Sandbox Reserved 1099: Difference between revisions
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Dermcidin is present in the sweat around 1-10 µg/ml. Spread by the sweat over the skin, DCD-1 acts like a regulator of the skin flora. The antimicrobial activity of DCD-1 is not only stable under different pH and salt conditions of the media but also under sweat-similar conditions.<ref> Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., Schirle, M., Schroeder, K., Blin, N., Meier, F., Rassner, G., Garbe, C., 2001. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol 2, 1133–1137. https://doi.org/10.1038/ni732 </ref> | Dermcidin is present in the sweat around 1-10 µg/ml. Spread by the sweat over the skin, DCD-1 acts like a regulator of the skin flora. The antimicrobial activity of DCD-1 is not only stable under different pH and salt conditions of the media but also under sweat-similar conditions.<ref> Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., Schirle, M., Schroeder, K., Blin, N., Meier, F., Rassner, G., Garbe, C., 2001. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol 2, 1133–1137. https://doi.org/10.1038/ni732 </ref> | ||
The overall negatively charged DCD-1L is a one amino acid longer DCD-1 and shows beside the antimicrobial activity against [https://en.wikipedia.org/wiki/Escherichia_coli_ ''Escherichia coli''], [https://en.wikipedia.org/wiki/Staphylococcus_aureus_ ''Staphylococcus aureus''] and [https://en.wikipedia.org/wiki/Enterococcus_faecalis_ ''Enterococcus faecalis''] additional high fungicidal activity on [https://en.wikipedia.org/wiki/Candida_albicans_ ''Candida albicans''].<ref name="novel"/> The first three amino acids (SSL) up to the 23th amino acids of DCD-1L is a region which appears to be responsible for the antibacterial activity. The killing of bacteria rises significantly after 2 – 3 hours of incubation which is not driven by a permeabilization of the outer nor inner bacterial membrane.<ref> Steffen, H., Rieg, S., Wiedemann, I., Kalbacher, H., Deeg, M., Sahl, H.-G., Peschel, A., Gotz, F., Garbe, C., Schittek, B., 2006. Naturally Processed Dermcidin-Derived Peptides Do Not Permeabilize Bacterial Membranes and Kill Microorganisms Irrespective of Their Charge. Antimicrobial Agents and Chemotherapy 50, 2608–2620. https://doi.org/10.1128/AAC.00181-06 </ref> However, some authors are not in agreement on this with each other<ref name="girdles"/> since it was also detected that DCD-1L creates ion channels into the bacterial membranes promoted by Zn<sup>2+</sup>.<ref> Paulmann, M., Arnold, T., Linke, D., Özdirekcan, S., Kopp, A., Gutsmann, T., Kalbacher, H., Wanke, I., Schuenemann, V.J., Habeck, M., Bürck, J., Ulrich, A.S., Schittek, B., 2012. Structure-Activity Analysis of the Dermcidin-derived Peptide DCD-1L, an Anionic Antimicrobial Peptide Present in Human Sweat. J. Biol. Chem. 287, 8434–8443. https://doi.org/10.1074/jbc.M111.332270 </ref> | The overall negatively charged DCD-1L is a one amino acid longer DCD-1 and shows beside the antimicrobial activity against [https://en.wikipedia.org/wiki/Escherichia_coli_ ''Escherichia coli''], [https://en.wikipedia.org/wiki/Staphylococcus_aureus_ ''Staphylococcus aureus''] and [https://en.wikipedia.org/wiki/Enterococcus_faecalis_ ''Enterococcus faecalis''] additional high fungicidal activity on [https://en.wikipedia.org/wiki/Candida_albicans_ ''Candida albicans''].<ref name="novel"/> The first three amino acids (SSL) up to the 23th amino acids of DCD-1L is a region which appears to be responsible for the antibacterial activity. The killing of bacteria rises significantly after 2 – 3 hours of incubation which is not driven by a permeabilization of the outer nor inner bacterial membrane.<ref> Steffen, H., Rieg, S., Wiedemann, I., Kalbacher, H., Deeg, M., Sahl, H.-G., Peschel, A., Gotz, F., Garbe, C., Schittek, B., 2006. Naturally Processed Dermcidin-Derived Peptides Do Not Permeabilize Bacterial Membranes and Kill Microorganisms Irrespective of Their Charge. Antimicrobial Agents and Chemotherapy 50, 2608–2620. https://doi.org/10.1128/AAC.00181-06 </ref> However, some authors are not in agreement on this with each other<ref name="girdles"/> since it was also detected that DCD-1L creates ion channels into the bacterial membranes promoted by Zn<sup>2+</sup>.<ref name="de"> Paulmann, M., Arnold, T., Linke, D., Özdirekcan, S., Kopp, A., Gutsmann, T., Kalbacher, H., Wanke, I., Schuenemann, V.J., Habeck, M., Bürck, J., Ulrich, A.S., Schittek, B., 2012. Structure-Activity Analysis of the Dermcidin-derived Peptide DCD-1L, an Anionic Antimicrobial Peptide Present in Human Sweat. J. Biol. Chem. 287, 8434–8443. https://doi.org/10.1074/jbc.M111.332270 </ref> | ||
DCD-1L is further processed ''in vitro'' but also in human sweat by the aspartate protease [https://www.uniprot.org/uniprot/P07339_ cathepsin D] (CatD) which cleaves between L44 and D45 and almost completely between L29 and E30. Actually, even more DCD-1L-derived peptides, namely 12, are present in human sweat. Some of them have no antimicrobial effect, however, one appears to be more active against ''E. coli'' than DCD-1L. Therefor the antimicrobial defense of humans does not stop at the point of DCD-1L but is more likely modulated by further proteolytic processes (e.g. by CatD) to maintain a healthy innate immune defense on the human skin.<ref name="baechle"/> | DCD-1L is further processed ''in vitro'' but also in human sweat by the aspartate protease [https://www.uniprot.org/uniprot/P07339_ cathepsin D] (CatD) which cleaves between L44 and D45 and almost completely between L29 and E30. Actually, even more DCD-1L-derived peptides, namely 12, are present in human sweat. Some of them have no antimicrobial effect, however, one appears to be more active against ''E. coli'' than DCD-1L. Therefor the antimicrobial defense of humans does not stop at the point of DCD-1L but is more likely modulated by further proteolytic processes (e.g. by CatD) to maintain a healthy innate immune defense on the human skin.<ref name="baechle"/> | ||
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===Skin disorders=== | ===Skin disorders=== | ||
Some skin disorders such as psoriasis are compensate by an overexpression and overproduction of the antimicrobial peptides. The results are that there are less infections on the injured skin.<ref> Harder, J., Bartels, J., Christophers, E., Schröder, J.-M., 1997. A peptide antibiotic from human skin. Nature 387, 861–861. https://doi.org/10.1038/43088 </ref> | Some skin disorders such as psoriasis are compensate by an overexpression and overproduction of the antimicrobial peptides. The results are that there are less infections on the injured skin.<ref> Harder, J., Bartels, J., Christophers, E., Schröder, J.-M., 1997. A peptide antibiotic from human skin. Nature 387, 861–861. https://doi.org/10.1038/43088 </ref> | ||
Atopic dermatitis is also linked to DCD peptides. A study proved that patients suffering from this skin disorder have reduced amount of these peptides which could provoke skin infections <ref name="de"/>. | |||
== References == | == References == | ||
<references /> | <references /> | ||
