Age-related changes of water content in the rat skin

Jung, Jinwook; Cha, Seung-Hoon; Lee, Seung−Chul; Chun, Inn-Ki; Kim, Young-Pio

doi:10.1016/s0923-1811(96)00542-7

Cited by 28 publications

(21 citation statements)

References 16 publications

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“…In this study we discovered that loss of DS decorin is associated with subtle, but reproducible, changes in the GAG composition of the skin, mainly characterized by a reduced overall sulfation of CS/DS up to 75 days of postnatal life. For wild-type mice the extracted uronic acid amount from skin is comparable to previous studies in rat as well as the finding of reduced sulfation with aging (Jung et al, 1997). A more detailed study revealed that the content of porcine skin decorin GAG was 0.1–0.12 mg/g wet skin (Zhao et al, 2013).…”

Section: Discussionsupporting

confidence: 87%

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A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function

et al. 2014

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Decorin is a small leucine-rich proteoglycan harboring a single glycosaminoglycan chain, which, in skin, is mainly composed of dermatan sulfate (DS). Mutant mice with targeted disruption of the decorin gene (Dcn−/−) exhibit an abnormal collagen architecture in the dermis and reduced tensile strength, collectively leading to a skin fragility phenotype. Notably, Ehlers-Danlos patients with mutations in enzymes involved in the biosynthesis of DS display a similar phenotype, and recent studies indicate that DS is involved in growth factor binding and signaling. To determine the impact of the loss of DS-decorin in the dermis, we analyzed the glycosaminoglycan content of Dcn−/− and wild-type mouse skin. The total amount of chondroitin/dermatan sulfate (CS/DS) was increased in the Dcn−/− skin, but was overall less sulfated with a significant reduction in bisulfated ΔDiS2,X (X=4 or 6) disaccharide units, due to the reduced expression of uronyl 2-O sulfotransferase (Ust). With increasing age, sulfation declined; however, Dcn−/− CS/DS was constantly undersulfated vis-à-vis wild-type. Functionally, we found altered fibroblast growth factor (Fgf)-7 and -2 binding due to changes in the micro-heterogeneity of skin Dcn−/− CS/DS. To better delineate the role of decorin, we used a 3D Dcn−/− fibroblast cell culture model. We found that the CS/DS extracts of wild-type and Dcn−/− fibroblasts were similar to the skin sugars, and this correlated with the lack of uronyl 2-O sulfotransferase in the Dcn−/− fibroblasts. Moreover, Ffg7 binding to total CS/DS was attenuated in the Dcn−/− samples. Surprisingly, wild-type CS/DS significantly reduced the binding of Fgf7 to keratinocytes in concentration dependent manner unlike the Dcn−/− CS/DS that only affected the binding at higher concentrations. Although binding to cell-surfaces was quite similar at higher concentrations, keratinocyte proliferation was differentially affected. Higher concentration of Dcn−/− CS/DS induced proliferation in contrast to wild-type CS/DS. 3D co-cultures of fibroblasts and keratinocytes showed that, unlike Dcn−/− CS/DS, wild-type CS/DS promoted differentiation of keratinocytes. Collectively, our results provide novel mechanistic explanations for the reported defects in wound healing in Dcn−/− mice and possibly Ehlers-Danlos patients. Moreover, the lack of decorin-derived DS and an altered CS/DS composition differentially influence keratinocyte behavior.

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Section: Discussionsupporting

confidence: 87%

“…1B). The content of CS/DS GAGs in wild-type is similar to the amount described for rat skin (Jung et al, 1997) and the amount of highly-sulfated CS/DS for the decorin extraction in porcine skin (Zhao et al, 2013). …”

Section: Resultssupporting

confidence: 71%

A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function

et al. 2014

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“…The water content of the skin is greatly influenced by ground substances, which may be responsible for wrinkling and laxity of the skin accompanying cutaneous ageing (Jung, Cha, Lee, Chun, & Kim, 1997). The results demonstrated that water level in mice skin was significantly reduced (p < 0.01) after exposure to UVA and UVB radiation (Table 1).…”

Section: Moisture and Lipids Contentsmentioning

confidence: 96%

“…Water contents dropped significantly and resulted in dry skin. Water content in the skin was presumed to be a critical determinant in cutaneous ageing, which may be responsible for wrinkling and laxity of the skin (Jung et al, 1997). CP1 and CP2 could reduce histological damage and the loss of water, which may be the reason why skin wrinkles were reduced.…”

Section: Moisture and Lipids Contentsmentioning

confidence: 99%

Moisture absorption and retention properties, and activity in alleviating skin photodamage of collagen polypeptide from marine fish skin

Hou

Zhang

et al. 2012

Food Chemistry

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“…According to Jung et al [36], the water and glycosaminoglycan content of the skin of Sprague-Dawley rats rapidly decreased until 3 months of age, then remained constant from 3 to 21 months of age. Similarly, Monterio-Riviere et al [37] reported that the epidermal thickness in Fischer-344 rats decreased from 2 to 3 months of age, then remained constant until 24 months of age.…”

Section: Enhancement Of Transdermal Penetration Of Fluorescein By Agingmentioning

confidence: 99%

Aging enhances maceration-induced ultrastructural alteration of the epidermis and impairment of skin barrier function

Minematsu

Yamamoto

Nagase

et al. 2011

Journal of Dermatological Science

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Age-related changes of water content in the rat skin

Cited by 28 publications

References 16 publications

A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function

A decorin-deficient matrix affects skin chondroitin/dermatan sulfate levels and keratinocyte function

Moisture absorption and retention properties, and activity in alleviating skin photodamage of collagen polypeptide from marine fish skin

Aging enhances maceration-induced ultrastructural alteration of the epidermis and impairment of skin barrier function

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