9 results on '"Yong Pyo Shin"'
Search Results
2. Antiseptic effect of antimicrobial peptide psacotheasin 2 derived from the yellow-spotted longicorn beetle (Psacothea hilaris)
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Minhee Baek, Joon Ha Lee, Ra-Yeong Choi, Seong Hyun Kim, Mi-Ae Kim, Yong Pyo Shin, Hwa Jeong Lee, Jae Sam Hwang, In-Woo Kim, and Minchul Seo
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0301 basic medicine ,Lipopolysaccharide ,medicine.drug_class ,Immunology ,Antibiotics ,Antimicrobial peptides ,Nitric Oxide Synthase Type II ,Psacothea hilaris ,Microbiology ,Nitric oxide ,Mice ,03 medical and health sciences ,chemistry.chemical_compound ,Antiseptic ,Sepsis ,medicine ,Animals ,Bacteria ,030102 biochemistry & molecular biology ,biology ,NF-kappa B ,Antimicrobial ,Immunity, Innate ,Coleoptera ,Nitric oxide synthase ,RAW 264.7 Cells ,030104 developmental biology ,chemistry ,Cyclooxygenase 2 ,biology.protein ,Cytokines ,Inflammation Mediators ,Peptides ,Antimicrobial Peptides ,Signal Transduction ,Developmental Biology - Abstract
Given the challenges posed by antibiotic resistant microbes and the high mortality rate associated with sepsis, there is an urgent need to develop novel peptide antibiotics that exhibit both antimicrobial and anti-inflammatory activities. Herein, we evaluated antimicrobial activity and anti-inflammatory activity of psacotheasin 2, one of the antimicrobial peptide candidates identified previously using an in silico analysis on the transcriptome of Psacothea hilaris. In addition to exhibiting antimicrobial activities against microorganisms without inducing hemolysis, psacotheasin 2 also decreased the nitric oxide production in lipopolysaccharide (LPS)-induced Raw264.7 cells. Moreover, ELISA and western blot analysis revealed that psacotheasin 2 reduced the expression levels of pro-inflammatory enzymes such as inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2). Further, we found that psacotheasin 2 markedly reduced the expression levels of pro-inflammatory cytokines (IL-6 and IL-1β) by regulating mitogen-activated protein kinases (MAPKs) and nuclear factor-kB (NF-kB) signaling in LPS-induced Raw264.7 cells. We also confirmed that the binding of psacotheasin 2 to bacterial cell membranes occurs via a specific interaction with LPS. In mouse models of LPS-induced shock, psacotheasin 2 significantly enhanced the survival rate and recovered weight by attenuating pro-inflammatory cytokines. Thus, psacotheasin 2 could be a promising candidate as a peptide antiseptic agent.
- Published
- 2021
3. De novo assembly and functional annotation of the Red-striped golden stink bug (Poecilocoris lewisi) transcriptome
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Ra Ham Lee, Seokhyun Lee, Jae Sam Hwang, Joon Ha Lee, Donghyun Shin, Minchul Seo, Yong Pyo Shin, Mi-Ae Kim, In-Woo Kim, and Hak-Kyo Lee
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0301 basic medicine ,media_common.quotation_subject ,Antimicrobial peptides ,Sequence assembly ,Insect ,Biology ,Hemiptera ,Heteroptera ,Transcriptome ,03 medical and health sciences ,0302 clinical medicine ,Genetics ,Animals ,Defensin ,media_common ,Host (biology) ,Gene Expression Profiling ,fungi ,High-Throughput Nucleotide Sequencing ,General Medicine ,Poecilocoris lewisi ,030104 developmental biology ,Functional annotation ,030220 oncology & carcinogenesis - Abstract
Insect antimicrobial peptides (AMPs) have a wide range of functions and potential applications, and have recently attracted attention as alternative foods and medicines for humans. Our study performed transcriptome analysis to explore the potential of the red-striped golden stink bug (Poecilocoris lewisi), and as a result, we have discovered new features of P. lewisi that have not been identified. Specifically, defensin found in P. lewisi is a well-known AMP and is expressed by various plants, animals and fungi for host defense. Moreover, the discovery of defensin in P. lewisi provides new research and important information. In this study, we identified AMP and related DEG in P. lewisi that are closely related to human disease and immune response. These findings will provide the basis and important information for future research on P. lewisi that has not yet been studied.
