FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2045492914> ?p ?o ?g. }

• W2045492914 endingPage "982" @default.
• W2045492914 startingPage "979" @default.
• W2045492914 abstract "epidermal melanocyte hair follicle melanocyte superoxide dismutase TO THE EDITOR Canities or senile hair graying, a universally recognized sign of aging, remains unresolved in terms of physiological causes, although a strong genetic contribution is understood (Gunn et al., 2009Gunn D.A. Rexbye H. Griffiths C.E. et al.Why some women look young for their age.PLoS One. 2009; 4: e8021Crossref PubMed Scopus (124) Google Scholar). As the hair fiber continues to grow long after melanin production ceases, we suggest that melanocytes in the hair follicle may be more sensitive to the impact of chronological aging than are keratinocytes. Moreover, follicular melanocytes also age more markedly than those in the overlying epidermis. The hair follicle provides a unique opportunity to decouple the impact of age on two hair follicular tissue functions: hair formation and hair pigmentation. Previous studies have pointed to a link between cellular aging mechanisms, including oxidative stress and hair graying (Arck et al., 2006Arck P.C. Overall R. Spatz K. et al.Towards a “free radical theory of graying”: melanocyte apoptosis in the aging human hair follicle is an indicator of oxidative stress induced tissue damage.FASEB J. 2006; 20: 1567-1569Crossref PubMed Scopus (155) Google Scholar; Wood et al., 2009Wood J.M. Decker H. Hartmann H. et al.Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair.FASEB J. 2009; 23: 2065-2075Crossref PubMed Scopus (141) Google Scholar). Commo et al., 2004Commo S. Gaillard O. Thibaut S. et al.Absence of TRP-2 in melanogenic melanocytes of human hair.Pigment Cell Res. 2004; 17: 488-497Crossref PubMed Scopus (56) Google Scholar and others (Nishimura et al., 2005Nishimura E.K. Granter S.R. Fisher D.E. Mechanisms of hair graying: incomplete melanocyte stem cell maintenance in the niche.Science. 2005; 307: 720-724Crossref PubMed Scopus (538) Google Scholar) have suggested that repopulation of the early anagen hair bulb with precursors of active melanocytes is also increasingly likely to fail with aging. However, most studies differentiate follicles on the basis of the level of pigmentation, not donor age. We also know that hair graying may be partially reversed in some skin disorders or after certain drug therapies (Reynolds et al., 1998Reynolds A. Murray P.I. Colloby P.S. Darkening of eyelashes in a patient treated with latanoprost.Eye (Lond). 1998; 12: 741-743Crossref PubMed Scopus (18) Google Scholar; Shaffrali et al., 2002Shaffrali F.C. McDonagh A.J. Messenger A.G. Hair darkening in porphyria cutanea tarda.Br J Dermatol. 2002; 146: 325-329Crossref PubMed Scopus (27) Google Scholar). Thus, graying may not necessarily indicate a complete deletion of the melanocyte stem cell population. We wanted to explore the impact of chronological age on melanocyte behavior to further understand the graying process and to identify associated molecular changes. This study provides analysis of race, age, and anatomically matched cultures of adult human epidermal and hair follicle melanocytes (HFMs) (Supplementary Table S1 online), and to our knowledge, this is previously unreported. Cultured HFMs showed at least three distinct sub-populations, including highly pigmented/dendritic bulbar melanocytes, less-differentiated tripolar cells, and an undifferentiated amelanotic bipolar sub-population (Supplementary Figure S1 online). By contrast, epidermal melanocytes (EMs) largely consisted of a homogeneous population of highly dendritic and uniformly weakly pigmented cells (Supplementary Figure S1 online). Unlike EMs, the most active melanocytes of the bulb do not survive when explanted ex vivo. Less-differentiated melanocytes, from elsewhere in the bulb and the outer root sheath, persist in graying, and can be cultured and induced to make melanin (Tobin and Paus, 2001Tobin D.J. Paus R. Graying: gerontobiology of the hair follicle pigmentary unit.Exp Gerontol. 