Dermcidin
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Ensembl |
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| Location (UCSC) | Chr 12: 54.64 – 54.65 Mb | n/a | |||||||
| PubMed search | [2] | n/a | |||||||
| View/Edit Human | |||
Dermcidin is a
anti-microbial peptides,[4] secreted by human eccrine sweat glands onto the skin as a part of the innate host defense of the immune system. PIF is involved in muscular proteolysis.[4]
Function
Dermcidin is a secreted protein that is subsequently processed into mature peptides of distinct biological activities. The C-terminal peptide is constitutively expressed in sweat and has
neural cell survival under conditions of severe oxidative stress. A glycosylated form of the N-terminal peptide may be associated with cachexia (muscle wasting) in cancer patients.[4]
Survival evasion peptide Antimicrobial peptide
YDPEAASAPGSGNPCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL
The C-terminal precursor DCD-1L is a 48 residue peptide that shows partial helicity in solution, as evidenced by the determination of its solution structure by
CD-spectroscopy. The full length precursor is processed by undetermined proteases present in human sweat, to form several shorter peptides that show variable antimicrobial activity, named according to their C-terminal triplet of amino acids and their residue length. One such active peptide is SSL25, which shows a 2-fold increase in activity against E. coli compared to DCD-1L.[5]
DCD-1L SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL DCD-1 SSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSV SSL25 SSLLEKGLDGAKKAVGGLGKLGKDA
Mechanism
The
ion gradient decoupling across biological membranes. This is supported by concurrent observations in experimental studies of a voltage dependent depolarization of lipid bilayers.[citation needed
]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000161634 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- S2CID 26126901.
- ^ a b c d "Entrez Gene: DCD dermicidin".
- PMID 16354654.
- PMID 23426625.
Further reading
- Todorov P, Cariuk P, McDevitt T, et al. (1996). "Characterization of a cancer cachectic factor". Nature. 379 (6567): 739–42. S2CID 4331928.
- Todorov PT, Deacon M, Tisdale MJ (1997). "Structural analysis of a tumor-produced sulfated glycoprotein capable of initiating muscle protein degradation". J. Biol. Chem. 272 (19): 12279–88. PMID 9139670.
- Cunningham TJ, Hodge L, Speicher D, et al. (1998). "Identification of a survival-promoting peptide in medium conditioned by oxidatively stressed cell lines of nervous system origin". J. Neurosci. 18 (18): 7047–60. PMID 9736629.
- Cunningham TJ, Jing H, Wang Y, Hodge L (2000). "Calreticulin binding and other biological activities of survival peptide Y-P30 including effects of systemic treatment of rats". Exp. Neurol. 163 (2): 457–68. S2CID 22279800.
- Cunningham TJ, Jing H, Akerblom I, et al. (2002). "Identification of the human cDNA for new survival/evasion peptide (DSEP): studies in vitro and in vivo of overexpression by neural cells". Exp. Neurol. 177 (1): 32–9. S2CID 11829104.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMID 12477932.
- Porter D, Weremowicz S, Chin K, et al. (2003). "A neural survival factor is a candidate oncogene in breast cancer". Proc. Natl. Acad. Sci. U.S.A. 100 (19): 10931–6. PMID 12953101.
- Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Sci. 13 (10): 2819–24. PMID 15340161.
- Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. PMID 15342556.
- Monitto CL, Dong SM, Jen J, Sidransky D (2005). "Characterization of a human homologue of proteolysis-inducing factor and its role in cancer cachexia". Clin. Cancer Res. 10 (17): 5862–9. PMID 15355918.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. PMID 15489334.
- Lai YP, Peng YF, Zuo Y, et al. (2005). "Functional and structural characterization of recombinant dermicidin-1L, a human antimicrobial peptide". Biochem. Biophys. Res. Commun. 328 (1): 243–50. PMID 15670776.
- Rieg S, Steffen H, Seeber S, et al. (2005). "Deficiency of dermicidin-derived antimicrobial peptides in sweat of patients with atopic dermatitis correlates with an impaired innate defense of human skin in vivo". J. Immunol. 174 (12): 8003–10. PMID 15944307.
- Watchorn TM, Dowidar N, Dejong CH, et al. (2006). "The cachectic mediator proteolysis inducing factor activates NF-kappaB and STAT3 in human Kupffer cells and monocytes". Int. J. Oncol. 27 (4): 1105–11. PMID 16142329.
- Lowrie AG, Wigmore SJ, Wright DJ, et al. (2006). "dermicidin expression in hepatic cells improves survival without N-glycosylation, but requires asparagine residues". Br. J. Cancer. 94 (11): 1663–71. PMID 16685272.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. PMID 17353931.
- Frum R, Busby SA, Ramamoorthy M, et al. (2007). "HDM2-binding partners: interaction with translation elongation factor EF1alpha". J. Proteome Res. 6 (4): 1410–7. PMID 17373842.
- Lee Motoyama JP, Kim-Motoyama H, Kim P, et al. (2007). "Identification of dermicidin in human gestational tissue and characterization of its proteolytic activity". Biochem. Biophys. Res. Commun. 357 (4): 828–33. PMID 17448443.
External links
- dermicidins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)