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Caspase-14 is required for filaggrin degradation to natural moisturizing factors in the skin

Esther Hoste UGent, Patrick Kemperman, Michael Devos UGent, Geertrui Denecker UGent, Sanja Kezic, Nico Yau, Barbara Gilbert UGent, Saskia Lippens UGent, Philippe De Groote UGent and Ria Roelandt UGent, et al. (2011) JOURNAL OF INVESTIGATIVE DERMATOLOGY. 131(11). p.2233-2241
abstract
Caspase-14 is a protease that is mainly expressed in suprabasal epidermal layers and activated during keratinocyte cornification. Caspase-14-deficient mice display reduced epidermal barrier function and increased sensitivity to UVB radiation. In these mice, profilaggrin, a protein with a pivotal role in skin barrier function, is processed correctly to its functional filaggrin (FLG) repeat unit, but proteolytic FLG fragments accumulate in the epidermis. In wild-type stratum corneum, FLG is degraded into free amino acids, some of which contribute to generation of the natural moisturizing factors (NMFs) that maintain epidermal hydration. We found that caspase-14 cleaves the FLG repeat unit and identified two caspase-14 cleavage sites. These results indicate that accumulation of FLG fragments in caspase-14(-/-) mice is due to a defect in the terminal FLG degradation pathway. Consequently, we show that the defective FLG degradation in caspase-14-deficient skin results in substantial reduction in the amount of NMFs, such as urocanic acid and pyrrolidone carboxylic acid. Taken together, we identified caspase-14 as a crucial protease in FLG catabolism.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
AMINO-ACIDS, GENE, EPIDERMAL DIFFERENTIATION, BARRIER FUNCTION, UROCANIC ACID, STRATUM-CORNEUM, ICHTHYOSIS VULGARIS, OF-FUNCTION MUTATIONS, PROTEASE BLEOMYCIN HYDROLASE, MODEL
journal title
JOURNAL OF INVESTIGATIVE DERMATOLOGY
J. Invest. Dermatol.
volume
131
issue
11
pages
2233 - 2241
Web of Science type
Article
Web of Science id
000296240100017
JCR category
DERMATOLOGY
JCR impact factor
6.314 (2011)
JCR rank
1/58 (2011)
JCR quartile
1 (2011)
ISSN
0022-202X
DOI
10.1038/jid.2011.153
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1941957
handle
http://hdl.handle.net/1854/LU-1941957
date created
2011-11-10 15:25:41
date last changed
2012-06-26 14:32:25
@article{1941957,
  abstract     = {Caspase-14 is a protease that is mainly expressed in suprabasal epidermal layers and activated during keratinocyte cornification. Caspase-14-deficient mice display reduced epidermal barrier function and increased sensitivity to UVB radiation. In these mice, profilaggrin, a protein with a pivotal role in skin barrier function, is processed correctly to its functional filaggrin (FLG) repeat unit, but proteolytic FLG fragments accumulate in the epidermis. In wild-type stratum corneum, FLG is degraded into free amino acids, some of which contribute to generation of the natural moisturizing factors (NMFs) that maintain epidermal hydration. We found that caspase-14 cleaves the FLG repeat unit and identified two caspase-14 cleavage sites. These results indicate that accumulation of FLG fragments in caspase-14(-/-) mice is due to a defect in the terminal FLG degradation pathway. Consequently, we show that the defective FLG degradation in caspase-14-deficient skin results in substantial reduction in the amount of NMFs, such as urocanic acid and pyrrolidone carboxylic acid. Taken together, we identified caspase-14 as a crucial protease in FLG catabolism.},
  author       = {Hoste, Esther and Kemperman, Patrick and Devos, Michael and Denecker, Geertrui and Kezic, Sanja and Yau, Nico and Gilbert, Barbara and Lippens, Saskia and De Groote, Philippe and Roelandt, Ria and Van Damme, Petra and Gevaert, Kris and Presland, Richard B and Takahara, Hidenari and Puppels, Gerwin and Caspers, Peter and Vandenabeele, Peter and Declercq, Wim},
  issn         = {0022-202X},
  journal      = {JOURNAL OF INVESTIGATIVE DERMATOLOGY},
  keyword      = {AMINO-ACIDS,GENE,EPIDERMAL DIFFERENTIATION,BARRIER FUNCTION,UROCANIC ACID,STRATUM-CORNEUM,ICHTHYOSIS VULGARIS,OF-FUNCTION MUTATIONS,PROTEASE BLEOMYCIN HYDROLASE,MODEL},
  language     = {eng},
  number       = {11},
  pages        = {2233--2241},
  title        = {Caspase-14 is required for filaggrin degradation to natural moisturizing factors in the skin},
  url          = {http://dx.doi.org/10.1038/jid.2011.153},
  volume       = {131},
  year         = {2011},
}

Chicago
Hoste, Esther, Patrick Kemperman, Michael Devos, Geertrui Denecker, Sanja Kezic, Nico Yau, Barbara Gilbert, et al. 2011. “Caspase-14 Is Required for Filaggrin Degradation to Natural Moisturizing Factors in the Skin.” Journal of Investigative Dermatology 131 (11): 2233–2241.
APA
Hoste, Esther, Kemperman, P., Devos, M., Denecker, G., Kezic, S., Yau, N., Gilbert, B., et al. (2011). Caspase-14 is required for filaggrin degradation to natural moisturizing factors in the skin. JOURNAL OF INVESTIGATIVE DERMATOLOGY, 131(11), 2233–2241.
Vancouver
1.
Hoste E, Kemperman P, Devos M, Denecker G, Kezic S, Yau N, et al. Caspase-14 is required for filaggrin degradation to natural moisturizing factors in the skin. JOURNAL OF INVESTIGATIVE DERMATOLOGY. 2011;131(11):2233–41.
MLA
Hoste, Esther, Patrick Kemperman, Michael Devos, et al. “Caspase-14 Is Required for Filaggrin Degradation to Natural Moisturizing Factors in the Skin.” JOURNAL OF INVESTIGATIVE DERMATOLOGY 131.11 (2011): 2233–2241. Print.