Ultrastructural localization of keratinocyte surface associated heparan sulphate proteoglycans in human epidermis

AlmtractHigh-molecular-weight [t4C]hyaluronate was incubated with cultured fibroblasts from human uterine cervix and skin, and then the depolymerization of the hyaluronate was investigated.[14C]Hyaluronate in the medium of skin fibroblasts was depolymerized into a constant molecular weight (Mr about 40,000), whereas that of cervix fibroblasts was not depolymerized, irrespective of incubation period. However, when progesterone was added to the medium of cervix fibroblasts, hyaluronate was depolymerized to the same extent as that in skin fibroblasts. The reducing terminal sugar of the depolymerized hyaluronate was N-aeetylglucosamine. These results suggest that a hyaluronate-depolymerizing enzyme, endo-,&N-acetylglucosaminidase, was induced by progesterone in cultured fibroblasts derived from human uterine cervix.

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“…then, hyaluronate-depolymerizing enzymes having a similar mechanism of action have been reported by other investigators [5,6].…”

Section: Introductionsupporting

confidence: 78%

Hyaluronate depolymerization activity induced by progesterone in cultured fibroblasts derived from human uterine cervix

et al. 1994

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“…This enzyme is synthesized by keratinocytes during late differentiation and is abundantly present in the stratum corneum (31). Its substrate heparan sulfate is present in many skin proteoglycans such as syndecan, epican and glypican (32–34). The exact physiological role of heparanase 1 is still under discussion.…”

Section: Introductionmentioning

confidence: 99%

Carbohydrate expression and modification during keratinocyte differentiation in normal human and reconstructed epidermis

Méhul

Corre

Capon

et al. 2003

Experimental Dermatology

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Using fluorescein isothiocyanate (FITC)-labeled lectins we were able to demonstrate the presence of specific carbohydrate moieties in normal human and reconstructed epidermis. Evidence is provided that in both cases the strongly reduced lectin staining at the level of the stratum corneum is the result of a hindered accessibility of the lectins in this lipid-rich hydrophobic environment. Isolated corneocytes and purified cornified envelopes (CEs) exhibited clearly glycosylated structures reacting with distinct lectins. The presence of glycosidase activity, particularly in the upper layers of the epidermis characterized by an acidic environment (pH 5.5), indicates that modifications of the sugar residues might be important in epidermal homeostasis, barrier behavior and desquamation. Absent or strongly reduced glycosidase activity in the stratum corneum of reconstructed epidermis with an impaired pH gradient could be in part responsible for the reduced barrier function and the lack of desquamation in this model.

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“…Heparan sulfate is the most abundant of the GAG family, and is present through the epidermis [ 99 , 100 ]. It is a linear polysaccharide chain composed of D-glucosamine, D-glucuronic acid, and L-iduronic acid [ 101 ].…”

Section: Heparanasementioning

confidence: 99%

Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin

Tsunenaga

2016

CTE

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Recent research suggests that the basement membrane at the dermal-epidermal junction of the skin plays an important role in maintaining a healthy epidermis and dermis, and repeated damage to the skin can destabilize the skin and accelerate the aging process. Skin-equivalent models are suitable for studying the reconstruction of the basement membrane and its contribution to epidermal homeostasis because they lack the basement membrane and show abnormal expression of epidermal differentiation markers. By using these models, it has been shown that reconstruction of the basement membrane is enhanced not only by supplying basement membrane components, but also by inhibiting proteinases such as urokinase and matrix metalloproteinase. Although matrix metalloproteinase inhibitors assist in the reconstruction of the basement membrane structure, their action is not sufficient to promote its functional recovery. However, heparanase inhibitors stabilize the heparan sulfate chains of perlecan (a heparan sulfate proteoglycan) and promote the regulation of heparan sulfate binding growth factors in the basement membrane. Heparan sulfate promotes effective protein-protein interactions, thereby facilitating the assembly of type VII collagen anchoring fibrils and elastin-associated microfibrils. Using both matrix metalloproteinase inhibitors and heparanase inhibitors, the basement membrane in a skin-equivalent model comes close to recapitulating the structure and function of an in vivo basement membrane. Therefore, by using an appropriate dermis model and suitable protease inhibitors, it may be possible to produce skin-equivalent models that are more similar to natural skin

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Ultrastructural localization of keratinocyte surface associated heparan sulphate proteoglycans in human epidermis

Cited by 14 publications

References 37 publications

Hyaluronate depolymerization activity induced by progesterone in cultured fibroblasts derived from human uterine cervix

Hyaluronate depolymerization activity induced by progesterone in cultured fibroblasts derived from human uterine cervix

Carbohydrate expression and modification during keratinocyte differentiation in normal human and reconstructed epidermis

Heparanase Inhibitors Facilitate the Assembly of the Basement Membrane in Artificial Skin

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