Elastic fibres in the dermal papilla

Tsuji, Takuo

doi:10.1111/j.1365-2133.1980.tb06554.x

Cited by 26 publications

(8 citation statements)

References 11 publications

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“…At the tips of the undulations, dermal elastic microfibril bundles frequently inserted into the basal lamina and traversed deep into the dermis, lending an element of stability to the serration pattern. Dermal elastic microfibril bundles are preferentially distributed in the dermal papillae [22], which is consistent with the distri bution of serrated cells.…”

Section: Regional Epidermal Specificities In Adult Skinsupporting

confidence: 77%

Epidermal-dermal Interactions in Adult Skin.

Briggaman¹

1982

J Invest Dermatol

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Epidermal-dermal interactions are important determinants of embryonic development in skin. This review examines the role of such epidermal-dermal interactions in the conservation of epithelial specificity in adult skin. The basic epidermal keratinization program as defined as a proliferative basal cell population, orderly stratified cytodifferentiation of the cells and production of stratum corneum can be expressed by adult epidermis without the continued presence of a specific dermis. This is evidenced by the ability of epidermis to differentiate fully in association with nondermal connective tissues. Several other epithelia including cornea and esophagus express their specific differentiative characteristics without the continued presence of specific connective tissue. On the other hand, certain regional epithelial specificities in adult skin may be determined by the dermis. These regional epidermal specificities involve alterations in epidermal thickness, size of epidermal compartments including the stratum corneum, and the folding pattern at the epidermal-dermal interface. Possible mechanisms by which dermis could control these regional characteristics are discussed. Epidermal-dermal recombination techniques have been used to define the site of gene action in a variety of inherited skin abnormalities in animals. Similar studies are reported utilizing adult human skin in long-term cultivation on nude athymic mice. The abnormal gene in lamellar ichthyosis exerts its effect directly on the epidermis. Generalized exfoliative psoriasis was also studied by recombination techniques. Both epidermis and dermis were required for the maintenance of psoriatic morphology, suggesting a complex polygenic mechanism or one involving both genetic and environmental factors.

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Section: Regional Epidermal Specificities In Adult Skinsupporting

confidence: 77%

Epidermal-dermal Interactions in Adult Skin.

Briggaman¹

1982

J Invest Dermatol

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“…Although it is a general principle that microfibrils intersect with basement membranes in various tissues (2)(3)(4)(5)(6)(7)(8), virtually nothing is known about how microfibrils are physically connected to these basement membranes. In this respect, the functional significance of the perlecan presence on microfibrils may also include mechanical anchoring of microfibrils to basement membranes or to structures in close vicinity of basement membranes.…”

Section: Discussionmentioning

confidence: 99%

“…Microfibrils are also found in the absence of elastin in many tissues either as individual entities or intersecting with basement membranes. In fact, attachment of microfibrils to basement membranes represents a universal principle of virtually all types of basement membranes in a broad variety of tissues such as blood vessels (2), eye (3), kidney (4), lung (5), muscle (6), fetal membranes (7), and skin (8).…”

mentioning

confidence: 99%

Microfibrils at Basement Membrane Zones Interact with Perlecan via Fibrillin-1

Tiedemann

Sasaki

Gustafsson

et al. 2005

Journal of Biological Chemistry

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Mutational defects in fibrillin-rich microfibrils give rise to a number of heritable connective tissue disorders, generally termed microfibrillopathies. To understand the pathogenesis of these microfibrillopathies, it is important to elucidate the supramolecular composition of microfibrils and their interaction properties with extracellular matrix components. Here we demonstrate that the proteoglycan perlecan is an associated component of microfibrils typically close to basement membrane zones. Double immunofluorescence studies demonstrate colocalization of fibrillin-1, the major backbone component of microfibrils, with perlecan in fibroblast cultures as well as in dermal and ocular tissues. Double immunogold labeling further confirms colocalization of perlecan to microfibrils in various tissues at the ultrastructural level. Extraction studies revealed that perlecan is not covalently associated with microfibrils. High affinity interactions between fibrillin-1 and perlecan were found by kinetic binding studies with dissociation constants in the low nanomolar range. A detailed mapping study of the interaction epitopes by solid phase binding assays primarily revealed interactions of perlecan domains I and II with a central region of fibrillin-1. Analysis of perlecan null embryos showed less microfibrils at the dermal-epidermal junction as compared with wild-type littermates. The data presented indicate a functional significance for perlecan in anchoring microfibrils to basement membranes and in the biogenesis of microfibrils.

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“…Electron micrographs of basement membrane regions in skin (Tsuji, 1980), lung (Low, 1961), kidney (Farquhar et al, 1961), and lens capsule (Raviola, 1971) reveal small connective tissue spaces with bundles of microfibrils that appear to intersect the lamina densa. These microfibrils intersecting basement membranes lack a visible amorphous elastic component.…”

mentioning

confidence: 99%

Fibrillin-1 and Fibulin-2 Interact and Are Colocalized in Some Tissues

Reinhardt

Sasaki

Dzamba

et al. 1996

Journal of Biological Chemistry

208

210

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Microfibrils 10 -12 nm in diameter are found in elastic and non-elastic tissues with fibrillin as a major component. Little is known about the supramolecular structure of these microfibrils and the protein interactions it is based on. To identify protein binding ligands of fibrillin-1, we tested binding of recombinant fibrillin-1 peptides to different extracellular matrix proteins in solid phase assays. Among the proteins tested, only fibulin-2 showed significant binding to rF11, the N-terminal half of fibrillin-1, in a calcium-dependent manner. Surface plasmon resonance demonstrated high affinity binding with a K d ‫؍‬ 56 nM. With overlapping recombinant fibrillin-1 peptides, the binding site for fibulin-2 was narrowed down to the N terminus of fibrillin-1 (amino acid positions 45-450). Immunofluorescence in tissues demonstrated colocalization of fibrillin and fibulin-2 in skin, perichondrium, elastic intima of blood vessels, and kidney glomerulus. Fibulin-2 was not present in ocular ciliary zonules, tendon, and the connective tissue around kidney tubules and lung alveoli, which all contain fibrillin. Immunogold labeling of fibulin-2 on microfibrils in skin was found preferentially at the interface between microfibrils and the amorphous elastin core, suggesting that in vivo the interaction between fibrillin-1 and fibulin-2 is regulated by cellular expression and deposition as well as by protein-protein interactions.

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Elastic fibres in the dermal papilla

Cited by 26 publications

References 11 publications

Epidermal-dermal Interactions in Adult Skin.

Epidermal-dermal Interactions in Adult Skin.

Microfibrils at Basement Membrane Zones Interact with Perlecan via Fibrillin-1

Fibrillin-1 and Fibulin-2 Interact and Are Colocalized in Some Tissues

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