DCD

Official Full Name

dermcidin

Organism

Homo sapiens

Gene ID

117159

Background

This antimicrobial gene encodes 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 antibacterial and antifungal activities. The N-terminal peptide, also known as diffusible survival evasion peptide, promotes 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. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Oct 2014]

Synonyms

PIF; AIDD; DSEP; HCAP; DCD-1

Cat.No.	Product Name	Price
CSC-DC004076	Panoply™ Human DCD Knockdown Stable Cell Line	Inquiry
CSC-SC004076	Panoply™ Human DCD Over-expressing Stable Cell Line	Inquiry
CLOE-0180	Human DCD HEK293 Cell Lysate	Inquiry

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LV10377L	human DCD (NM_053283) lentivirus particles	Inquiry

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SHH275073	shRNA set against Human DCD (NM_053283.2)	Inquiry

Cat.No.	Product Name	Price
CDCB158265	Human DCD ORF clone (BC062682)	Inquiry
MiUTR1H-02685	DCD miRNA 3'UTR clone	Inquiry
CDCS416606	Human DCD ORF Clone (BC062682)	Inquiry

Detailed Information

The Dermcidin (DCD) gene, located on chromosome 8, is a highly conserved gene that plays a significant role in the regulation of various physiological processes, including cell differentiation, development, and stress responses. The gene encodes a protein called Dermcidin (DCD), which is a member of the small heat shock protein (sHSP) family. DCD is known to be involved in protecting cells from various environmental stresses such as heat, cold, and oxidative stress.

Structure And Function of DCD

The DCD gene is composed of 12 exons and the length of the encoded protein is 131 amino acids. The protein is characterized by a highly conserved N-terminal domain, a central alpha-Helical structural domains and a C-terminal domain. The N-terminal domain is responsible for the chaperone activity of DCD, which helps to protect cells from oxidative stress and other environmental stresses. These central alpha-Helical structural domains are involved in the dimerization of DCD, which is necessary for its chaperone activity. The C-terminal domain is responsible for the interaction of DCD with other cellular components and plays a role in the localization of the protein within the cell.

Regulation of DCD Expression

The DCD gene is regulated by various transcription factors and signaling pathways. One of the key regulators of DCD expression is the heat shock factor (HSF) protein. HSF binds to the heat shock element (HSE) present in the promoter region of the DCD gene and activates its transcription. Otherwise, DCD expression can also be regulated by other transcription factors such as basic leucine zipper (bZIP) proteins, nuclear factor-κB (NF-κB), and activating transcription factor 2 (ATF2).

Role of DCD in Cancer

DCD gene plays a crucial role in the process of cancerogenesis. DCD is a natural antimicrobial peptide encoded by the DCD gene, which is expressed in various tissues, including skin, lung, and prostate. Increasing evidence suggests that DCD expression is dysregulated in many types of cancers, contributing to the development and progression of the disease. In cancer cells, the DCD gene undergoes mutations and abnormal expressions, leading to its functional impairment. These mutations can cause the cells to lose normal growth control, enabling them to divide uncontrollably and form tumors. Moreover, DCD's antimicrobial function is also disrupted in cancer cells, leading to increased susceptibility to infections, which is common in cancer patients. The role of DCD in cancer progression is multifaceted. It has been implicated in promoting angiogenesis, the formation of new blood vessels that supply nutrients and oxygen to tumors. Additionally, DCD can modulate immune cell function, influencing the immune response against cancer cells. Furthermore, it interacts with various signaling pathways, such as the MAPK and PI3K/Akt pathways, which are critical for cancer cell survival and proliferation.

Figure 1. DCD may be involved in a few processes of many types of cancer cells.

References:

Stewart, Grant D et al. "The dermcidin gene in cancer: role in cachexia, carcinogenesis and tumour cell survival." Current opinion in clinical nutrition and metabolic care vol. 11,3 (2008): 208-13. doi:10.1097/MCO.0b013e3282fb7b8d
Li, Tiemei et al. "Bone Marrow Mesenchymal Stem Cell-Derived Dermcidin-Containing Migrasomes enhance LC3-Associated Phagocytosis of Pulmonary Macrophages and Protect against Post-Stroke Pneumonia." Advanced science (Weinheim, Baden-Wurttemberg, Germany) vol. 10,22 (2023): e2206432. doi:10.1002/advs.202206432
Schittek, Birgit. "The multiple facets of dermcidin in cell survival and host defense." Journal of innate immunity vol. 4,4 (2012): 349-60. doi:10.1159/000336844

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