Sandbox Reserved 1099: Difference between revisions

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'''Dermcidin''' is a '''Human antimicrobial, anionic and ion membrane channel''' ([https://www.rcsb.org/structure/2YMK_ 2YMK]) discovered in 2001 based on 6 dermcidin antimicrobial peptides of 110 amino acids present in sweat. These peptides, encoded by the ''DCD gene'', play a role in the host defense system as a trimeric channel and thus, are able to prevent infection after injuries or any skin disorders. Scientists are focused on this molecule due to his charge particularity and since antibiotic resistances have been observed.
'''Dermcidin''' is a '''Human antimicrobial, anionic and ion membrane channel''' ([https://www.rcsb.org/structure/2YMK_ 2YMK]) discovered in 2001 based on 6 dermcidin antimicrobial peptides of 110 amino acids present in sweat. These peptides, encoded by the ''DCD gene'', play a role in the host defense system as a trimeric channel and thus, are able to prevent infection after injuries or any skin disorders. Scientists are focused on this molecule due to his charge particularity and since antibiotic resistances have been observed.
== Expression and maturation ==
Dermcidin gene (''DCD gene'') is located on the '''chromosome 12''' and constitutively expressed as '''precursor''' of 110 amino acids only in mucous cells of [https://en.wikipedia.org/wiki/Eccrine_sweat_gland_ eccrine sweat glands] within the dermis of the skin. The molecular weight of the DCD full-length sequence is 9.3 kDa including the signal peptide. The peptide is then secreted by granules in sweat and transported on the epidermal surface.
However, some clivage 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'''.
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. http://www.jbc.org/content/281/9/5406.long </ref>.


==Homology==
==Homology==
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But, some size and structural similarities can be found with the defensin family. <ref>Birgit Schittek, Rainer Hipfel, Birgit Sauer, Jürgen Bauer, Hubert Kalbacher, Stefan Stevanovic, Markus Schirle, Kristina Schroeder, Nikolaus Blin, Friedegund Meier, Gernot Rassner & Claus Garbe. "Dermcidin: a novel human antibiotic peptide secreted by sweat glands" Nature Immunology 2, no. 12 (December, 2001): 1133-37. https://www.nature.com/articles/ni732</ref>
But, some size and structural similarities can be found with the defensin family. <ref>Birgit Schittek, Rainer Hipfel, Birgit Sauer, Jürgen Bauer, Hubert Kalbacher, Stefan Stevanovic, Markus Schirle, Kristina Schroeder, Nikolaus Blin, Friedegund Meier, Gernot Rassner & Claus Garbe. "Dermcidin: a novel human antibiotic peptide secreted by sweat glands" Nature Immunology 2, no. 12 (December, 2001): 1133-37. https://www.nature.com/articles/ni732</ref>
== Expression and maturation ==
Dermcidin gene (''DCD gene'') is located on the '''chromosome 12''' and constitutively expressed as '''precursor''' of 110 amino acids only in mucous cells of [https://en.wikipedia.org/wiki/Eccrine_sweat_gland_ eccrine sweat glands] within the dermis of the skin. The molecular weight of the DCD full-length sequence is 9.3 kDa including the signal peptide. The peptide is then secreted by granules in sweat and transported on the epidermal surface.
However, some clivage 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'''.
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. http://www.jbc.org/content/281/9/5406.long </ref>.


== Structural highlights ==
== Structural highlights ==
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