Abnormal fat accumulation with gut microbiota dysbiosis results in hepatic inflammation by upregulating the release of lipopolysaccharide (LPS) and inflammatory cytokine. Gochujang, a traditional fermented condiment, has beneficial effects, such as anti-colonic inflammatory effects. However, Gochujang has been controversial because of its high salt content (the Korean Paradox). Thus, the present study aimed to investigate the preventative effects of Gochujang on hepatic inflammation and related gut microbiota through discussing the Korean Paradox. The mice were divided into groups including a normal diet (ND), high-fat diet (HD), HD with salt (SALT), HD with a high percentage of beneficial microbiota Gochujang (HBM), and HD with diverse beneficial microbiota Gochujang (DBM). Gochujang markedly reduced lipid accumulation, hepatic injury, and inflammation response. Furthermore, Gochujang attenuated protein expression involved in the JNK/IκB/NF-κB pathway. Additionally, Gochujang regulated the gut microbiota-derived LPS production and Firmicutes/Bacteroidetes ratio. Gochujang regulated the levels of gut microbiota such as Bacteroides, Muribaculum, Lactobacillus, and Enterorhabdus, which were correlated with hepatic inflammation. Salt did not have foregoing effects, meaning that the salt content in Gochujang did not affect its anti-inflammatory effect. In conclusion, Gochujang showed anti-hepatic inflammation effects via reduced lipid accumulation, hepatic injury, and inflammatory response together with reorganization of gut microbiota dysbiosis regardless of salt content and the difference of micro bacteria composition.

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In all mammalian species, progesterone is essential in the preparation for and maintenance of pregnancy, if it occurs. Progesterone primes the endometrium for possible implantation and inhibits uterine contraction until birth. Aldo‐keto reductases (AKRs) belong to a superfamily of NADPH‐dependent reductases that act on a wide range of substrates, including simple carbohydrates, steroid hormones, and endogenous prostaglandins. 20‐alpha hydroxysteroid dehydrogenase (20α‐HSD; EC.1.1.1.149) enzyme belongs to the family of aldo‐keto reductases. 20α‐HSD predominantly converts progesterone into its biologically inactive form 20α‐hydroxyprogesterone (20α‐OHP), and plays a crucial role in the termination of pregnancy and initiation of parturition. We have been reporting on the molecular characterizations of placental and ovarian 20α‐HSD in the bovine, pig, deer and monkey.In this study, to understand the fundamental function of monkey 20α‐HSD, we created transgenic mice expressing EGFP gene under monkey 20α‐HSD promoter. The EGFP protein was expressed in the placenta and ovary of tg mice during pregnancy. Now, we are trying to elucidate the function by PGF2α, Prolactin, Oxytocin. (Eun‐Bi Seo and Chae‐Won Park were supported by a scholarship from the BK21 Plus Program (31Z20130012928). the Ministry of Education, Science and Technology, korea)

The glycoprotein hormone family consists of luteinizing hormone (LH), follicle‐stimulating hormone (FSH), and thyroid‐stimulating hormone (TSH), which are secreted by the pituitary gland in all mammalian species, and chorionic gonadotropin (CG), which is secreted by placental trophoblast cells in primates and equids. These hormones consists of non‐covalently associated α and β subunits. Within a species, the amino acid sequence of the α subunit is identical across all glycoprotein hormones and is encoded by a single gene. The αβ dimer is the active form of the hormone, and biological specificity is conferred by the β subunit. Also in fish, the duality of gonadotropin hormone (GTH), GTH‐1 (FSH‐like GTH), and GTH‐II (LH‐like GTH) is found in certain teleost. In this study, in order to understand the fundamental mechanisms involved in teleost reproduction and to proved a broader basis for comparative studt of teleost GTHs, we isolated a cDNA encoding the α and β subunit of GHT‐1 from eel and produced it's recombinant protein from E.coli and CHO cells. To obtain tethered eelFSH, the cDNA encoding the full‐length eel FSH β‐subunit (signal sequence of 22 amino acid residues and the mature protein of 105 amino acid residues) was fused with the mature protein (93 amino acids) of the α‐subunit by overlapping PCR mutagenesis. Subsequently, PCR fragement was inserted into the pCR2.1 clon ing vector and sequenced. After then, it was digested with the EcoRI and SalI enzymes and ligated into the eukaryotic expression vector pcDNA3. The gene was completely sequenced to confirm the presence of the Kozak site and, myc‐tag and to role out the possibility of any PCR erros. Eel FSH protein was expressed in the E. coli system using the pREST expression plasmid vector, and the protein was purified by NI‐NTA column. Eel FSH protein was detected at the predicted molecular weight of 24.3 kDa by SDS‐PAGE in E.coli and 32‐45 kDa in CHO cell lines. Grant Funding Source: This work was supported by NFRDI