Sandbox Reserved 1099: Difference between revisions

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However, some cleavage of the precursor occurred probably in sweat to produce different active forms of dermcidin peptide. The most abundant proteolytically processed DCD peptide presents in sweat is '''DCD-1L''' (in bold).

DCD-1L is created by proteases in sweat after the first post-secretory processing step consisting to reduce the peptide to the C-terminal thereupon containing 48 residues, from the 63 to the 110 amino acid. And secondly, the cathepsin D with 1,10-phenthroline-sensitive carboxypeptidase still not cited in sweat composition yet and an unidentified endoprotease contribute to further processed the DCD-1L C-terminal to produce other derived-peptides <ref>Daniel Baechle, Thomas Flad, Alexander Cansier, Heiko Steffen, Birgit Schittek, Jonathan Tolson, Timo Herrmann, Hassan Dihazi􏰀, Alexander Beck, Gerhard A. Mueller􏰀, Margret Mueller, Stefan Stevanovic, Claus Garbe, Claudia A. Mueller, and Hubert Kalbacher. "Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L" J. Biol. Chem. 281, no. 9 (March 3, 2006): 5406-15. https://doi.org/10.1074/jbc.M504670200 </ref>. One of them is DCD-1.

DCD-1L is created by proteases in sweat after the first post-secretory processing step consisting to reduce the peptide to the C-terminal thereupon containing 48 residues, from the 63 to the 110 amino acid. And secondly, the cathepsin D with 1,10-phenthroline-sensitive carboxypeptidase still not cited in sweat composition yet and an unidentified endoprotease contribute to further processed the DCD-1L C-terminal to produce other derived-peptides <ref name = "cat">Daniel Baechle, Thomas Flad, Alexander Cansier, Heiko Steffen, Birgit Schittek, Jonathan Tolson, Timo Herrmann, Hassan Dihazi􏰀, Alexander Beck, Gerhard A. Mueller􏰀, Margret Mueller, Stefan Stevanovic, Claus Garbe, Claudia A. Mueller, and Hubert Kalbacher. "Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L" J. Biol. Chem. 281, no. 9 (March 3, 2006): 5406-15. https://doi.org/10.1074/jbc.M504670200 </ref>. One of them is DCD-1.

== Structural highlights ==

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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>

The derived peptides described before in the expression and maturation part can modulate innate immune response because they are effective against particular micro-~~organism~~.

The derived peptides described before in the expression and maturation part can modulate the innate immune response because they are effective against particular micro-organisms. For exemple the peptide SSL-25 have a huge and specific action on E. coli and S. aureus <ref name = "cat"/>.

== Related diseases ==

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@@ Line 22: / Line 22: @@
 However, some cleavage of the precursor occurred probably in sweat to produce different active forms of dermcidin peptide. The most abundant proteolytically processed DCD peptide presents in sweat is '''DCD-1L''' (in bold).
-DCD-1L is created by proteases in sweat after the first post-secretory processing step consisting to reduce the peptide to the C-terminal thereupon containing 48 residues, from the 63 to the 110 amino acid. And secondly, the cathepsin D with 1,10-phenthroline-sensitive carboxypeptidase still not cited in sweat composition yet and an unidentified endoprotease contribute to further processed the DCD-1L C-terminal to produce other derived-peptides <ref>Daniel Baechle, Thomas Flad, Alexander Cansier, Heiko Steffen, Birgit Schittek, Jonathan Tolson, Timo Herrmann, Hassan Dihazi􏰀, Alexander Beck, Gerhard A. Mueller􏰀, Margret Mueller, Stefan Stevanovic, Claus Garbe, Claudia A. Mueller, and Hubert Kalbacher. "Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L" J. Biol. Chem. 281, no. 9 (March 3, 2006): 5406-15. https://doi.org/10.1074/jbc.M504670200 </ref>. One of them is DCD-1.
+DCD-1L is created by proteases in sweat after the first post-secretory processing step consisting to reduce the peptide to the C-terminal thereupon containing 48 residues, from the 63 to the 110 amino acid. And secondly, the cathepsin D with 1,10-phenthroline-sensitive carboxypeptidase still not cited in sweat composition yet and an unidentified endoprotease contribute to further processed the DCD-1L C-terminal to produce other derived-peptides <ref name = "cat">Daniel Baechle, Thomas Flad, Alexander Cansier, Heiko Steffen, Birgit Schittek, Jonathan Tolson, Timo Herrmann, Hassan Dihazi􏰀, Alexander Beck, Gerhard A. Mueller􏰀, Margret Mueller, Stefan Stevanovic, Claus Garbe, Claudia A. Mueller, and Hubert Kalbacher. "Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L" J. Biol. Chem. 281, no. 9 (March 3, 2006): 5406-15. https://doi.org/10.1074/jbc.M504670200 </ref>. One of them is DCD-1.
 == Structural highlights ==
@@ Line 52: / Line 52: @@
 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>
-The derived peptides described before in the expression and maturation part can modulate innate immune response because they are effective against particular micro-organism.
+The derived peptides described before in the expression and maturation part can modulate the innate immune response because they are effective against particular micro-organisms. For exemple the peptide SSL-25 have a huge and specific action on E. coli and S. aureus <ref name = "cat"/>.
 == Related diseases ==