Cloning of porcine chemerin, ChemR23 and GPR1 and their involvement in regulation of lipogenesis
1
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
Chemerin is a novel adipokine which is abundant in adipose tissue to promote adipocyte differentiation and with significant relativity to BMI and insulin sensitivity. We report here the molecular characterization of porcine chemerin and its receptors ChemR23 and GPR1, as well as their transcriptional regulation during lipogenesis. Chemerin was mainly expressed in liver, intestine, kidney and adipose tissue, consistent with the expression pattern of GPR1, but not ChemR23, which was predominantly present in spleen and temperately in adipose tissue. We further investigated the lipogenesis-related transcriptional activation of PPARγ and KLF15 on chemerin and its receptors. The data showed that KLF15, but not PPARγ, can up-regulate the mRNA level of chemerin, ChemR23 and GPR1, which was consistent with the results of luciferase assay that confirmed the effect of KLF15 on ChemR23 promoter. Taken together, our data provide basic molecular information for the further investigation on the function of chemerin in lipogenesis.
Abstract
Chemerin is a novel adipokine which is abundant in adipose tissue to promote adipocyte differentiation and with significant relativity to BMI and insulin sensitivity. We report here the molecular characterization of porcine chemerin and its receptors ChemR23 and GPR1, as well as their transcriptional regulation during lipogenesis. Chemerin was mainly expressed in liver, intestine, kidney and adipose tissue, consistent with the expression pattern of GPR1, but not ChemR23, which was predominantly present in spleen and temperately in adipose tissue. We further investigated the lipogenesis-related transcriptional activation of PPARγ and KLF15 on chemerin and its receptors. The data showed that KLF15, but not PPARγ, can up-regulate the mRNA level of chemerin, ChemR23 and GPR1, which was consistent with the results of luciferase assay that confirmed the effect of KLF15 on ChemR23 promoter. Taken together, our data provide basic molecular information for the further investigation on the function of chemerin in lipogenesis.
참고문헌 (27)
- Hotamisligil, G. S., "Inflammation and metabolic disorders", Nature, 444, pp.860~867 (2006)
- Trujillo, M. E., "Adipose tissue-derived factors: impact on health and disease", Endocr. Rev., 27, pp.762~778 (2006)
- Nagpal, S., "Tazarotene-induced gene 2 (TIG2), a novel retinoid-responsive gene in skin", J. Invest. Dermatol., 109, pp.91~95 (1997)
- Parolini, S., "The role of chemerin in the colocalization of NK and dendritic cell subsets into inflamed tissues", Blood, 109, pp.3625~3632 (2007)
- Wittamer, V., "Specific recruitment of antigen-presenting cells by chemerin, a novel processed ligand from human inflammatory fluids", J. Exp. Med., 198, pp.977~985 (2003)
- Wittamer, V., "Neutrophil-mediated maturation of chemerin: a link between innate and adaptive immunity", J. Immunol., 175, pp.487~493 (2005)
- Zabel, B. A., "Chemerin activation by serine proteases of the coagulation, fibrinolytic, and inflammatory cascades", J. Biol. Chem., 280, pp.34661~34666 (2005)
- Guillabert, A., "Role of neutrophil proteinase 3 and mast cell chymase in chemerin proteolytic regulation", J. Leukoc. Biol., 84, pp.1530~1538 (2008)
- Cash, J. L., "Synthetic chemerin-derived peptides suppress inflammation through ChemR23", J. Exp. Med., 205, pp.767~775 (2008)
- Bozaoglu, K., "Chemerin is a novel adipokine associated with obesity and metabolic syndrome", Endocrinology, 148, pp.4687~4694 (2007)
- Lehrke, M., "Chemerin is associated with markers of inflammation and components of the metabolic syndrome but does not predict coronary atherosclerosis", Eur. J. Endocrinol., 161, pp.339~344 (2009)
- Weigert, J., "Systemic chemerin is related to inflammation rather than obesity in type 2 diabetes", Clin. Endocrinol. (Oxf), 72, pp.342~348 (2009)
- Roh, S. G., "Chemerin--a new adipokine that modulates adipogenesis via its own receptor", Biochem. Biophys. Res. Commun., 362, pp.1013~1018 (2007)
- Goralski, K. B., "Chemerin, a novel adipokine that regulates adipogenesis and adipocyte metabolism", J. Biol. Chem., 282, pp.28175~28188 (2007)
- Takahashi, M., "Chemerin enhances insulin signaling and potentiates insulin-stimulated glucose uptake in 3T3-L1 adipocytes", FEBS Lett., 582, pp.573~578 (2008)
- Sell, H., "Chemerin is a novel adipocyte-derived factor inducing insulin resistance in primary human skeletal muscle cells", Diabetes, 58, pp.2731~2740 (2009)
- Zabel, B. A., "Mast cell-expressed orphan receptor CCRL2 binds chemerin and is required for optimal induction of IgE-mediated passive cutaneous anaphylaxis", J. Exp. Med., 205, pp.2207~2220 (2008)
- Barnea, G., "The genetic design of signaling cascades to record receptor activation", Proc. Natl. Acad. Sci. U.S.A., 통권 : 105, pp.64~69 (2008)
- Zabel, B. A., "Chemoattractants, extracellular proteases, and the integrated host defense response", Exp. Hematol., 34, pp.1021~1032 (2006)
- Pease, J. E., "The attraction of chemokines as a target for specific anti-inflammatory therapy", Br. J. Pharmacol., 147(1), pp.S212~S221 (2006)
- Martensson, U. E., "Genomic organization and promoter analysis of the gene encoding the mouse chemoattractant-like receptor, CMKLR1", Gene, 328, pp.167~176 (2004)
- Otteson, D. C., "Zinc-finger domains of the transcriptional repressor KLF15 bind multiple sites in rhodopsin and IRBP promoters including the CRS-1 and G-rich repressor elements", BMC Mol. Biol., 6, pp.15~ (2005)
- Wittamer, V., "The C-terminal nonapeptide of mature chemerin activates the chemerin receptor with low nanomolar potency", J. Biol. Chem., 279, pp.9956~9962 (2004)
- Mori, T., "Role of Kruppel-like factor 15 (KLF15) in transcriptional regulation of adipogenesis", J. Biol. Chem., 280, pp.12867~12875 (2005)
- Muruganandan, S., "Role of Chemerin", CMKLR1 Signaling in Adipogenesis and Osteoblastogenesis of Bone Marrow Stem Cells, 2009, pp.25, 222~234
- Yerle, M., "A somatic cell hybrid panel for pig regional gene mapping characterized by molecular cytogenetics", Cytogenet. Cell Genet., 73, pp.194~202 (1996)
- Ramirez-Zacarias, J. L., "Quantitation of adipose conversion and triglycerides by staining intracytoplasmic lipids with Oil red O", Histochemistry, 97, pp.493~497 (1992)
