariae following a 2 h exposure to the haemolymph in vivo. These findings suggest that haemocytes are directly involved in the killing of Onchocerca microfilariae in the blackfly.

scholarly journals Reevaluating αE-catenin monomer and homodimer functions by characterizing E-cadherin/αE-catenin chimeras

2015 ◽  
Vol 210 (7) ◽  
pp. 1065-1074 ◽  
Author(s):  
Julie M. Bianchini ◽  
Khameeka N. Kitt ◽  
Martijn Gloerich ◽  
Sabine Pokutta ◽  
William I. Weis ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Intercellular Adhesion ◽  
Dependent Cell ◽  
In Cells ◽  
E Cadherin ◽  
Cell Cell

As part of the E-cadherin–β-catenin–αE-catenin complex (CCC), mammalian αE-catenin binds F-actin weakly in the absence of force, whereas cytosolic αE-catenin forms a homodimer that interacts more strongly with F-actin. It has been concluded that cytosolic αE-catenin homodimer is not important for intercellular adhesion because E-cadherin/αE-catenin chimeras thought to mimic the CCC are sufficient to induce cell–cell adhesion. We show that, unlike αE-catenin in the CCC, these chimeras homodimerize, bind F-actin strongly, and inhibit the Arp2/3 complex, all of which are properties of the αE-catenin homodimer. To more accurately mimic the junctional CCC, we designed a constitutively monomeric chimera, and show that E-cadherin–dependent cell adhesion is weaker in cells expressing this chimera compared with cells in which αE-catenin homodimers are present. Our results demonstrate that E-cadherin/αE-catenin chimeras used previously do not mimic αE-catenin in the native CCC, and imply that both CCC-bound monomer and cytosolic homodimer αE-catenin are required for strong cell–cell adhesion.

scholarly journals Desmosomal glycoproteins 2 and 3 (desmocollins) show N-terminal similarity to calcium-dependent cell-cell adhesion molecules

1990 ◽  
Vol 97 (2) ◽  
pp. 239-246
Author(s):  
J.L. Holton ◽  
T.P. Kenny ◽  
P.K. Legan ◽  
J.E. Collins ◽  
J.N. Keen ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Intercellular Space ◽  
Solid Phase ◽  
Rabbit Antiserum ◽  
High Titre ◽  
Polyclonal Antiserum ◽  
Keyhole Limpet Haemocyanin ◽  
Calcium Dependent ◽  
Dependent Cell

The N-terminal sequence of a mixture of desmosomal glycoproteins 2 and 3 (dg2/3, desmocollins) from bovine nasal epidermis, prepared by electro-elution from polyacrylamide gels, was determined by solid-phase Edman degradation. A sequence of 23 amino acids was obtained. This showed 43% identity with that of the N terminus of the calcium-dependent cell adhesion molecule, N-cadherin. A lesser degree of identity with other members of the cadherin-uvomorulin-L-CAM family was also found. In order to confirm that the sequence was derived from the dg2/3 molecules a rabbit antiserum was raised against a synthetic peptide corresponding to the sequence, conjugated to keyhole limpet haemocyanin (KLH). The antiserum obtained showed high (titre) activity against both the peptide and KLH in ELISA. Each activity could be specifically adsorbed with the appropriate ligand. The antiserum reacted specifically with both dg2 and dg3 of bovine nasal epidermis on immunoblots, this binding was blocked by the N-terminal peptide but was unaffected by KLH. The identity of dg2 and -3 in these preparations was confirmed by immunoblotting with two monoclonal antibodies and one polyclonal antiserum raised against the whole molecules. The N-terminal peptide antiserum was shown to bind to the intercellular space of desmosome profiles by immunoelectron microscopy on ultra-thin frozen sections. One of the two monoclonal antibodies (07–4D) also reacted with the desmosomal intercellular space. dg2 and -3 were shown by Staphylococcus aureus V8 protease digestion to have identical one-dimensional peptide maps. Both the N-terminal antiserum and 07–4D reacted with a V8 fragment of 19,000 Mr derived from dg2 and dg3.(ABSTRACT TRUNCATED AT 250 WORDS)

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