TY - JOUR
T1 - Highly complex peptide aggregates of the S100 fused-type protein hornerin are present in human skin
AU - Wu, Zhihong
AU - Meyer-Hoffert, Ulf
AU - Reithmayer, Katrin
AU - Paus, Ralf
AU - Hansmann, Britta
AU - He, Yinghong
AU - Bartels, Joachim
AU - Gläser, Regine
AU - Harder, Jürgen
AU - Schröder, Jens Michael
N1 - Funding Information:
We thank Dr Marie-Luise Kruse for help with laser scanning microscopy (DFG, SFB 415); Professor Joachim Grötzinger for secondary structure prediction of hornerin; Björn Schröder for help in the isolation of recombinant hornerin peptides; Christel Martensen-Kerl, Jutta Quitzau, Claudia Mehrens, and Marlies Brandt for excellent technical assistance; and Dr Neil Warner for help with the paper. This study was supported in parts by grants of the Deutsche Forschungsgemeinschaft DFG (SFB 617 J-M Schröder), the Medical Faculty of Kiel (U Meyer-Hoffert), the Deutsche Dermatologische Gesellschaft DDG (U Meyer-Hoffert), and from the Faculty Research Focus on Autoimmunity, University of Luebeck (R Paus).
PY - 2009/6
Y1 - 2009/6
N2 - Human hornerin (HRNR) is a 245kDa S100 fused-type protein which contains 95 tandem quasi-repeating glycine- and serine-rich domains. Previously HRNR was not thought to be expressed in healthy skin; however, we purified an HRNR peptide fragment from stratum corneum. Moreover, we found that HRNR mRNA is expressed in skin biopsies from different sites as head, trunk, legs, hands, and feet. In cultured human epidermal keratinocytes, HRNR mRNA expression was transiently induced during Ca2-dependent differentiation. Immunostaining using distinct antibodies generated against four putative HRNR domains revealed strong HRNR immunoreactivity in healthy epidermis as well as in the entire outer root sheath of normal human scalp hair follicles. In lesions from psoriasis and atopic dermatitis patients, HRNR immunoreactivity was reduced compared with uninvolved skin of these patients. Electrospray ionization mass spectrometry and Western blot analyses revealed that HRNR is a highly degradable protein that forms complex high molecular weight peptide aggregates. Our findings suggest that HRNR is expressed in healthy skin and give insight into the complex biology of this protein. HRNR and its degradation products might contribute to the barrier function of healthy human skin.
AB - Human hornerin (HRNR) is a 245kDa S100 fused-type protein which contains 95 tandem quasi-repeating glycine- and serine-rich domains. Previously HRNR was not thought to be expressed in healthy skin; however, we purified an HRNR peptide fragment from stratum corneum. Moreover, we found that HRNR mRNA is expressed in skin biopsies from different sites as head, trunk, legs, hands, and feet. In cultured human epidermal keratinocytes, HRNR mRNA expression was transiently induced during Ca2-dependent differentiation. Immunostaining using distinct antibodies generated against four putative HRNR domains revealed strong HRNR immunoreactivity in healthy epidermis as well as in the entire outer root sheath of normal human scalp hair follicles. In lesions from psoriasis and atopic dermatitis patients, HRNR immunoreactivity was reduced compared with uninvolved skin of these patients. Electrospray ionization mass spectrometry and Western blot analyses revealed that HRNR is a highly degradable protein that forms complex high molecular weight peptide aggregates. Our findings suggest that HRNR is expressed in healthy skin and give insight into the complex biology of this protein. HRNR and its degradation products might contribute to the barrier function of healthy human skin.
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U2 - 10.1038/jid.2008.370
DO - 10.1038/jid.2008.370
M3 - Article
C2 - 19020553
AN - SCOPUS:67349198055
VL - 129
SP - 1446
EP - 1458
JO - Journal of Investigative Dermatology
JF - Journal of Investigative Dermatology
SN - 0022-202X
IS - 6
ER -
