• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.5
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• pp.864-868
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• 2004

Iron is an essential ingredient for all metabolism in a living body However, because of the very low content of the iron in foods, many researches have been performed about iron-fortified food additives. We developed an iron-fortified food additive using the liposome that contain ferrous sulfate and hemin. For preventing the autoxidation of the ferrous sulfate, ascorbic acid was applied. Also, to prevent the oxidation of the liposome induced by the added ferrous sulfate and/or hemin, $\alpha$ -tocopherol was additionally applied. Though the effect of the added aqueous ascorbic acid did not show the antioxidative activity on the liposome containing ferrous sulfate and/or hemin, the added $\alpha$ -tocopherol in the phospholipid bilayer could retard the oxidation of the liposome. These results support that the liposome containing ferrous sulfate, hemin and ascorbic acid with the incorporated $\alpha$ -tocopherol could be applied in the food industry as an iron-fortified additive.

• Journal of Dental Rehabilitation and Applied Science
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• v.37 no.1
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• pp.31-38
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• 2021

Purpose: The purpose of this study was to investigate effect of heme on periodontopathogens. Materials and Methods: The experiment was performed using 7 types of anaerobic bacteria present in the periodontal pocket. The bacteria were cultured using suitable medium in an anaerobic condition with or without hemin, and the growth of the bacteria was measured every 6 hours by a spectrophotometer. Results: the growth of Porphyromonas gingivalis was different only by the presence or absence of hemin. The growth of other periodontopathogens except Treponema denticola was different in a hemin concentration-dependent manner. The growth of T. denticola was interfered by hemin. Conclusion: Heme may be a factor that leads dysbiosis in the microbial ecosystem of the subgingival plaque and thereby promote a periodontitis-causing environment.

• Journal of Veterinary Science
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• v.23 no.5
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• pp.74.1-74.16
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• 2022

Background: Previous studies have presented evidence to support the significant association between red meat intake and colon cancer, suggesting that heme iron plays a key role in colon carcinogenesis. Epigallocatechin-3-gallate (EGCG), the major constituent of green tea, exhibits anti-oxidative and anti-cancer effects. However, the effect of EGCG on red meat-associated colon carcinogenesis is not well understood. Objectives: We aimed to investigate the regulatory effects of hemin and EGCG on colon carcinogenesis and the underlying mechanism of action. Methods: Hemin and EGCG were treated in Caco2 cells to perform the water-soluble tetrazolium salt-1 assay, lactate dehydrogenase release assay, reactive oxygen species (ROS) detection assay, real-time quantitative polymerase chain reaction and western blot. We investigated the regulatory effects of hemin and EGCG on an azoxymethane (AOM) and dextran sodium sulfate (DSS)-induced colon carcinogenesis mouse model. Results: In Caco2 cells, hemin increased cell proliferation and the expression of cell cycle regulatory proteins, and ROS levels. EGCG suppressed hemin-induced cell proliferation and cell cycle regulatory protein expression as well as mitochondrial ROS accumulation. Hemin increased nuclear factor erythroid-2-related factor 2 (Nrf2) expression, but decreased Keap1 expression. EGCG enhanced hemin-induced Nrf2 and antioxidant gene expression. Nrf2 inhibitor reversed EGCG reduced cell proliferation and cell cycle regulatory protein expression. In AOM/DSS mice, hemin treatment induced hyperplastic changes in colon tissues, inhibited by EGCG supplementation. EGCG reduced the hemin-induced numbers of total aberrant crypts and malondialdehyde concentration in the AOM/DSS model. Conclusions: We demonstrated that EGCG reduced hemin-induced proliferation and colon carcinogenesis through Nrf2-inhibited mitochondrial ROS accumulation.

• Microbiology and Biotechnology Letters
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• v.49 no.1
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• pp.57-64
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• 2021

Lactic acid bacteria (LAB), belonging to the Firmicutes phylum, lack heme biosynthesis and, thus, are characterized as fermentative and catalase-negative organisms. To verify the hypothesis that heme-rich-nutrients might compensate the heme-biosynthesis incapability of non-respiratory LAB in animal gut, a heme-rich-nutrient was fed to a dog and its fecal microbiome was analyzed. Firmicutes abundance in the feces from the heme-rich-nutrient-fed dog was 99%, compared to 92% in the control dog. To clarify the reason of increased Firmicutes abundance in the feces from the heme-rich-nutrient-fed dog, Lacobacillus gasseri were used as model anerobic LAB to study a purified heme (hemin). The anaerobic growth of L. gasseri in the medium with 25 µM hemin supplementation was faster than that in the medium without hemin, while the growth in the 50 µM hemin-supplemented medium did not vary. Cellular activities of the cytochrome bd complex were 1.55 ± 0.19, 2.11 ± 0.14, and 2.20 ± 0.08 U/gcell in the cells from 0, 25, and 50 µM hemin-supplemented medium, while intracellular ATP concentrations were 7.90 ± 1.12, 11.95 ± 0.68, and 12.56 ± 0.58 µmol_ATP/g_cell, respectively. The ROS-scavenging activities of the L. gasseri cytosol from 25 µM and 50 µM hemin-supplemented medium were 68% and 82% greater than those of the cytosol from no hemin supplemented-medium, respectively. These findings indicate that external hemin could compensate the heme-biosynthesis incapability of L. gasseri by increasing the cytosolic ROS-scavenging and extra ATP generation, possibly through increasing the electron transfer. Increase in the number of anaerobic bacteria in heme-rich-nutrient-fed animal gut is discussed based on the results.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.7
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• pp.1120-1126
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• 2007

