Uncoupling protein 2 (UCP2) is a proton transporter located in the inner mitochondrial membrane, and inhibits the formation of adenosine triphosphate and reactive oxygen species by uncoupling oxidative phosphorylation...Uncoupling protein 2 (UCP2) is a proton transporter located in the inner mitochondrial membrane, and inhibits the formation of adenosine triphosphate and reactive oxygen species by uncoupling oxidative phosphorylation. To provide a theoretical basis for the role of SiUCP2 in lipid metabolism, a 2 341-bp full-length cDNA of SiUCP2 from sea urchin Strongylocentrotus intermedius , which encodes 323 amino acids (predicted MW 36.11 kDa) was obtained, and the structure and function of the SiUCP2 gene and its expression at the mRNA and protein level were studied. SiUCP2 had high homology with UCP2 of other species. Expression of SiUCP2 was detected in the order of tube feet > gonads > coelomocytes > intestines. The expression level was the highest in prismatic larvae and lowest in the two-cell stage. Moreover, using in-situ hybridization, we found that SiUCP2 protein was expressed in the gonads and intestine. This study provided a theoretical basis for subsequent studies on the role of SiUCP2 and its regulatory mechanism in lipid metabolism, and for the improvement of gonad quality to obtain a higher economic value from sea urchins.展开更多
基金Supported by the National Key Research and Development Program of China(No.2018YFD0901601)Chinese Outstanding Talents in Agricultural Sciences(for Yaqing CHANG)。
文摘Uncoupling protein 2 (UCP2) is a proton transporter located in the inner mitochondrial membrane, and inhibits the formation of adenosine triphosphate and reactive oxygen species by uncoupling oxidative phosphorylation. To provide a theoretical basis for the role of SiUCP2 in lipid metabolism, a 2 341-bp full-length cDNA of SiUCP2 from sea urchin Strongylocentrotus intermedius , which encodes 323 amino acids (predicted MW 36.11 kDa) was obtained, and the structure and function of the SiUCP2 gene and its expression at the mRNA and protein level were studied. SiUCP2 had high homology with UCP2 of other species. Expression of SiUCP2 was detected in the order of tube feet > gonads > coelomocytes > intestines. The expression level was the highest in prismatic larvae and lowest in the two-cell stage. Moreover, using in-situ hybridization, we found that SiUCP2 protein was expressed in the gonads and intestine. This study provided a theoretical basis for subsequent studies on the role of SiUCP2 and its regulatory mechanism in lipid metabolism, and for the improvement of gonad quality to obtain a higher economic value from sea urchins.