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- 2021
4. Therapeutic efficacy of halocidin-derived peptide HG1 in a mouse model of Candida albicans oral infection
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Seo Hwa Shin, Hee-Ra Chang, In Hee Lee, Woong Sik Jang, Yong Pyo Shin, Bosung Kim, Young Shin Lee, and Myung Hwa Kim
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Microbiology (medical) ,Saliva ,Antifungal Agents ,Administration, Oral ,Pharmacology ,Microbiology ,Mice ,Pharmacokinetics ,Candidiasis, Oral ,In vivo ,Oral administration ,Candida albicans ,Animals ,Medicine ,Pharmacology (medical) ,Biological Products ,Mice, Inbred ICR ,biology ,business.industry ,Antimicrobial ,biology.organism_classification ,Disease Models, Animal ,Infectious Diseases ,Oral microbiology ,Female ,Peptides ,business ,Ex vivo - Abstract
HG1 is an antimicrobial peptide derived from halocidin, which is naturally found in tunicates. The purpose of this study was to evaluate the therapeutic potential of HG1 as a novel antifungal agent for treating oral candidiasis.The pharmacokinetic properties of HG1 were explored in mice, which were orally administered a single dose of HG1. Anti-Candida activity of HG1 was investigated in a time-dependent manner in the presence of saliva obtained from healthy donors or patients with oral candidiasis. In addition, HG1 was evaluated for its anti-Candida activity in the presence of proteins extracted from the culture supernatant of Candida albicans. The therapeutic potential in vivo and ex vivo of HG1 against oral candidiasis was investigated using a mouse model of oral candidiasis.Our data showed that absorption of HG1 into the blood did not occur following oral administration. In addition, HG1 exerted marked anti-Candida activity after short-term incubation at a concentration of 20 mg/L and it also caused a considerable reduction in fungal burden in the oral candidiasis mouse model when treated with 1 mg or 0.5 mg.This study suggests that HG1, as a novel component of mouthwash, might become an alternative antifungal agent to conventional drugs used to manage oral candidiasis.
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- 2013
5. Immune Evasion of Enterococcus faecalis by an Extracellular Gelatinase That Cleaves C3 and iC3b
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Ho Jin Park, Chong Han Kim, Yeon Sun Seong, Yong Pyo Shin, Byung Sam Kim, Sook Jae Seo, Shin Yong Park, and In Hee Lee
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Blood Bactericidal Activity ,Neutrophils ,Phagocytosis ,Complement Pathway, Alternative ,Guinea Pigs ,Molecular Sequence Data ,Immunology ,Virulence ,Enterococcus faecalis ,Microbiology ,Mice ,Dogs ,Extracellular ,Animals ,Humans ,Immunology and Allergy ,Gelatinase ,Amino Acid Sequence ,Complement Activation ,Opsonin ,Gram-Positive Bacterial Infections ,biology ,Hydrolysis ,Extracellular Fluid ,Complement C3 ,biology.organism_classification ,Complement system ,Gelatinases ,Complement C3b ,iC3b ,Chickens - Abstract
Enterococcus faecalis (Ef) accounts for most cases of enterococcal bacteremia, which is one of the principal causes of nosocomial bloodstream infections (BSI). Among several virulence factors associated with the pathogenesis of Ef, an extracellular gelatinase (GelE) has been known to be the most common factor, although its virulence mechanisms, especially in association with human BSI, have yet to be demonstrated. In this study, we describe the complement resistance mechanism of Ef mediated by GelE. Using purified GelE, we determined that it cleaved the C3 occurring in human serum into a C3b-like molecule, which was inactivated rapidly via reaction with water. This C3 convertase-like activity of GelE was shown to result in a consumption of C3 and thus inhibited the activation of the complement system. Also, GelE was confirmed to degrade an iC3b that was deposited on the Ag surfaces without affecting the bound C3b. This proteolytic effect of GelE against the major complement opsonin resulted in a substantial reduction in Ef phagocytosis by human polymorphonuclear leukocytes. In addition, we verified that the action of GelE against C3, which is a central component of the complement cascade, was human specific. Taken together, it was suggested that GelE may represent a promising molecule for targeting human BSI associated with Ef.
- Published
- 2008
6. Enantiomeric CopA3 dimer peptide suppresses cell viability and tumor xenograft growth of human gastric cancer cells
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Yong Pyo Shin, Ho Jin Park, Jae Sam Hwang, In-Woo Kim, Sung-Hee Nam, Joon Ha Lee, Mi-Ae Kim, Dong-Chul Kang, Eun-Young Yun, Young Shin Lee, In Hee Lee, and Mi-Young Ahn
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0301 basic medicine ,Programmed cell death ,Cell Survival ,Blotting, Western ,Mice, Nude ,Antineoplastic Agents ,Apoptosis ,Biology ,Cell Line ,03 medical and health sciences ,chemistry.chemical_compound ,Stomach Neoplasms ,Cell Line, Tumor ,Animals ,Humans ,Viability assay ,Amino Acid Sequence ,Cytotoxicity ,Mice, Inbred BALB C ,TUNEL assay ,Dose-Response Relationship, Drug ,Acridine orange ,Stereoisomerism ,General Medicine ,Molecular biology ,Xenograft Model Antitumor Assays ,Tumor Burden ,030104 developmental biology ,chemistry ,Cell culture ,Caspases ,Cancer cell ,Insect Proteins ,Protein Multimerization ,Antimicrobial Cationic Peptides ,HeLa Cells ,Signal Transduction - Abstract
The CopA3 dimer peptide is a coprisin analog that has an anticancer effect against human cancer cells in vitro. In this study, we investigated the anticancer activity of the enantiomeric CopA3 dimer peptide in human gastric cancer cell lines as well as in an in vivo tumor xenograft model. Enantiomeric CopA3 reduced gastric cancer cell viability and exhibited cytotoxicity against cancer cells. Enantiomeric CopA3-induced cell death was mediated by specific interactions with phosphatidylserine and phosphatidylcholine, membrane components that are enriched in cancer cells, in a calcein leakage assay. Moreover, acridine orange/ethidium bromide staining, flow cytometric analysis, and Western blot analysis showed that enantiomeric CopA3 induced apoptotic and necrotic gastric cancer cell death. The antitumor effect was also observed in a mouse tumor xenograft model in which intratumoral inoculation of the peptide resulted in a significant decrease in the SNU-668 gastric cancer tumor volume. In addition, periodic acid-Schiff and hematoxylin staining and terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL) assay revealed apoptotic and necrotic cell death in tumor masses treated with greater than 150 μg CopA3. Collectively, these results indicate that the enantiomeric CopA3 dimer peptide induces apoptosis and necrosis of gastric cancer cells in vitro and in vivo, indicating that the peptide is a potential candidate for the treatment of gastric cancer, which is a common cause of cancer and cancer deaths worldwide.