2001; 36: 29-54Crossref PubMed Scopus (224) Google Scholar; Slominski et al., 2004Slominski A. Tobin D.J. Shibahara S. et al.Melanin pigmentation in mammalian skin and its hormonal regulation.Physiol Rev. 2004; 84: 1155-1228Crossref PubMed Scopus (1300) Google Scholar). Download .pdf (.25 MB) Help with pdf files Supplementary Information Proliferation of HFMs and EMs was examined in matched cultures derived from young, middle-aged, and older donors (Supplementary Table S1 online). Both EM and HFM proliferation decreased with age, HFM by 49.7±2.4% and EM by 42.6±5.7%. Tyrosinase expression was reduced with age in EMs by 51.6% and by 77.1% in HFMs (Supplementary Table S2 and S3 online; Supplementary Figure 1 online). In marked contrast, tyrosinase-related protein-1 expression was increased with age in both EMs (+24.3%) and HFMs (+43.6%) (Supplementary Table S2 and S3 online; Figure 1). It was noteworthy that dopachrome tautomerase was greatly reduced in EMs obtained from older donors, but the expression of the native form of this important melanogenic enzyme was elevated by 67.2% with age in HFMs (Supplementary Table S2 and S3 online), although the glycosylated form was much less affected. Recent data from our laboratory have shown that dopachrome tautomerase levels may be associated with protection against oxidative stress in EMs (Gledhill et al., unpublished). Dopachrome tautomerase may also provide such protection from quinone metabolites (Michard et al., 2008Michard Q. Commo S. Rocchetti J. et al.TRP-2 expression protects HEK cells from dopamine- and hydroquinone-induced toxicity.Free Radic Biol Med. 2008; 45: 1002-1010Crossref PubMed Scopus (16) Google Scholar), highlighting an additional non-pigmentary role for this enzyme in maintaining cellular redox status. The precise relationship between dopachrome tautomerase and eumelanogenic HFMs remains unresolved, as this relationship seems to vary between follicles from different body sites (Commo et al., 2004Commo S. Gaillard O. Thibaut S. et al.Absence of TRP-2 in melanogenic melanocytes of human hair.Pigment Cell Res. 2004; 17: 488-497Crossref PubMed Scopus (56) Google Scholar; Thibaut et al., 2009Thibaut S. De Becker E. Caisey L. et al.Human eyelash characterization.Br J Dermatol. 2009; 162: 304-310Crossref PubMed Scopus (35) Google Scholar). Recent data have suggested that HFMs and EMs may be regulated independently; even by shared signaling pathways (Van Raamsdonk et al., 2009Van Raamsdonk C.D. Barsh G.S. Wakamatsu K. et al.Independent regulation of hair and skin color by two G protein-coupled pathways.Pigment Cell Melanoma Res. 2009; 22: 819-826Crossref PubMed Scopus (37) Google Scholar). As accumulation of oxidative stress is a leading cellular aging mechanism, and melanin synthesis itself is an oxidative process (Pawelek and Lerner, 1978Pawelek J.M. Lerner A.B. 5,6-Dihydroxyindole is a melanin precursor showing potent cytotoxicity.Nature. 1978; 276: 626-628Crossref PubMed Scopus (154) Google Scholar), we examined the relative expression of key anti-oxidant enzymes (such as catalase, superoxide dismutase (SOD)-1, and SOD-2) in fully matched HFMs and EMs obtained from donors of different ages. SOD-1 and SOD-2 protein expressions were similar in HFMs and EMs and were not changed with age (data not shown). However, by contrast, catalase expression was markedly reduced in HFMs derived from older donors as seen by immunocytochemical examination (Figure 2a1, a2 vs. b1, b2) and western blotting (68.8% reduction with age; Figure 2c; Supplementary Table S4 online), and catalase activity was also reduced with age (42.0% Figure 2e). Catalase expression was also reduced in EMs with age (51.6% Figure 2c; Supplementary Table S4 online). Lowered catalase protein expression/activity with elevated H2O2 production, due to superoxide dismutation by SOD, may lead to an accumulation of H2O2 in cells. This is likely to have cytotoxic implications; such a scenario has been implicated in vitiligo (Wood et al., 2008Wood J.M. Gibbons N.C. Chavan B. et al.Computer simulation of heterogeneous single nucleotide polymorphisms in the catalase gene indicates structural changes in the enzyme active site, NADPH-binding and tetramerization domains: a genetic predisposition for an altered catalase in patients with vitiligo?.Exp Dermatol. 