Detection of dermcidin-derived peptides in sweat by ProteinChip® Technology

Flad, Thomas; Bogumil, Ralf; Tolson, Jonathan; Schittek, Birgit; Garbe, Claus; Deeg, Martin; Mueller, Claudia; Kalbacher, Hubert

doi:10.1016/s0022-1759(02)00229-6

Cited by 52 publications

(40 citation statements)

References 14 publications

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“…Although it is not clear how these polypeptides are produced from the entire DCD protein, it is likely that differential proteolysis is responsible for the production of the different DCD peptides. Four different peptides have been identified in sweat, and all of these peptides appear to be proteolytic products (Flad et al 2002). However, the specific proteases involved in differential proteolysis remain to be determined.…”

Section: Discussionmentioning

confidence: 99%

“…In eccrine sweat, differently processed DCD-derived C-terminal peptides comprising 48 aa residues (DCD-1L), 47 aa residues (DCD-1), and shorter fragments were detected (Flad et al 2002), and additional studies confirmed the antimicrobial activity of DCD-1L and DCD-1 against a variety of pathogenic micro-organisms (Schittek et al 2001, Vuong et al 2004, Lai et al 2005. Human sweat contains 1-10 mg/ml DCD-1, which is a concentration that is toxic to most micro-organisms that have been tested (Flad et al 2002). Using serial analysis of gene expression, Porter et al (2003) identified DCD as a candidate oncogene in breast cancer and suggested that DCD plays a role in tumorigenesis by enhancing cell growth and survival in a subset of breast carcinomas.…”

Section: Introductionmentioning

confidence: 99%

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Effect of dermcidin, an antimicrobial peptide, on body fat mobilization in normal mice

Kim¹,

Ka²,

Moon³

et al. 2008

Journal of Endocrinology

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Dermcidin (DCD), an antimicrobial peptide that is secreted by sweat glands, is reportedly a human homolog of mouse proteolysis-inducing factor. This study was conducted to investigate the effect of DCD on body fat mobilization. The expression level of DCD in the livers of Ad-DCD-injected mice was higher than in those of Ad-b-galactosidase (Ad-bgal)-injected mice 7 days after injection. In addition, injection with the Ad-DCD virus led to decreased body weight and epididymal fat mass when compared with controls. The plasma triglyceride level was decreased, whereas the free fatty acid and glycerol levels were increased in the Ad-DCDinjected group. Epididymal adipose tissues obtained from Ad-DCD-injected mice consisted of smaller adipocytes than tissues obtained from Ad-b-gal-injected mice. The gene expression profiles revealed an upregulation of hormonesensitive lipase and adipose fatty acid-binding protein, both of which are involved in adipocyte lipolysis, in Ad-DCDinjected mice, and this lipolytic effect of DCD paralleled the increase of circulating tumor necrosis factor-a (TNF-a) level that was observed. The perilipin levels in adipose tissue were decreased in Ad-DCD-injected mice when compared with those of the control mice. Taken together, these results suggest that DCD-mediated body fat reduction might occur as a result of TNF-a-induced downregulation of perilipin in adipose tissue.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effect of dermcidin, an antimicrobial peptide, on body fat mobilization in normal mice

Kim¹,

Ka²,

Moon³

et al. 2008

Journal of Endocrinology

View full text Add to dashboard Cite

show abstract

“…Secondly, the sequence of Y-P30 can be directly deduced from continuous exons and the cleavage site of the signal peptide is encoded entirely by exon 1, suggesting that they are not products of differential splicing. It is therefore likely that differential proteolysis is responsible for the production of the different dermcidin peptides and in sweat, four different peptides have been identified, which appear to be proteolytic products (Flad et al, 2002). The specific proteases involved remain to be determined.…”

Section: Discussionmentioning

confidence: 99%

Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues

et al. 2006

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Proteolysis-inducing factor, a cachexia-inducing tumour product, is an N-glycosylated peptide with homology to the unglycosylated neuronal survival peptide Y-P30 and a predicted product of the dermcidin gene, a pro-survival oncogene in breast cancer. We aimed to investigate whether dermcidin is pro-survival in liver cells, in which proteolysis-inducing factor induces catabolism, and to determine the role of potentially glycosylated asparagine residues in this function. Reverse cloning of proteolysis-inducing factor demonstrated B100% homology with the dermcidin cDNA. This cDNA was cloned into pcDNA3.1 þ and both asparagine residues removed using site-directed mutagenesis. In vitro translation demonstrated signal peptide production, but no difference in molecular weight between the products of native and mutant vectors. Immunocytochemistry of HuH7 cells transiently transfected with V5-His-tagged dermcidin confirmed targeting to the secretory pathway. Stable transfection conferred protection against oxidative stress. This was abrogated by mutation of both asparagines in combination, but not by mutation of either asparagine alone. These findings suggest that dermcidin may function as an oncogene in hepatic as well as breast cells. Glycosylation does not appear to be required, but the importance of asparagine residues suggests a role for the proteolysis-inducing factor core peptide domain.

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“…This class of peptides have the broad spectrum of action in the large diapason of pH and chloride ions ; molecular mass varied close to 5-8 kDa. They are excreted on the skin surface at 1-10 µg/ml of sweat, at that this concentration is toxic for bacteria and yeasts (Schittek et al, 2001;Flad et al, 2002). In connection with skin have mentioned the following dermcidins: DCD-1,DCD-1L, , among which are cationic, anionic and neutral peptides.…”

Section: Antimicrobial Peptides In Local Defence Of Skinmentioning

confidence: 99%

The New About Congenital Antimicrobial Defense of Some Epithelial Tissues – Vaginal Mucosa and Hair

Vera¹,

Ekaterina²,

Nune³

2012

A Search for Antibacterial Agents

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Detection of dermcidin-derived peptides in sweat by ProteinChip® Technology

Cited by 52 publications

References 14 publications

Effect of dermcidin, an antimicrobial peptide, on body fat mobilization in normal mice

Effect of dermcidin, an antimicrobial peptide, on body fat mobilization in normal mice

Dermcidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues

The New About Congenital Antimicrobial Defense of Some Epithelial Tissues – Vaginal Mucosa and Hair

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