Cross-linking of the dermo-epidermal junction of skin regenerating from keratinocyte autografts. Anchoring fibrils are a target for tissue transglutaminase.
@article{Raghunath1996CrosslinkingOT,
title={Cross-linking of the dermo-epidermal junction of skin regenerating from keratinocyte autografts. Anchoring fibrils are a target for tissue transglutaminase.},
author={Michael Raghunath and Bianca H{\"o}pfner and Daniel Aeschlimann and Ursula Lüthi and Martin Meuli and Stefan Altermatt and Rita Gobet and Leena Bruckner-Tuderman and Beat Steinmann},
journal={The Journal of clinical investigation},
year={1996},
volume={98 5},
pages={
1174-84
}
}Since transglutaminases create covalent gamma-glutamyl-epsilon-lysine cross-links between extracellular matrix proteins they are prime candidates for stabilizing tissue during wound healing. Therefore, we studied the temporo-spatial expression of transglutaminase activity in skin regenerating from cultured epithelial autografts in severely burned children by the specific incorporation of monodansylcadaverine into cryostat sections from skin biopsies obtained between 5 d to 17 mo after grafting…
109 Citations
Supramolecular Interactions in the Dermo-epidermal Junction Zone
- Chemistry, BiologyJournal of Biological Chemistry
- 2008
In vitro binding studies demonstrated that a von Willebrand factor A-like motif in collagen VII was essential for binding of anchoring fibrils to reconstituted collagen I fibril, which is stabilized in situ and resists dissociation by strong denaturants.
Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source.
- BiologyThe Journal of investigative dermatology
- 2003
Data suggest that changes in cross-linking both in the intracellular and extracellular compartments elicited by tissue transglutaminase following exposure to ultraviolet provides a rapid tissue stabilization process following damage, but as such may be a contributory factor to the scarring process that results.
Making more matrix: enhancing the deposition of dermal-epidermal junction components in vitro and accelerating organotypic skin culture development, using macromolecular crowding.
- BiologyTissue engineering. Part A
- 2015
The findings corroborate the role of fibroblasts as important players in producing collagen VII and inducing collagen VII deposition in the DEJ, and that macromolecular crowding leads to organotypic epidermal differentiation in tissue culture in a significantly condensed time frame.
Transglutaminase activity in the eye: cross-linking in epithelia and connective tissue structures.
- Biology, MedicineInvestigative ophthalmology & visual science
- 1999
TGase 2 appears to be an important cross-linker and thus stabilizer of ocular connective tissue, in particular the ciliary zonules, which is of relevance in hereditary microfibrillopathies such as Marfan syndrome.
Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis
- Biology, MedicineFASEB journal : official publication of the Federation of American Societies for Experimental Biology
- 1999
It is established that TG is an important tissue stabilizing enzyme that is active during wound healing and can function to promote angiogenesis.
Immunohistochemical study of type I collagen turn-over and of matrix metalloproteinases in chromoblastomycosis before and after treatment by terbinafine.
- BiologyPathology, research and practice
- 1998
Transglutaminases, involucrin, and loricrin as markers of epidermal differentiation in skin substitutes derived from human sweat gland cells
- Biology, MedicinePediatric Surgery International
- 2009
Findings support the thesis that SG cells have the potential to form a near normal stratified epidermal analog that might be used as a skin substitute.
Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development.
- BiologyAmerican journal of respiratory cell and molecular biology
- 1997
It is concluded that tTG is expressed and externalized into the extracellular matrix of lung shortly before maturation of an organ area, and it is hypothesize that it may prevent or delay further remodeling of basement membranes and may stabilize otherextracellular components, such as microfibrils.
Collagen VII Half-Life at the Dermal-Epidermal Junction Zone: Implications for Mechanisms and Therapy of Genodermatoses.
- BiologyThe Journal of investigative dermatology
- 2016
Facilitated wound healing by activation of the Transglutaminase 1 gene.
- BiologyThe American journal of pathology
- 2000
References
SHOWING 1-10 OF 45 REFERENCES
Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: identification of osteonectin as a major glutaminyl substrate
- Biology, EngineeringThe Journal of cell biology
- 1995
The demonstration of extracellular transglutaminase activity in differentiating cartilage, i.e., cross-linking of osteonectin in situ, shows that tissue transglUTaminase-catalyzed cross- linking is a physiological mechanism for cartilage matrix stabilization.
Skin regenerated from cultured epithelial autografts on full-thickness burn wounds from 6 days to 5 years after grafting. A light, electron microscopic and immunohistochemical study.
- MedicineLaboratory investigation; a journal of technical methods and pathology
- 1989
Regeneration of skin from cultured keratinocyte autografts used in the treatment of full-thickness burn wounds was studied in 21 pediatric patients from 6 days to 5 years after grafting, and normal histologic features were maintained for years after transplanting.
Type VII collagen, anchoring fibrils, and epidermolysis bullosa.
- Chemistry, BiologyThe Journal of investigative dermatology
- 1993
Understanding the function of type VII collagen at the molecular level will be the key to devising strategies to moderate the pathophysiology of dystrophic epidermolysis bullosa.
Immunohistochemical and mutation analyses demonstrate that procollagen VII is processed to collagen VII through removal of the NC-2 domain
- BiologyThe Journal of cell biology
- 1995
The results indicate that in normal human skin, the removal of the NC-2 domain from procollagen VII precedes its deposition at the dermal-epidermal junction, and suggest that an aberration in the procollsagen VII cleavage interferes with the normal fibrillogenesis of the anchoring fibrils.
Cross-linking of laminin-nidogen complexes by tissue transglutaminase. A novel mechanism for basement membrane stabilization.
- BiologyThe Journal of biological chemistry
- 1991
Tissue form of type VII collagen from human skin and dermal fibroblasts in culture.
- BiologyEuropean journal of biochemistry
- 1987
The triple-helical domain of type VII collagen was isolated from human placental membranes by mild digestion with pepsin, and polyclonal antibodies were raised in rabbits against this protein, and this protein was identified by immunoblotting with the antibodies.
Transglutaminase-catalyzed cross-linking of fibrils of collagen V/XI in A204 rhabdomyosarcoma cells.
- BiologyBiochemistry
- 1995
Both collagens V and XI are specific glutaminyl substrates for tissue transglutaminase in vitro, as shown by incorporation of [3H]putrescine and Trypsin cleaved the 3H label from the alpha 1 chain of collagen V, demonstrating that the cross-linking occurs in the non triple helical propeptide domains.
Biochemical, Structural, and Transglutaminase Substrate Properties Of Human Loricrin, the Major Epidermal Cornified Cell Envelope Protein (*)
- BiologyThe Journal of Biological Chemistry
- 1995
The data support a hypothesis for the essential and complementary roles of both TGase 1 and TGase 3 in cross-linking of loricrin in vivo, and may explain the phenotype of lamellar ichthyosis, a disease caused by mutations in theTGase 1 gene.
Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes
- Biology, EngineeringThe Journal of cell biology
- 1993
Tissue transglutaminase expression in skeletal tissues is strictly regulated, correlates with chondrocyte differentiation, precedes cartilage calcification, and could lead to cross-linking of the mineralizing matrix.
Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme
- BiologyJournal of cellular physiology
- 1991
It is reported here that endogenous tissue TGase is localized on the adjacent ECM after puncture wounding embryonic human lung fibroblasts (WI‐38) and bound TGase persisted at the wound site for many hours, demonstrated by immunofluorescence and by catalytic activity using an overlay assay.







