The structure of type VII collagen
Available from: Douglas R Keene
- "This suggests that the HD defect in ΔVI-III grafts was more significant and more easily disrupted by external forces than the lack of type VII collagen/ laminin-332 binding associated with the absence of laminin β3 domain V-III. As type VII collagen is known to bind to other molecules, including collagen IV in the lamina densa (Burgeson et al., 1985) and collagen I in the papillary dermis (Villone et al., 2008), it is possible that these interactions can partially stabilize type VII collagen and provide a cohesive force even in the absence of laminin-332. "
Journal of Investigative Dermatology 08/2010; 130(8):2147-50. DOI:10.1038/jid.2010.85 · 7.22 Impact Factor
Available from: Carolyn C Compton
- "Previous studies of cultured autografts in burn patients have shown that full maturation of anchoring fibrils may take as long as 1 yr (Compton et al., 1989). The slowly increasing diameter of anchoring fibrils beneath the human xenografts supports the hypothesis that anchoring fibrils grow by continued unstaggered lateral aggregation of newly synthesized type VH procollagen/collagen dimers (Burgeson et al., 1985) and that they are not inserted into the hemidesmosomes from the stromal side (Gipson and Trinkhaus-Randall, 1985) after complete assembly in the dermis. The findings suggest that the transport of type VII procollagen/collagen can occur across a confluent basal lamina. "
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ABSTRACT: Anchoring fibrils are essential structural elements of the dermoepidermal junction and are crucial to its functional integrity. They are composed largely of type VII collagen, but their cellular origin has not yet been confirmed. In this study, we demonstrate that the anchoring fibrils are primarily a product of epidermal keratinocytes. Human keratinocyte sheets were transplanted to a nondermal connective tissue graft bed in athymic mice. De novo anchoring fibril formation was studied ultrastructurally by immunogold techniques using an antiserum specific for human type VII procollagen. At 2 d after grafting, type VII procollagen/collagen was localized both intracellularly within basal keratinocytes and extracellularly beneath the discontinuous basal lamina. Within 6 d, a subconfluent basal lamina had developed, and newly formed anchoring fibrils and anchoring plaques subjacent to the xenografts were labeled. Throughout the observation period of the experiment, the maturity, population density, and architectural complexity of anchoring fibrils beneath the human epidermal graft continuously increased. Identical findings were obtained using xenografts cultivated from cloned human keratinocytes, eliminating the possibility of contributions to anchoring fibril regeneration from residual human fibroblasts. Immunolabeling was not observed at the mouse dermoepidermal junction at any time. These results demonstrate that the type VII collagen of human cutaneous anchoring fibrils and plaques is secreted by keratinocytes and can traverse the epidermal basal lamina and that the fibril formation can occur in the absence of cells of human dermal origin.
The Journal of Cell Biology 12/1990; 111(5 Pt 1):2109-15. · 9.83 Impact Factor
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ABSTRACT: This paper presents a discussion and interpretation of critical factors relevant to the design of support systems to enhance the quality of organizational decisionmaking. The roles of information, feedback, and individual and organization learning in determining choice, and the organizational objectives that lead to choice and are responsive to choice, are emphasized.
Decision and Control, 1982 21st IEEE Conference on; 01/1983
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