Desmosomal glycoprotein DGI, a component of intercellular desmosome junctions, is related to the cadherin family of cell adhesion molecules.
Grant N. Wheeler,A. E. Parker,C L Thomas,P Ataliotis,D. Poynter,Joachim Arnemann,A. J. Rutman,S C Pidsley,Fiona M. Watt,David A. Rees +9 more
TL;DR: It is shown for desmosomes that a major glycop protein component (desmosomal glycoprotein DGI) has extensive homology with the cadherins, defining an extended family, but also has unique features in its cytoplasmic domain that are likely to be relevant to the association with intermediate rather than actin filaments.
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Abstract: Among the variety of specialized intercellular junctions, those of the adherens type have the most obvious association with cytoskeletal elements. This may be with the actin microfilament system as in the zonula adherens or with intermediate filaments as in the macula adherens, or desmosome. In the former case, it is clear that transmembrane glycoproteins of the cadherin family are important adhesive components of the molecular assembly. We now show for desmosomes that a major glycoprotein component (desmosomal glycoprotein DGI) has extensive homology with the cadherins, defining an extended family, but also has unique features in its cytoplasmic domain that are likely to be relevant to the association with intermediate rather than actin filaments. A novel 282-residue extension contains repeats of approximately 29 amino acid residues predicted to have an antiparallel beta-sheet structure, followed by a glycine-rich sequence. As in the cadherins, the extracellular domain contains possible Ca2(+)-binding sequences and a potential protease processing site. The cell adhesion recognition region (His-Ala-Val) of the cadherins is modified to Arg-Ala-Leu.
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Citations
Autoantibodies against a novel epithelial cadherin in pemphigus vulgaris, a disease of cell adhesion
TL;DR: It is demonstrated that a novel epithelial cadherin is the target of autoantibodies in PV, and the deduced amino acid sequence of PVA was unique but showed significant homology with members of the cadher in family of Ca(2+)-dependent cell adhesion molecules.
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Mechanisms of foam cell formation in atherosclerosis
Dimitry A. Chistiakov,Alexandra A. Melnichenko,Veronika A. Myasoedova,Andrey V. Grechko,Alexander N. Orekhov +4 more
TL;DR: In atherosclerosis, pro-inflammatory stimuli upregulates expression of scavenger receptors, especially LOX-1, and downregulate expression of cholesterol transporters, which results in deposition of free and esterified cholesterol in macrophages and generation of foam cells.
571
Targeted Disruption of the Pemphigus Vulgaris Antigen (Desmoglein 3) Gene in Mice Causes Loss of Keratinocyte Cell Adhesion with a Phenotype Similar to Pemphigus Vulgaris
Peter Koch,My G. Mahoney,Hiroyasu Ishikawa,Leena Pulkkinen,Jouni Uitto,Leonard Shultz,George F. Murphy,Diana Whitaker-Menezes,John R. Stanley +8 more
TL;DR: It is suggested that pemphigus autoantibodies might interfere directly with such a function of DSG3, and the critical importance of Dsg3 for adhesion in deep stratified squamous epithelia is demonstrated.
The uvomorulin-anchorage protein alpha catenin is a vinculin homologue.
Kurt Herrenknecht,Masayuki Ozawa,Christoph Eckerskorn,Friedrich Lottspeich,Martin Lenter,Rolf Kemler +5 more
TL;DR: The results suggest the possibility of a new vinculin-related protein family involved in the cytoplasmic anchorage of cell-cell and cell-substrate adhesion molecules.
371
Autoantibodies against the amino-terminal cadherin-like binding domain of pemphigus vulgaris antigen are pathogenic.
TL;DR: Results indicate that at least one pathogenic epitope, which is sufficient to cause suprabasilar acantholysis in neonatal mice, is located on the amino-terminal region of PVA, an area thought to be important in cadherin homophilic adhesion.
References
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Talila Volk,Benjamin Geiger +1 more
TL;DR: The results obtained strongly suggest that A-CAM is a Ca2+-dependent adherens junction- specific membrane glycoprotein that is involved in intercellular adhesion in these sites.
Desmoplakin I and desmoplakin II. Purification and characterization.
TL;DR: Cross-linking by disuccinimidyl suberate of 125I-labeled DP1 or DP2 at nanomolar concentrations confirmed that DP1 is a dimer by doubling of its apparent Mr on sodium dodecyl sulfate gels and indicated that DP2, which failed to become cross-linked, is a monomer.