scholarly journals Inversa Dystrophic Epidermolysis Bullosa Is Caused by Missense Mutations at Specific Positions of the Collagenic Domain of Collagen Type VII

2010 ◽  
Vol 130 (10) ◽  
pp. 2508-2511 ◽  
Author(s):  
Christine Chiaverini ◽  
Alexandra V. Charlesworth ◽  
Monia Youssef ◽  
Jean-François Cuny ◽  
Smail H. Rabia ◽  
...  
Keyword(s):  
Epidermolysis Bullosa ◽  
Collagen Type ◽  
Missense Mutations ◽  
Dystrophic Epidermolysis Bullosa ◽  
Collagen Type Vii

Collagen type VII

1998 ◽  
pp. 77-80
Author(s):  
Shirley Ayad ◽  
Ray Boot-Handford ◽  
Martin J. Humphries ◽  
Karl E. Kadler ◽  
Adrian Shuttleworth
Keyword(s):  
Collagen Type ◽  
Collagen Type Vii

Basement Membrane in Middle Ear Cholesteatoma Immunohistochemical and Ultrastructural Observations

1996 ◽  
Vol 105 (10) ◽  
pp. 804-810 ◽  
Author(s):  
Jesus Bujía ◽  
Anja Holly ◽  
Holger Sudhoff ◽  
Gerd Borkowski ◽  
Henning Hildmann ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Middle Ear ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Middle Ear Mucosa ◽  
Type Iv ◽  
Middle Ear Cholesteatoma ◽  
Human Middle Ear ◽  
Cell Matrix Interactions ◽  
Collagen Type Vii

We investigated the distribution of basement membrane zone (BMZ) components collagen type IV, collagen type VII, and fibronectin in human middle ear cholesteatoma, auditory meatal skin, and middle ear mucosa using both immunohistochemical and ultrastructural methods. Collagen type IV inununoreactivity of skin and middle ear mucosa is continuous in the BMZ, whereas cholesteatoma frequently showed absent immunoreactivity or focal discontinuities. Collagen type VII inununoreactivity is detected similarly within the BMZ of cholesteatoma and skin. Fibronectin immunoreactivity is observed within the dermoepithelial junction of skin and middle ear mucosa. In cholesteatoma, however, fibronectin immunoreactivity is markedly increased within the extrinsic BMZ and the subepithelial connective tissue. The ultrastructural arrangement of the BMZ of cholesteatoma is like that of skin; however, it exhibits distinct alterations of the lamina fibroreticularis and lamina densa. Our results outline cholesteatoma as a disease with disturbed cell matrix interactions analogous to those of wound reepithelialization.

scholarly journals Surface relocation of alpha 6 beta 4 integrins and assembly of hemidesmosomes in an in vitro model of wound healing.

1991 ◽  
Vol 115 (6) ◽  
pp. 1737-1750 ◽  
Author(s):  
M A Kurpakus ◽  
V Quaranta ◽  
J C Jones
Keyword(s):  
Wound Healing ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Connective Tissue ◽  
Collagen Type ◽  
Polyclonal Antibodies ◽  
Vitro Model ◽  
Tissue Attachment ◽  
Collagen Type Vii

