A novel mutation in the ARS (component B) gene encoding SLURP-1 in a family with Mal de Meleda

Yerebakan, Özlem; Hu, Gang; Yılmaz, Ertan; Çelebi, Jülide Tok

doi:10.1046/j.1365-2230.2003.01342.x

Cited by 14 publications

(13 citation statements)

References 10 publications

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“…It is located in exon 3 corresponding to the Cterminus of the protein which probably is involved in the protein binding to its receptor [19]. Moreover, the truncated protein formed lacks one of the disulfide bridges which is critical for the normal function of the protein [22]. This mutation has been previously reported in patients from Turkey and Croatia [13].…”

Section: Discussionmentioning

confidence: 83%

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Mutations in the SLURP-1 gene underlie Mal de Meleda in three Pakistani families

Wajid

Kurban

Shimomura

et al. 2009

Journal of Dermatological Science

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Section: Discussionmentioning

confidence: 83%

“…In fact, most mutations are clustered in exon 3. MDM is an autosomal recessive palmoplantar keratoderma that is clinically and genetically heterogeneous [2] and detailed genotype-phenotype correlations are as yet unclear [22]. Most of the patients are members of consanguineous families [1].…”

Section: Discussionmentioning

confidence: 99%

Mutations in the SLURP-1 gene underlie Mal de Meleda in three Pakistani families

Wajid

Kurban

Shimomura

et al. 2009

Journal of Dermatological Science

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“…Interestingly, Leu-135 is conserved across mammalian species. Moreover, the corresponding residue in SLURP1, CD59, and UPAR is also a leucine, and a missense mutation involving that leucine in SLURP1 causes mal de Meleda (21).…”

Section: Discussionmentioning

confidence: 99%

Assessing the Role of the Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1) Three-finger Domain in Binding Lipoprotein Lipase

Beigneux¹,

Davies²,

Tat³

et al. 2011

Journal of Biological Chemistry

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Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) is an endothelial cell protein that transports lipoprotein lipase (LPL) from the subendothelial spaces to the capillary lumen. GPIHBP1 contains two main structural motifs, an amino-terminal acidic domain enriched in aspartates and glutamates and a lymphocyte antigen 6 (Ly6) motif containing 10 cysteines. All of the cysteines in the Ly6 domain are disulfide-bonded, causing the protein to assume a three-fingered structure. The acidic domain of GPIHBP1 is known to be important for LPL binding, but the involvement of the Ly6 domain in LPL binding requires further study. To assess the importance of the Ly6 domain, we created a series of GPIHBP1 mutants in which each residue of the Ly6 domain was changed to alanine. The mutant proteins were expressed in Chinese hamster ovary (CHO) cells, and their expression level on the cell surface and their ability to bind LPL were assessed with an immunofluorescence microscopy assay and a Western blot assay. We identified 12 amino acids within GPIHBP1, aside from the conserved cysteines, that are important for LPL binding; nine of those were clustered in finger 2 of the GPIHBP1 three-fingered motif. The defective GPIHBP1 proteins also lacked the ability to transport LPL from the basolateral to the apical surface of endothelial cells. Our studies demonstrate that the Ly6 domain of GPIHBP1 is important for the ability of GPIHBP1 to bind and transport LPL.

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“…Zhao et al suggest it may, if only for historical reasons [37]. Figure 2 [7,11,17,[32][33][34][35][36][38][39][40][41] shows an exon/intron map of the SLURP-1 gene and lists the mutation types and their location in Mal de Meleda (as well as the Gamborg-Nielsen variant).…”

Section: Genetics and Pathophysiologymentioning

confidence: 99%

“…c.1A>C (p. Met1Leu) [34] Ivs1+1G>A (alt splice site) [17] c.82delT (p.Cys28fs32X) [33] Ivs2+1G>A (alt splice site) [33] c.229T>C (p.Cys77Arg) [35] c.43T>C (p.Trp15Arg) [36] c.58+5G>T (alt splice site) [11] c.129C>A (p.C43X) [38] c.244C>T (p.Pro82Ser) [32] c.212G>A (p.Arg71His) [41] c.256G>C (p.Gly86Arg) [34] c.212G>C (p.Arg71Pro) [36] c.256G>A (p.Gly86Arg) [34] c.280T>A (p.Cys94Ser) [7] c.286C>T (p.Arg96Term) [33] c.293T>C (p.Leu98Pro) [39] c.296G>A (p.Cys99Tyr) [40] AD autosomal dominant, AR autosomal recessive, PPK palmoplantar keratoderma Reed et al [73] discussed effective treatment with oral 13-cis retinoid acid following failed treatment with corticosteroid, lactic acid, retinoid acid, and emollients. More recently, Gruber et al [32] showed effective treatment with oral acitretin 20 mg/day plus topical antimicrobial and keratolytic therapy.…”

Section: Intron 1 (405 Bp) Intron 2 (526 Bp)mentioning

confidence: 99%

Mal de Meleda: A Focused Review

Pérez

Khachemoune

2015

Am J Clin Dermatol

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Mal de Meleda is a rare autosomal recessive palmoplantar keratoderma (PPK) disease with an estimated prevalence of 1:100,000. Clinically, the onset of the disease is typically soon after birth and features a transgrediens (plantar surface progressing to dorsal surface) and progrediens (worsening with age) pattern of hyperkeratosis of the palms and soles. The disease can feature other potentially disfiguring effects on the hands and feet that can severely impact function. Histologically, the lesions show hyperkeratosis and acanthosis without epidermolysis in the epidermis, accompanied by perivascular lymphocytic infiltrate in the dermis. Secreted LY6/urokinase-type plasminogen activator receptor (uPAR)-related protein-1 (SLURP-1) genetic mutations are implicated in Mal de Meleda. SLURP-1 is involved in mediation of inflammation as well as keratinocyte apoptosis regulation. Because the disease is so rare, there are no set guidelines for management, but the accepted approach tends to include oral acitretin plus topical keratolytic therapy. Genetic counseling should also be offered. This focused review highlights the clinical and histological features, differential diagnoses, genetic background, and the current thoughts on management of Mal de Meleda.

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A novel mutation in the ARS (component B) gene encoding SLURP-1 in a family with Mal de Meleda

Cited by 14 publications

References 10 publications

Mutations in the SLURP-1 gene underlie Mal de Meleda in three Pakistani families

Mutations in the SLURP-1 gene underlie Mal de Meleda in three Pakistani families

Assessing the Role of the Glycosylphosphatidylinositol-anchored High Density Lipoprotein-binding Protein 1 (GPIHBP1) Three-finger Domain in Binding Lipoprotein Lipase

Mal de Meleda: A Focused Review

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