2008; 17: 366-371Crossref PubMed Scopus (20) Google Scholar). Although we did not measure H2O2 levels in our EMs and HFMs, we have subsequently shown that addition of H2O2 reveals an “aged” HFM phenotype that is refractory to stress responses (Kauser et al., manuscript in preparation). Keratinocytes surrounding melanocytes in the epidermis may well be a source of H2O2 that is uncharged and freely diffusible (Pelle et al., 2005Pelle E. Mammone T. Maes D. et al.Keratinocytes act as a source of reactive oxygen species by transferring hydrogen peroxide to melanocytes.J Invest Dermatol. 2005; 124: 793-797Crossref PubMed Scopus (71) Google Scholar), and there is evidence of H2O2 damage to proteins in graying hair follicles (Wood et al., 2009Wood J.M. Decker H. Hartmann H. et al.Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair.FASEB J. 2009; 23: 2065-2075Crossref PubMed Scopus (141) Google Scholar). Thus, the generalized loss of catalase in the hair follicle could contribute to an “aged” melanocyte phenotype, heightened by the greater age-related susceptibility of HFMs compared with their epidermal counterparts. Such oxidative damage may also, as suggested by others (Wood et al., 2009Wood J.M. Decker H. Hartmann H. et al.Senile hair graying: H2O2-mediated oxidative stress affects human hair color by blunting methionine sulfoxide repair.FASEB J. 2009; 23: 2065-2075Crossref PubMed Scopus (141) Google Scholar), cause damage to other systems in the hair follicle and affect the hair fiber itself. It may be expected that higher expression/activity of catalase is required by melanocytes with higher pigmentation levels (also in pigmented vs. the gray/white anagen hair bulbs); however, it is also the case that hair fiber production, by very high metabolic and mitotic activity in white/gray hair bulbs and associated reactive oxygen species production, does not seem to be impaired by the reduced catalase expression/activity in these follicles. In summary, we have demonstrated that we can successfully transfer an aged HFM phenotype from ex vivo skin to in vitro cell culture, and we now propose that catalase expression/activity is an important effector in the responses of melanocytes to aging. Our data lend support to the hypothesis that the susceptibility of HFMs to oxidative stress over time may be a major factor in the loss of hair pigment, the reduction in overall numbers of melanocytes per follicle, and ultimately for the increase in number of “white” hairs. This research was supported by Unilever R&D, UK. Supplementary material is linked to the online version of the paper at http://www.nature.com/jid" @default.
• W2045492914 created "2016-06-24" @default.
• W2045492914 creator A5009477818 @default.
• W2045492914 creator A5053029677 @default.
• W2045492914 creator A5062623085 @default.
• W2045492914 creator A5067673754 @default.
• W2045492914 date "2011-04-01" @default.
• W2045492914 modified "2023-10-17" @default.
• W2045492914 title "Human Hair Follicle and Epidermal Melanocytes Exhibit Striking Differences in Their Aging Profile which Involves Catalase" @default.
• W2045492914 cites W1982630371 @default.
• W2045492914 cites W1993590338 @default.
• W2045492914 cites W2003748223 @default.
• W2045492914 cites W2010622540 @default.
• W2045492914 cites W2014975722 @default.
• W2045492914 cites W2041578893 @default.
• W2045492914 cites W2043584813 @default.
• W2045492914 cites W2051082097 @default.
• W2045492914 cites W2072773214 @default.
• W2045492914 cites W2111368663 @default.
• W2045492914 cites W2118800143 @default.
• W2045492914 cites W2122552127 @default.
• W2045492914 cites W2139775939 @default.
• W2045492914 cites W2144200294 @default.
• W2045492914 cites W2329485902 @default.
• W2045492914 doi "https://doi.org/10.1038/jid.2010.397" @default.
