Decorin

[IDW2BB]

http://www.ncbi.nlm.nih.gov/pubmed/24816226

Expression of Decorin throughout the Murine Hair Follicle Cycle: Hair Cycle-Dependence and Anagen Phase Prolongation.

Jing J1, Wu XJ, Li YL, Cai SQ, Zheng M, Lu ZF.



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Abstract

Decorin is a prototypical member of the small leucine-rich proteoglycan (SLRP) family, which is involved in numerous biological processes. The role of decorin, as a representative SLRP, in hair follicle morphogenesis has not been elucidated. We present our initial findings on decorin expression patterns during induced murine HF cycles. It was found that: decorin expression is exclusively restricted to the epidermis, outer root sheath, and sebaceous glands during the anagen phase, which correlates with the upregulation of decorin mRNA and protein expression in depilated murine dorsal skin. Furthermore, we used a functional approach to investigate the effects of recombinant human decorin (rhDecorin) via cutaneous injection into HFs at various murine hair cycle stages. The local injection of rhDecorin (100 μg/ml) into the hypodermis of depilated C57BL/6 mice at anagen delayed catagen progression. In contrast, rhDecorin injection during the telogen phase caused the premature onset of anagen, as demonstrated by assessment of the following parameters: (1) hair shaft length, (2) follicular bulbar diameter, (3) hair follicle cycling score, and (4) follicular phase percentage. Taken together, our results suggest that decorin may modulate follicular cycling and morphogenesis. In addition, this study also provides insight into the molecular control mechanisms governing hair follicular epithelial-mesenchymal interactions. This article is protected by copyright. All rights reserved.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3623574/

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http://www.ncbi.nlm.nih.gov/pubmed/8326155

Hair follicle proteoglycans.

Couchman JR.



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Abstract

Proteoglycans are polymorphic macromolecules present in all mammalian tissues, including the skin and its appendages. They consist of a core protein to which one or more glycosaminoglycan chains are covalently attached. Broadly, they can be divided into classes based on location and core protein structure. These classes include cell surface proteoglycans, basement membrane proteoglycans, small leucine-rich proteoglycans, large proteoglycans aggregating with hyaluronan, and intracellular granule proteoglycans. They have a wide range of functions, but little is known of the proteoglycans that are present in the epithelial and stromal compartments of hair follicles. However, the transmembrane proteoglycan syndecan may be important in follicle morphogenesis, both with respect to the epithelium and dermal papilla cells. Syndecan may possess both heparan and chondroitin sulfate chains, interacts with growth factors as well as fibronectin and interstitial collagens, and can associate in a transmembrane relationship with the cellular cytoskeleton. It is strongly expressed in mesenchymal cells coincident with stromal-epithelial interactions during tissue morphogenesis. Proteoglycans are present in all basement membranes, including those surrounding the epithelial compartment of hair follicles. Additionally, and quite unlike the dermis, the dermal papilla is enriched in basement-membrane components, especially a chondroitin 6-sulfate-containing proteoglycan, BM-CSPG. The function of this proteoglycan is not known, but developmental studies indicate that it may have a role in stabilizing basement membranes. In the hair cycle, BM-CSPG decreases through catagen and is virtually absent from the telogen papilla. One or more heparan sulfate proteoglycans, including perlecan, are also present in papilla and follicular basement membranes. Some of the leucine-rich proteoglycans, such as decorin, are associated with interstitial collagens, and may influence fibrillogenesis. Because small amounts of types I and III collagens may be present in anagen papillae, decorin may also be a constituent.

 

[waynakyo]

New one:

http://www.ncbi.nlm.nih.gov/pubmed/24942290

[h=1][FONT=Verdana, Arial, Tahoma, Calibri, Geneva, sans-serif]A newly discovered linkage between proteoglycans and hair biology: Decorin acts as an anagen inducer.[/FONT][/h][FONT=Verdana, Arial, Tahoma, Calibri, Geneva, sans-serif]Inui S1, Itami S.[/FONT]
[h=3][FONT=Verdana, Arial, Tahoma, Calibri, Geneva, sans-serif]Author information[/FONT][/h]

[h=3][FONT=Verdana, Arial, Tahoma, Calibri, Geneva, sans-serif]Abstract[/FONT][/h][FONT=Verdana, Arial, Tahoma, Calibri, Geneva, sans-serif]Proteoglycans have been suggested to play pivotal roles in hair biology. Decorin is a prototypical member of the small leucine-rich proteoglycan family, which is involved in numerous biological processes. However, the role of decorin in the hair cycle has not been elucidated. Moreover, the effects of decorin on the activities of many growth factors are complex and it is hard to predict whether decorin would affect hair growth or the hair cycle positively or negatively. Jing et al. focused on the potential role of decorin in the hair cycle and found that decorin is highly expressed in the epidermis, in hair follicle epithelial cells and in dermal papilla cells in the anagen phase. The expression of decorin was decreased during catagen to telogen, except for the bulge region. Exogenous administration of decorin accelerated anagen and delayed catagen transition as a positive regulator of the hair cycle. Because TGF-β is one of androgen-induced pathogenic factors in androgenetic alopecia, this study provides clues to understand the pathogenesis and new therapeutic targets of hair loss. This article is protected by copyright. All rights reserved.[/FONT]
[FONT=Verdana, Arial, Tahoma, Calibri, Geneva, sans-serif]This article is protected by copyright. All rights reserved.[/FONT]