2013 Fiscal Year Final Research Report
Significance of kallikrein-5 in the formation of filaggrin monomer
| Project/Area Number |
24659525
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Dermatology
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| Research Institution | Hamamatsu University School of Medicine |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
HIRAKAWA Satoshi 浜松医科大学, 医学部, 准教授 (50419511)
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| Co-Investigator(Renkei-kenkyūsha) |
SAKAVE Jun-ichi 浜松医科大学, 医学部, 特任助教 (30631494)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | 皮膚生理学 / フィラグリン / 角層 / バリア / カリクレイン / 角化細胞 |
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| Research Abstract |
Filaggrin contributes to the formation of the human skin barrier. Profilaggrin is cleaved by proteolytic enzymes and converted to functional filaggrin, but its processing mechanism remains not fully elucidated. Kallikrein-related peptidase 5 (KLK5) is a major serine protease found in the skin. We searched for profilaggrin-processing protease(s) by partial purification of epidermal extracts and found KLK5 as a possible candidate. We used HPLC coupled with mass spectrometry to show that KLK5 cleaves profilaggrin. KLK5 also cleaved fusion protein containing liker of profilaggrin. Furthermore, based on a proximity ligation assay, immunohistochemistry, and immunoelectron microscopy analysis, we reveal that KLK5 and profilaggrin co-localize in the stratum granulosum in human epidermis. KLK5 knockdown in normal cultured human epidermal keratinocytes resulted in higher levels of profilaggrin, indicating that KLK5 potentially functions in profilaggrin cleavage.
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[Journal Article] A group of atopic dermatitis without IgE elevation or barrier impairment shows a high Th1 frequency : Possible immunological state of the intrinsic type2012
Author(s)
Kabashima-Kubo R, Nakamura M, Sakabe JI, Sugita K, Hino R, Mori T, Kobayashi M, Bito T, Kabashima K, Ogasawara K, Nomura Y, Nomura T, Akiyama M, Shimizu H, Tokura Y.
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Journal Title
J Dermatol Sci
Volume: 67
Pages: 37-43
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