• W2045492914 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21191398" @default.
• W2045492914 hasPublicationYear "2011" @default.
• W2045492914 type Work @default.
• W2045492914 sameAs 2045492914 @default.
• W2045492914 citedByCount "48" @default.
• W2045492914 countsByYear W20454929142012 @default.
• W2045492914 countsByYear W20454929142013 @default.
• W2045492914 countsByYear W20454929142014 @default.
• W2045492914 countsByYear W20454929142015 @default.
• W2045492914 countsByYear W20454929142016 @default.
• W2045492914 countsByYear W20454929142017 @default.
• W2045492914 countsByYear W20454929142018 @default.
• W2045492914 countsByYear W20454929142019 @default.
• W2045492914 countsByYear W20454929142020 @default.
• W2045492914 countsByYear W20454929142021 @default.
• W2045492914 countsByYear W20454929142022 @default.
• W2045492914 countsByYear W20454929142023 @default.
• W2045492914 crossrefType "journal-article" @default.
• W2045492914 hasAuthorship W2045492914A5009477818 @default.
• W2045492914 hasAuthorship W2045492914A5053029677 @default.
• W2045492914 hasAuthorship W2045492914A5062623085 @default.
• W2045492914 hasAuthorship W2045492914A5067673754 @default.
• W2045492914 hasBestOaLocation W20454929141 @default.
• W2045492914 hasConcept C102570824 @default.
• W2045492914 hasConcept C134018914 @default.
• W2045492914 hasConcept C16005928 @default.
• W2045492914 hasConcept C2776151105 @default.
• W2045492914 hasConcept C2777216303 @default.
• W2045492914 hasConcept C2777658100 @default.
• W2045492914 hasConcept C2778979269 @default.
• W2045492914 hasConcept C2779769559 @default.
• W2045492914 hasConcept C2909910311 @default.
• W2045492914 hasConcept C502942594 @default.
• W2045492914 hasConcept C71924100 @default.
• W2045492914 hasConcept C86803240 @default.
• W2045492914 hasConcept C95444343 @default.
• W2045492914 hasConceptScore W2045492914C102570824 @default.
• W2045492914 hasConceptScore W2045492914C134018914 @default.
• W2045492914 hasConceptScore W2045492914C16005928 @default.
• W2045492914 hasConceptScore W2045492914C2776151105 @default.
• W2045492914 hasConceptScore W2045492914C2777216303 @default.
• W2045492914 hasConceptScore W2045492914C2777658100 @default.
• W2045492914 hasConceptScore W2045492914C2778979269 @default.
• W2045492914 hasConceptScore W2045492914C2779769559 @default.
• W2045492914 hasConceptScore W2045492914C2909910311 @default.
• W2045492914 hasConceptScore W2045492914C502942594 @default.
• W2045492914 hasConceptScore W2045492914C71924100 @default.
• W2045492914 hasConceptScore W2045492914C86803240 @default.
• W2045492914 hasConceptScore W2045492914C95444343 @default.
• W2045492914 hasIssue "4" @default.
• W2045492914 hasLocation W20454929141 @default.
• W2045492914 hasLocation W20454929142 @default.
• W2045492914 hasOpenAccess W2045492914 @default.
• W2045492914 hasPrimaryLocation W20454929141 @default.
• W2045492914 hasRelatedWork W1500967168 @default.
• W2045492914 hasRelatedWork W1965404183 @default.
• W2045492914 hasRelatedWork W2045492914 @default.
• W2045492914 hasRelatedWork W2119529572 @default.
• W2045492914 hasRelatedWork W2122431136 @default.
• W2045492914 hasRelatedWork W2126945805 @default.
• W2045492914 hasRelatedWork W2410205450 @default.
• W2045492914 hasRelatedWork W4248717461 @default.
• W2045492914 hasRelatedWork W99770010 @default.
• W2045492914 hasRelatedWork W3032032708 @default.
• W2045492914 hasVolume "131" @default.
• W2045492914 isParatext "false" @default.
• W2045492914 isRetracted "false" @default.
• W2045492914 magId "2045492914" @default.
• W2045492914 workType "article" @default.