ArticleThe Journal of biological chemistry2011
Deimination of human filaggrin-2 promotes its proteolysis by calpain 1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 81 citations in OpenAlex.
- Review
- Role of Nutritional Elements in Skin Homeostasis: A Review.Biomolecules · 2025Review
- Neutrophil-Derived Peptidyl Arginine Deiminase Activity Contributes to Pulmonary Emphysema by Enhancing Elastin Degradation.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Cornification of keratinocytes is associated with differential changes in the catalytic activity and the immunoreactivity of transglutaminase-1.Scientific reports · 2023Article
- Deimination in epidermal barrier and hair formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Review
- Down-regulation of peptidylarginine deiminase type 1 in reconstructed human epidermis disturbs nucleophagy in the granular layer and affects barrier function.Cell death discovery · 2023Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Article
- Expression levels of filaggrin-2 in relation to drip loss in pigs.Animal bioscience · 2022Article
- Exome Sequencing of 5 Families with Severe Early-Onset Periodontitis.Journal of dental research · 2022Article
- The Discovery and Function of Filaggrin.International journal of molecular sciences · 2022Review
- Cracking the Skin Barrier: Liquid-Liquid Phase Separation Shines under the Skin.JID innovations : skin science from molecules to population health · 2021Review
- Edible Bird's Nest, an Asian Health Food Supplement, Possesses Moisturizing Effect by Regulating Expression of Filaggrin in Skin Keratinocyte.Frontiers in pharmacology · 2021Article
- Update on canine filaggrin: a review.The veterinary quarterly · 2020Review
- Deimination, Intermediate Filaments and Associated Proteins.International journal of molecular sciences · 2020Review
- Unveiling the Physical and Functional Niches of FAM26F by Analyzing Its Subcellular Localization and Novel Interacting Partners.ACS omega · 2020Article
- Eosinophilic Esophagitis in Adults: A Concise Overview of an Evolving Disease.Korean journal of family medicine · 2020Article
- Deimination and Peptidylarginine Deiminases in Skin Physiology and Diseases.International journal of molecular sciences · 2020Review
- Filaggrin and filaggrin 2 processing are linked together through skin aspartic acid protease activation.PloS one · 2020Article
- Peptidylarginine Deiminase Inhibitor Cl-Amidine Attenuates Cornification and Interferes with the Regulation of Autophagy in Reconstructed Human Epidermis.The Journal of investigative dermatology · 2019Article
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Filaggrin-2 (FLG2), a member of the S100-fused type protein family, shares numerous features with filaggrin (FLG), a key protein implicated in the epidermal barrier functions. Both display a related structural organization, an identical pattern of expression and localization in human epidermis, and proteolytic processing of a large precursor. Here, we tested whether FLG2 was a substrate of calpain 1, a calcium-dependent protease directly involved in FLG catabolism. In addition, deimination being critical for FLG degradation, we analyzed whether FLG2 deimination interfered with its proteolytic processing. With this aim, we first produced a recombinant form of FLG2 corresponding to subunits B7 to B10 fused to a COOH-terminal His tag. Incubation with calpain 1 in the presence of calcium induced a rapid degradation of the recombinant protein and the production of several peptides, as shown by Coomassie Blue-stained gels and Western blotting with anti-FLG2 or anti-His antibodies. MALDI-TOF mass spectrometry confirmed this result and further evidenced the production of non-immunoreactive smaller peptides. The degradation was not observed when a calpain 1-specific inhibitor was added. The calpain cleavage sites identified by Edman degradation were regularly present in the B-type repeats of FLG2. Moreover, immunohistochemical analysis of normal human skin revealed colocalization of FLG2 and calpain 1 in the upper epidermis. Finally, the FLG2 deiminated by human peptidylarginine deiminases was shown to be more susceptible to calpain 1 than the unmodified protein. Altogether, these data demonstrate that calpain 1 is essential for the proteolytic processing of FLG2 and that deimination accelerates this process.
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