Short form of α9 promotes α9β1 integrin-dependent cell adhesion by modulating the function of the full-length α9 subunit

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.

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Identification of mammalian and invertebrate analogues of the avian calcium-dependent cell adhesion protein N-cadherin with syntheticpeptide directed antibodies against a conserved cytoplasmic domain

Biochemical and Biophysical Research Communications ◽

10.1016/s0006-291x(05)80211-6 ◽

1990 ◽

Vol 172 (1) ◽

pp. 313-320 ◽

Cited By ~ 13

Author(s):

Laura A. Lagunowich ◽

Larry A. Donoso ◽

Gerald B. Grunwald

Keyword(s):

Cell Adhesion ◽

Cytoplasmic Domain ◽

Adhesion Protein ◽

Calcium Dependent ◽

Cell Adhesion Protein ◽

Dependent Cell

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Kinetic analysis of integrin-dependent cell adhesion on vitronectin. The inhibitory potential of plasminogen activator inhibitor-1 and RGD peptides

European Journal of Biochemistry ◽

10.1046/j.1432-1327.1998.2530669.x ◽

1998 ◽

Vol 253 (3) ◽

pp. 669-674 ◽

Cited By ~ 31

Author(s):

Matthias Germer ◽

Sandip M. Kanse ◽

Tove Kirkegaard ◽

Lars Kjoller ◽

Brunhilde Felding-Habermann ◽

...

Keyword(s):

Cell Adhesion ◽

Kinetic Analysis ◽

Plasminogen Activator ◽

Plasminogen Activator Inhibitor ◽

Plasminogen Activator Inhibitor 1 ◽

Rgd Peptides ◽

Dependent Cell ◽

Inhibitory Potential ◽

Activator Inhibitor

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Reliability of Proposed Short Form of Illinois Test of Psycholinguistic Abilities

Council review ◽

10.1177/001440297804500306 ◽

1978 ◽

Vol 45 (3) ◽

pp. 198-204 ◽

Cited By ~ 2

Author(s):

Ronald P. Maggiore

Keyword(s):

Internal Consistency ◽

Short Form ◽

Full Length ◽

Psychometric Instrument ◽

Tests Of Significance ◽

The Future ◽

Administration Time

The reliability of the proposed short form of the Revised Illinois Test of Psycholinguistic Abilities (Newcomer & Hammill, 1974) was computed on data derived from 6 year old ITPA standardization test booklets. Measures of internal consistency and between forms reliability were obtained for both full length and short form scorings of single ITPA test administrations. Tests of significance yielded significantly lower measures on 10 of 12 subtests for the short form test when compared to the internal consistency of the full length test. The correlation between the two forms was significantly reduced in all cases when the part-whole correspondence was accounted for. The results were discussed in terms of their impact on the future use of the proposed short form as a psychometric instrument of questionable reliability. Suggestions were proposed for those concerned with reducing administration time.

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

The Journal of Cell Biology ◽

10.1083/jcb.201411080 ◽

2015 ◽

Vol 210 (7) ◽

pp. 1065-1074 ◽

Cited By ~ 18

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.

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

Journal of Cell Science ◽

10.1242/jcs.97.2.239 ◽

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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