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Complement C1q Tumor Necrosis Factor-Related Protein 5 (CTRP5)

CTRP5 is a member of the C1q and tumor necrosis factor superfamily whose structure resembles adiponectin, being a 25 kD secretory protein. CTRP5 was identified in a cDNA library enriched for genes showing expression specific for the retinal pigment epithelium (RPE). A subsequent RT-PCR study demonstrated CTRP5 expression in RPE, liver, lung, placenta, and brain. It has been proposed that a CTRP mutation (S163R) plays a critical role in affecting its higher order protein structure, potentially leading to a cause of abnormal adhesion between the RPE and Bruch membrane. A recent data showed that CTRP is one of the genes highly induced by elimination of mitochondria and was able to activate AMPK in a rat myotube cell line, L6. Stimulation of L6 with recombinant CTRP5, full length as well as globular domain, enhanced glucose uptake and fatty acid oxidation. These biochemical events did not seem to be mediated via AdipoR1 or AdipoR2, suggesting that a novel receptor(s) may exist for CTRP5 in this muscle cell line. Some CTRP members can physically interact with adiponectin, forming various multimeric structures. A compensatory upregulation of mouse CTRP members was observed in adiponectin-deficient mice. Therefore, measuring serum or plasma CTRP5 may provide important information on its involvement in novel metabolism.

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