A transmembrane extracellular matrix receptor of the integrin family, alpha 6 beta 4, is a component of the hemidesmosome, an adhesion complex of importance in epithelial cell-connective tissue attachment (Stepp, M. A., S. Spurr-Michaud, A. Tisdale, J. Elwell, and I. K. Gipson. 1990. Proc. Natl. Acad. Sci. USA. 87:8970-8974; Jones, J. C. R., M. A. Kurpakus, H. M. Cooper, and V. Quaranta. 1991. Cell Regulation. 2:427-438). Cytosolic components of hemidesmosomes include bullous pemphigoid (BP) antigens while extracellular components include a 125-kD component of anchoring filaments (CAF) and collagen type VII-containing anchoring fibrils. We have monitored the incorporation of the alpha 6 beta 4 integrins into forming hemidesmosomes in an in vitro wound-healing explant model. In epithelial cells recently migrated from the edges of unwounded sites over bare connective tissue, alpha 6 beta 4 first appears along the entire cell surface. At this stage, these cells contain little or no cytosolic hemidesmosomal components, at least as detectable by immunofluorescence using BP autoantibodies, whereas they are already positive for laminin and CAF. At a later stage, as cells become positive for cytosolic hemidesmosome components such as BP antigens as well as collagen type VII, alpha 6 beta 4 becomes concentrated along the basal pole of the epithelial cell where it abuts the connective tissue of the explant. Polyclonal antibodies to beta 4 do not interfere with the migration of epithelial cells in the explant. However, they prevent assembly of hemidesmosomal complexes and inhibit expression of collagen type VII in cells that have migrated over wound areas. In addition, they induce disruption of established hemidesmosomes in nonmigrating cells of the unwounded area of the explant. Monoclonal antibodies to alpha 6 have a more dramatic effect, since they completely detach epithelial cells in the unwounded area of the explant. Antibodies to CAF also detach epithelial cells in unwounded areas, apparently by inducing separation between epithelium and connective tissue at the lamina lucida of the basement membrane zone. These results suggest a model whereby polarization of alpha 6 beta 4 to the basal surface of the cells, perhaps induced by a putative anchoring filament-associated ligand, triggers assembly of hemidesmosome plaques.

scholarly journals Genetic Linkage Between the Collagen Type VII Gene COL7A1 and Pretibial Epidermolysis Bullosa with Lichenoid Features

1995 ◽  
Vol 104 (5) ◽  
pp. 803-805 ◽  
Author(s):  
Jean Marie Naeyaert ◽  
Lieve Nuytinck ◽  
Sylvia De Bie ◽  
Hilde Beele ◽  
André Kint ◽  
...  
Keyword(s):  
Epidermolysis Bullosa ◽  
Genetic Linkage ◽  
Collagen Type ◽  
Collagen Type Vii

Analysis of wound healing in an in vitro model: early appearance of laminin and a 125 × 10(3) Mr polypeptide during adhesion complex formation

1990 ◽  
Vol 96 (4) ◽  
pp. 651-660
Author(s):  
M.A. Kurpakus ◽  
E.L. Stock ◽  
J.C. Jones
Keyword(s):  
Wound Healing ◽  
Basement Membrane ◽  
In Vitro Model ◽  
Collagen Type ◽  
Basement Membrane Zone ◽  
Lamina Densa ◽  
Vitro Model ◽  
Collagen Type Vii ◽  
Adhesion Complex

The adhesion complex, which plays an important role in cell-substratum attachment, consists of a cellular hemidesmosomal plaque, anchoring filaments, the basement membrane zone and anchoring fibrils. An analysis of the temporal sequence of assembly of the adhesion complex was undertaken in an in vitro model of epithelial cell wound healing by immunofluorescence and electron microscopy. A monoclonal antibody directed against a 125K (K = 10(3) Mr) polypeptide (mAbHD), bullous pemphigoid (BP) autoantibodies, antibodies directed against collagen type VII and laminin antibodies were used as markers for anchoring filaments, the hemidesmosome, anchoring fibrils and the laminin component of the basement membrane zone, respectively. Fluorescence labeling could be detected with mAbHD before labeling with BP autoantibodies or collagen type VII antibodies. Laminin fluorescence was detected at the same time as mAbHD. Furthermore, the 125K polypeptide and laminin were located extracellularly prior to the appearance of BP antigen and collagen type VII. The appearance of the hemidesmosomal plaque at the electron microscope level succeeded the localization of BP antigen in basal cells detected by immunofluorescence microscopy. No evidence for the coordinated appearance of BP antigen, collagen type VII and laminin was observed in this model. We discuss the possibility that the 125K protein and laminin may play roles in the initiation of complex formation. Furthermore, although basement membrane zone components were detected early in adhesion complex re-formation, formation of the lamina densa region of the basement membrane zone followed the appearance of the hemidesmosomal plaque, indicating a role for the hemidesmosomal plaque in organizing the structure of the lamina densa.

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