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- 2015
7. Therapeutic Efficacy of Halocidin-Derived Peptide HG1 in a Mouse Model of Surgical Wound Infection with Methicillin-Resistant Staphylococcus aureus▿
- Author
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Yong Pyo Shin, Myung Hwa Kim, In Hee Lee, Seungmi Park, Seo Hwa Shin, and Young Shin Lee
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Methicillin-Resistant Staphylococcus aureus ,medicine.drug_class ,Antibiotics ,Biology ,Skin infection ,medicine.disease_cause ,Staphylococcal infections ,Microbiology ,Mice ,Dermis ,medicine ,Animals ,Surgical Wound Infection ,Pharmacology (medical) ,Experimental Therapeutics ,Pharmacology ,Surgical wound ,Staphylococcal Infections ,Antimicrobial ,medicine.disease ,Methicillin-resistant Staphylococcus aureus ,Anti-Bacterial Agents ,Infectious Diseases ,medicine.anatomical_structure ,Staphylococcus aureus ,Female ,Peptides - Abstract
We evaluated the therapeutic potential of HG1, an antimicrobial peptide, as a novel topical antibiotic by the use of a mouse surgical wound model of infection with methicillin-resistant Staphylococcus aureus . First, we attempted to determine whether or not HG1 infiltrated into the dermis when topically administered. Second, we evaluated the antibiotic effects of HG1 on skin infection via bacterial-enumeration and microscopic analyses. The results showed that topically administered HG1 was capable of penetrating into the dermis at the infection site, where it exerted its antimicrobial effects.
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- 2011
8. Characterization of Kunitz-type protease inhibitor purified from hemolymph of Galleria mellonella larvae
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Joon Lee, Yong Pyo Shin, Hwan Myung Lee, Chong Han Kim, Ho Jin Park, Seungmi Park, In Hee Lee, and Byung Sam Kim
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Serine Proteinase Inhibitors ,medicine.medical_treatment ,Proteolysis ,Fat Body ,Gene Expression ,Moths ,Biochemistry ,Hemolymph ,Extracellular ,medicine ,Escherichia coli ,Animals ,Extracellular Signal-Regulated MAP Kinases ,Molecular Biology ,Protease ,biology ,medicine.diagnostic_test ,fungi ,Midgut ,Epithelial Cells ,biology.organism_classification ,Trypsin ,Molecular biology ,Galleria mellonella ,Insect Science ,Larva ,Insect Proteins ,Integument ,medicine.drug - Abstract
We characterized a Kunitz-type protease inhibitor (Gm KTPI) obtained from the hemolymph of Galleria mellonella larvae immunized with Escherichia coli. The structural analysis of the cloned cDNA showed that it consists of 56 residues derived from the precursor of 75 amino acids. The peptide was constitutively produced in the fat bodies, but not in the midgut nor the integument of larvae. In our analysis of stage-dependent expression, its transcript was detected within the midgut, the fat bodies and the integument of the prepupae, which undergo tissue remodeling. The inhibition assays showed that Gm KTPI was capable of inhibiting only the trypsin-like activity of the larval midgut extracts. Furthermore, it was determined that Gm KTPI induced the activation of extracellular signal-regulated kinase (ERK) in the fat bodies and integument cells, and this kinase is known to perform a central role in cell proliferation signaling. Its effect on ERK activation was also verified in a control experiment using a human endothelial cell culture. Collectively, it was suggested that Gm KTPI might be responsible for the protection of other tissues against proteolytic attack by trypsin-like protease(s) from larval midgut during metamorphosis, and might play a role in the proliferation of cells in the fat body and integument.
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- 2010
9. An insect multiligand recognition protein functions as an opsonin for the phagocytosis of microorganisms
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Yeon Soo Han, