• Journal of Mushroom
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• v.7 no.1
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• pp.9-21
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• 2009

This study was executed in an attempt to investigate a artificial requisites of fruitbody occurrence. Environmental requirements on habitat for fruitbody occurrence of collected cultures resulted in leading to $13-16^{\circ}C$ and 75% relative humidity, and requiring silt loam of soil texture which had more nutritional substances than a dry field. Optimal temperature was $25^{\circ}C$, medium PDB, and pH 5.0 in cultural conditions. Mannose required of 5% in ASI 59002, 59003, 59004, but 3% in ASI 59001 was selected as optimum carbon source. The substrates stimulating sclerotium formation were cotton waste, or cotton waste + oak sawdust (mixture ratio of 8:2), which had 20% additive of wheat barn respectively. Sclerotium was formed well in the substrate adjusted chemical properties by applying 2% of calcium sulfate. Sclerotium formation was the most effective in the treatment of peat moss + oak sawdust (mixture ratio of 5:5) + 30% of wheat barn.

• Journal of Acupuncture Research
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• v.22 no.2
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• pp.55-70
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• 2005

Objective: Ulmus davidiana Planch (Ulmaceae) has long been known to have anti-inflammnatory in the traditional Korean medicine. UD has been reported as a good enhancer for bone healing. Methods : In this experiment, we investigate the Inhibitory effects of UD on bone resorption using the bone cells culture. Different concentrations of crude extract of UD were added to mouse bone cells culture. The mitochondria activity of the bone cells after exposure was determined by colorimetric MIT assay. It was demonstrated that UD has potential effects on bone cells culture without any cytotoxicity. The most effective concentration of UD on bone cells were $100\;{\mu}g/ml$. Cathepsin K (Cat K) is the major cysteine protease expressed in osteoclasts and is thought to play a key role in matrix degradation during bone resorption. Results : When mouse long bone cells including osteoclasts and osteoblast were treated with the PI3-Kinase inhibitor, wortmannin (WT), WT prevented the osteoclast-mediated intracellular processing of Cat K. Similarly, treatment of osteoclasts-containing long bone cells with UD extracts prevented the intracellular maturation of Cat K, suggesting that UD may disrupt the intracellular trafficking of pro Cat K. This is similar to that of WT. Since secreted proenzymes have the potential to reenter the cell via mannose-6-phosphate (M6P) receptor, to prevent this possibility, we tested WT and UD in the absence or presence of M6P. Inhibition of Cat K processing by WT or UD was observed in a dose-dependent manner. Furthermore, the addition of M6P resulted in enhanced potency of WT and UD. Conclusion : UD dose-dependently inhibited in vitro bone resorption with a potency similar to that observed for inhibition of Cat K processing.

• Reproductive and Developmental Biology
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• v.32 no.1
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• pp.65-70
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• 2008

Members of the Vps (Vacuolar protein sorting) protein family involved in the formation of the retromer complex have been discovered in a variety of species such as yeast, mouse, and human. A mammalian retromer complex is composed of Vps26, Vps29, and Vps35 proteins and plays and important role in cation-independent mannose-6-phosphate receptor retrieval from the endosome to the trans-Golgi network. In this study, we have identified the full-length sequences of the retromer components of Vps26, Vps29, and Vps35 in micro pigs. The cDNA sequences of these retromer components have been determined and the result showed there is 99% homology among the component counterparts from mouse, micro pigs, and humans. In addition, the retromer complexes formed with hetero-components were found in the brain of micro pigs. Based on above results, we suggest mammalian Vps components are well conserved in micro pigs.

• Korean Journal of Food Science and Technology
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• v.8 no.1
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• pp.33-41
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• 1976

These experiment were conducted to investigate the cultural condition of the lipase production by Rhizopus japonicus. The results obtained were as follows: 1. Soybean meal and ammonium sulfate were the most effective in the lipase production as organic and inorganic nitrogen sources, respectively. 2. The lipase production was strongly inhibited, when added as carbon sources xylose, glucose, fructose, galactose, maltose, soluble starch, and dextrin causing the lowering of pH of the medium during culture. Sucrose did not inhibit the lipase production, but not caused any effect when added. 3. $K_2HPO_4$ as phosphate salt and $MgSO_4{\cdot}7H_2O$ as magnesium salt were the most effective in the lipase production. 4. The addition of olive oil, soybean oil, and coconut oil respectively increased the enzyme production and especially 1% olive oil increased it by 50%. 5. The enzyme production increased slightly on the addition of yeast extract to $0.05{\sim}0.07%$. 6. The optimum composition of the medium for the lipase production by Rhizopus japonicus was in the composition of soybean meal 2%; $K_2HPO_4{\cdot}$ 0.5%; $(NH_4)_2SO_4$ 0.1%; $MgSO_4\;7H_2O$ 0.05%; yeast extract 0.05%; olive oil 1%. The maximum production of the lipase was attained by the incubation far 48hrs under the optimum incubation condition.

