Purpose Of Review: The diverse protein products of the dermcidin gene are relevant to immunity, cancer cell progression and cancer cachexia. This article evaluates recent developments/controversies around dermcidin.
Recent Findings: Dermcidin has recently been shown to act as a survival/proliferation factor in hepatoma and prostate cancer cell lines. Recent studies suggest that the Y-P30 subunit of the dermcidin polypeptide offers a survival advantage in such cancer cells. Nevertheless, the relevance of Y-P30 to cancer growth in vivo, and mechanisms of action remain unknown. In mice, tumour cells appear to glycosylate the Y-P30 subunit, transforming it into a potent skeletal muscle proteolysis-inducing factor. Recent work has described a receptor and signal transduction pathways for murine glycosylated proteolysis-inducing factor. The absence of classical N-glycosylation sites in the human proteolysis-inducing factor peptide and the lack of specific tools for the detection of the key carbohydrate moieties conferring the proteolysis-inducing activity, however, remain barriers to confirming glycosylated proteolysis-inducing factor as a pro-cachectic factor in humans.
Summary: There is a growing body of evidence illustrating dermcidin as an oncogene and Y-P30 as a survival factor. The biology of murine proteolysis-inducing factor as a pro-cachectic factor continues to evolve; however, its role in human biology remains speculative.
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http://dx.doi.org/10.1097/MCO.0b013e3282fb7b8d | DOI Listing |
Gan To Kagaku Ryoho
December 2019
Dept. of Pulmonary Medicine, Kyoto Prefectural University of Medicine, Graduate School of Medical Science.
Cachexia is well known to be a complication with malignant disease. The frequency of cancer-associated cachexia is different among various type of cancer, and relatively high in pancreas cancer, gastric cancer or lung cancer. The typical symptoms with cancer-associated cachexia includes body weight loss, appetite loss and general fatigue.
View Article and Find Full Text PDFPhysiol Rep
August 2019
Mays Cancer Center at UT Health San Antonio, San Antonio, Texas.
Muscle loss is a debilitating side effect to prostate cancer (PCa) experienced by nearly 60% of men. The purpose of this study was to test the hypothesis that Nexrutine , a bark extract from the Phellodendrum amurense, can protect against prostate cancer induced muscle loss in a similar manner as exercise, using the transgenic adenocarcinoma of mouse prostate (TRAMP) model. Forty-five, 8- to 10-week old TRAMP mice were randomized to either control, Nexrutine (600 mg/kg pelleted in chow) or exercise (voluntary wheel running).
View Article and Find Full Text PDFOncotarget
September 2016
Department of Bone Marrow Transplantation and Cancer Immunotherapy, Hadassah-Hebrew University Medical Center, Jerusalem, 91120, Israel.
Acute Radiation Syndrome (ARS) may lead to cancer and death and has few effective countermeasures. Efficacy of synthetic PIF treatment was demonstrated in preclinical autoimmune and transplantation models. PIF protected against inflammation and mortality following lethal irradiation in allogeneic bone marrow transplant (BMT) model.
View Article and Find Full Text PDFIn Vitro Cell Dev Biol Anim
September 2016
Nutritional Biomedicine, School of Life and Health Sciences, Aston University, Birmingham, B4 7ET, UK.
EPA has been clinically shown to reduce muscle wasting during cancer cachexia. This study investigates whether curcumin or green tea extract (GTE) enhances the ability of low doses of eicosapentaenoic acid (EPA) to reduce loss of muscle protein in an in vitro model. A low dose of EPA with minimal anti-cachectic activity was chosen to evaluate any potential synergistic effect with curcumin or GTE.
View Article and Find Full Text PDFBr J Cancer
August 2014
Department of Nutritional Biomedicine, School of Life and Health Sciences, Aston University, Birmingham B4 7ET, UK.
Background: Cachexia in both mice and humans is associated with tumour production of a sulphated glycoprotein called proteolysis-inducing factor (PIF). In mice PIF binds with high affinity to a surface receptor in skeletal muscle, but little is known about the human receptor. This study compares the human PIF receptor with the murine.
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