An iron-fortified whey protein concentrate (Fe-WPC) was prepared by addition of ferric chloride to concentrated whey. A large part of the iron in the Fe-WPC existed as complexes with proteins such as ${\beta}$-lactoglobulin. The bioavailability of iron from Fe-WPC was evaluated using iron-deficient rats, in comparison with heme iron. Rats were separated into a control group and an iron-deficiency group. Rats in the control group were given the standard diet containing ferrous sulfate as the source of iron throughout the experimental feeding period. Rats in the iron-deficiency group were made anemic by feeding on an Fe-deficient diet without any added iron for 3 wk. After the iron-deficiency period, the iron-deficiency group was separated into an Fe-WPC group and a heme iron group fed Fe-WPC and hemin as the sole source of iron, respectively. The hemoglobin content, iron content in liver, hemoglobin regeneration efficiency (HRE) and apparent iron absorption rate were examined when iron-deficient rats were fed either Fe-WPC or hemin as the sole source of iron for 20 d. Hemoglobin content was significantly higher in the rats fed the Fe-WPC diet than in rats fed the hemin diet. HRE in rats fed the Fe-WPC diet was significantly higher than in rats fed the hemin diet. The apparent iron absorption rate in rats fed the Fe-WPC diet tended to be higher than in rats fed the hemin diet (p = 0.054). The solubility of iron in the small intestine of rats at 2.5 h after ingestion of the Fe-WPC diet was approximately twice that of rats fed the hemin diet. These results indicated that the iron bioavailability of Fe-WPC was higher than that of hemin, which seemed due, in part, to the different iron solubility in the intestine.

• Biomedical Science Letters
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• v.11 no.3
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• pp.349-353
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• 2005

The globin in cytosol receives the heme in mitochondria and folds to the hemoglobin within erythrocyte. Two mechanisms have been proposed that the heme was transfered post-translationally or cotranslationally to the globin. In this research, how the globin in cytosol receives post-translationally the heme from membranes was studied according to pH and phospholipid composition. Globins dissolved in various pH buffer solutions $(PH\;3\~7)$ were rapidly added into the bulk of egg phosphatidylcholine $100\%\;or\;60\%$ liposomes containing hemin in pH 7 buffer solution. Hemin was very highly transferred to globin at pH 4 and 6. Also, hemin was more efficiently transfered to globin in egg phosphatidylcholine $100\%$ than in $60\%$ liposomes.

• Archives of Pharmacal Research
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• v.25 no.3
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• pp.343-348
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• 2002

Carbon monoxide (CO) are produced by heme oxygenase (HO), and HO was detected in hypothalamus. However, the roles of CO produced in hypothalamus was not fully elucidated. So, we tested the effects of CO on body temperature because preoptic-anterior hypothalamus was known as the presumptive primary fever-producing site. CO-saturated aCSF ($4{\;}{\mu}l$, i.c.v.) and hemin ($10{\;}{\mu}g$, i.c.v.) elicited marked febrile response. Pretreatment with indomethacin completely inhibited CO- and hemin-induced fever. Zinc protoporphyrin-IX ($10{\;}{\mu}g$, i.c.v.) or ODQ ($50{\;}{\mu}g$, i.c.v.) partially reduced hemin-induced febrile response. Dibutyryl-cGMP ($100{\;}{\mu}g$, i.c.v.) produced profound febrile response and this febrile response was attenuated by indomethacin. These results indicate that endogenous CO may have a role as a pyrogenic mediator in CNS and CO-mediated pyresis is dependent on prostaglandin production and partially on activation of soluble guanylate cyclase.

• Bulletin of the Korean Chemical Society
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• v.7 no.2
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• pp.155-157
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• 1986

• Archives of Pharmacal Research
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• v.28 no.8
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• pp.963-969
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• 2005

Many reports have stated that some of the pathogenic bacteria can obtain iron from ferroproteins, such as cytochrome C, ferritin, hemin, hemoglobin, and myoglobin. These reports prompted us to determine if an opportunistic pathogenic fungus, Candida albicans, can utilize ferroproteins to circumvent the iron-regulatory effect of transferrin. The following assays were carried out to measure in vitro growth stimulation by the ferroproteins: as an initial step, C. albicans was cultured in iron-free (pretreated with apotransferrin for 24h) culture medium. Once Candida albicans yeast cell growth reached stasis from iron starvation, individual ferroproteins were added to the culture media. Results showed that hemin, hemoglobin, and myoglobin supported a partial growth recovery. Additional studies with haptoglobin, a serum protein that interacts with the globin moiety of certain ferroproteins, established that C. albicans could obtain iron from the haptoglobin-ferroprotein complexes. These data indicate that the heme part of the ferroproteins is the source of iron. This implies that heme oxygenase, CaHMX1 might be involved in bringing about dissociation of heme-containing protein for iron-acquisition. In addition, anticandidal activity of transferrin takes place not only by the process of iron regulation, but also by direct interaction with the yeast cells.

• 대한치주과학회:학술대회논문집
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• 2002.11a
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• pp.87-87
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• 2002