• Clinical and Experimental Reproductive Medicine
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• v.23 no.3
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• pp.247-268
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• 1996

It has been known for a long time that gonadotropins and steroid hormones play a pivotal role in a series of reproductive biological phenomena including the maturation of ovarian follicles and oocytes, ovulation and implantation, maintenance of pregnancy and fetal growth & development, parturition and mammary development and lactation. Recent investigations, however, have elucidated that in addition to these classic hormones, multiple growth factors also are involved in these phenomena. Most growth factors in reproductive organs mediate the actions of gonadotropins and steroid hormones or synergize with them in an autocrine/paracrine manner. The insulin-like growth factor(IGF) system, which is one of the most actively investigated areas lately in the reproductive organs, has been found to have important roles in a wide gamut of reproductive phenomena. In the present communication, published literature pertaining to the intrauterine IGF system will be reviewed preceded by general information of the IGF system. The IGF family comprises of IGF-I & IGF-II ligands, two types of IGF receptors and six classes of IGF-binding proteins(IGFBPs) that are known to date. IGF-I and IGF-II peptides, which are structurally homologous to proinsulin, possess the insulin-like activity including the stimulatory effect of glucose and amino acid transport. Besides, IGFs as mitogens stimulate cell division, and also play a role in cellular differentiation and functions in a variety of cell lines. IGFs are expressed mainly in the liver and messenchymal cells, and act on almost all types of tissues in an autocrine/paracrine as well as endocrine mode. There are two types of IGF receptors. Type I IGF receptors, which are tyrosine kinase receptors having high-affinity for IGF-I and IGF-II, mediate almost all the IGF actions that are described above. Type II IGF receptors or IGF-II/mannose-6-phosphate receptors have two distinct binding sites; the IGF-II binding site exhibits a high affinity only for IGF-II. The principal role of the type II IGF receptor is to destroy IGF-II by targeting the ligand to the lysosome. IGFs in biological fluids are mostly bound to IGFBP. IGFBPs, in general, are IGF storage/carrier proteins or modulators of IGF actions; however, as for distinct roles for individual IGFBPs, only limited information is available. IGFBPs inhibit IGF actions under most in vitro situations, seemingly because affinities of IGFBPs for IGFs are greater than those of IGF receptors. How IGF is released from IGFBP to reach IGF receptors is not known; however, various IGFBP protease activities that are present in blood and interstitial fluids are believed to play an important role in the process of IGF release from the IGFBP. According to latest reports, there is evidence that under certain in vitro circumstances, IGFBP-1, -3, -5 have their own biological activities independent of the IGF. This may add another dimension of complexity of the already complicated IGF system. Messenger ribonucleic acids and proteins of the IGF family members are expressed in the uterine tissue and conceptus of the primates, rodents and farm animals to play important roles in growth and development of the uterus and fetus. Expression of the uterine IGF system is regulated by gonadal hormones and local regulatory substances with temporal and spatial specificities. Locally expressed IGFs and IGFBPs act on the uterine tissue in an autocrine/paracrine manner, or are secreted into the uterine lumen to participate in conceptus growth and development. Conceptus also expresses the IGF system beginning from the peri-implantation period. When an IGF family member is expressed in the conceptus, however, is determined by the presence or absence of maternally inherited mRNAs, genetic programming of the conceptus itself and an interaction with the maternal tissue. The site of IGF action also follows temporal (physiological status) and spatial specificities. These facts that expression of the IGF system is temporally and spatially regulated support indirectly a hypothesis that IGFs play a role in conceptus growth and development. Uterine and conceptus-derived IGFs stimulate cell division and differentiation, glucose and amino acid transport, general protein synthesis and the biosynthesis of mammotropic hormones including placental lactogen and prolactin, and also play a role in steroidogenesis. The suggested role for IGFs in conceptus growth and development has been proven by the result of IGF-I, IGF-II or IGF receptor gene disruption(targeting) of murine embryos by the homologous recombination technique. Mice carrying a null mutation for IGF-I and/or IGF-II or type I IGF receptor undergo delayed prenatal and postnatal growth and development with 30-60% normal weights at birth. Moreover, mice lacking the type I IGF receptor or IGF-I plus IGF-II die soon after birth. Intrauterine IGFBPs generally are believed to sequester IGF ligands within the uterus or to play a role of negative regulators of IGF actions by inhibiting IGF binding to cognate receptors. However, when it is taken into account that IGFBP-1 is expressed and secreted in primate uteri in amounts assessedly far exceeding those of local IGFs and that IGFBP-1 is one of the major secretory proteins of the primate decidua, the possibility that this IGFBP may have its own biological activity independent of IGF cannot be excluded. Evidently, elucidating the exact role of each IGFBP is an essential step into understanding the whole IGF system. As such, further research in this area is awaited with a lot of anticipation and attention.

• Journal of The Korean Society of Inherited Metabolic disease
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• v.5 no.1
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• pp.65-75
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• 2005

Purpose: To understand genetic differences and similarities between mucolipidosis and control. Methods: Using the fibroblast of the mucolipidosis II and control, forward and reverse subtracted libraries were constructed. Among these clones, we investigated mutations in the GNPTA (MGC4170) gene, which codes for the ${\alpha}/{\beta}$ subunits of phosphotransferase, and in the GNPTAG gene, which codes for the ${\gamma}$ subunits in 5 Korean patients with mucolipidosis type II or IIIA. Result: Several differentially expressed cDNAs were cloned and their sequences were determined. Mutation analysis of the interested gene, GNPTA was performed and we identified 7 mutations in the GNPTA gene, but none in the GNPTAG gene. The mutations in type II patients included p.Q104X(c.310C>T), p.R1189X(c.3565C>T), p.S1058X(c.3173C>G), p.W894X(c.2681G>A) and p.H1158fsX15(c.3474_3475delTA), all of which are non-sense or frame shift mutations. However, a splicing site mutation, IVS13+1G>A (c.2715+1G>A) was detected along with a non-sense or a frame shift mutation (p.R1189X or p.E858fsX3(c.2574_2575delGA)) in two mucolipidosis type IIIA patients. Conclusion: This report shows that mutations in the GNPTA gene coding for the ${\alpha}{\beta}$subunits of phosphotransferase, and not mutations in the GNPTAG gene, account for most of mutations found in Korean patients with mucolipidosis type II or IIIA.