Cited by 250Genetic and rare skin diseases.Skin and Cellular Biology ResearchDermatology and Skin Diseases

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Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of Mal de Meleda

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Chimienti, F.·2003·Human Molecular Genetics

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Abstract

Mal de Meleda is an autosomal recessive inflammatory and keratotic palmoplantar skin disorder due to mutations in the ARS B gene, encoding for SLURP-1 (secreted mammalian Ly-6/uPAR-related protein 1). SLURP-1 belongs to the Ly-6/uPAR superfamily of receptor and secreted proteins, which participate in signal transduction, immune cell activation or cellular adhesion. The high degree of structural similarity between SLURP-1 and the three fingers motif of snake neurotoxins and Lynx1 suggests that this protein interacts with the neuronal acetylcholine receptors. We found that SLURP-1 potentiates the human alpha 7 nicotinic acetylcholine receptors that are present in keratinocytes. These results identify SLURP-1 as a secreted epidermal neuromodulator which is likely to be essential for both epidermal homeostasis and inhibition of TNF-alpha release by macrophages during wound healing. This explains both the hyperproliferative as well as the inflammatory clinical phenotype of Mal de Meleda.

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Saitou, N., & Nei, M. (1987) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040454 · Cited by 59,959
Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin
Borovikova, L. V., Ivanova, S., Zhang, M., Yang, H., Botchkina, G. I., Watkins, L. R., Wang, H., Abumrad, N., Eaton, J. W., & Tracey, K. J. (2000) · Nature · doi:10.1038/35013070 · Cited by 4,211
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Wang, H., Yu, M., Ochani, M., Amella, C. A., Tanovic, M., Susarla, S., Li, J. H., Wang, H., Yang, H., Ulloa, L., et al. (2003) · Nature · doi:10.1038/nature01339 · Cited by 3,228
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Kelley, L. A., MacCallum, R. M., & Sternberg, M. J. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3741 · Cited by 1,464
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Blasi, F., & Carmeliet, P. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm977 · Cited by 1,224
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Jordan, M., Schallhorn, A., & Wurm, F. M. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.4.596 · Cited by 862
Human keratinocytes are a source for tumor necrosis factor alpha: evidence for synthesis and release upon stimulation with endotoxin or ultraviolet light.
Köck, A., Schwarz, T., Kirnbauer, R., Urbanski, A., Perry, P., Ansel, J. C., & Luger, T. A. (1990) · The Journal of Experimental Medicine · doi:10.1084/jem.172.6.1609 · Cited by 712
Prostate stem cell antigen: A cell surface marker overexpressed in prostate cancer
Reiter, R. E., Gu, Z., Watabe, T., THOMAS, G. V., Szigeti, K., Davis, E., Wahl, M. I., Nisitani, S., Yamashiro, J. M., Beau, M. M. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1735 · Cited by 675
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Menon, G. K., Grayson, S., & Elias, P. M. (1985) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12273485 · Cited by 457
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Miwa, J. M., Ibáñez-Tallon, I., Crabtree, G. W., Sánchez, R., Šali, A., Role, L. W., & Heintz, N. (1999) · Neuron · doi:10.1016/s0896-6273(00)80757-6 · Cited by 287

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Rat retinal transcriptome: Effects of aging and AMD-like retinopathy
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SLURP-1 and -2 in normal, immortalized and malignant oral keratinocytes
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Levitin, F., Weiss, M., Hahn, Y., Stern, O., Papke, R. L., Matusik, R. J., Nandana, S., Ziv, R., Pichinuk, E., Salame, S., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801454200 · Cited by 62
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Primary sensory neuronal expression of SLURP-1, an endogenous nicotinic acetylcholine receptor ligand.
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Authors: Chimienti, F.
Affiliations: Centre Hospitalier Universitaire Vaudois (CH)
Corresponding author: Chimienti, F.
ORCID: Chimienti, F.
Venue: Human Molecular Genetics
Publisher: Oxford University Press (OUP)
Published: 2003-09-18
Volume: 12
Issue: 22
Pages: 3017-3024
ISSN: 0964-6906 (ISSN-L)
1460-2083
DOI: 10.1093/hmg/ddg320
OpenAlex: W2127747996
Cited by: 247
References: 40
Citations by year: 2026: 2 · 2025: 4 · 2024: 3 · 2023: 7 · 2022: 2 · 2021: 8 · 2020: 7 · 2019: 8 · 2018: 9 · 2017: 11 · 2016: 14 · 2015: 16 · 2014: 12 · 2013: 9 · 2012: 18
FWCI: 6.05
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Human Molecular Genetics (publishedVersion)
PubMed (publishedVersion)
SERVAL (Université de Lausanne) (publishedVersion, other-oa)
reroDoc Digital Library (submittedVersion)
IRIS (submittedVersion)
Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Funders: National Science Foundation
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
Topics: Health Sciences › Medicine › Dermatology › Genetic and rare skin diseases.
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
Health Sciences › Medicine › Dermatology › Dermatology and Skin Diseases
Keywords: SLURP-1, Mal de Meleda, alpha7 nicotinic acetylcholine receptor, keratinocytes, keratosis, anti-TNF therapy, macrophages, wound healing, epidermal homeostasis, autosomal recessive inheritance
MeSH terms: Acetylcholine, Amino Acid Sequence, Animals, Antigens, Ly, Cell Line, Cell Nucleus, Clone Cells, Dose-Response Relationship, Drug, Epidermis, Female, Genes, Recessive, Humans, Keratoderma, Palmoplantar, Microinjections, Models, Molecular, Moths, Mutation, Oocytes, Peptides, Phenotype, Receptors, Cholinergic, Recombinant Proteins, Urokinase-Type Plasminogen Activator, Xenopus laevis, Protein Structure, Tertiary, DNA, Complementary, Neurotransmitter Agents, Patch-Clamp Techniques

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Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of Mal de Meleda

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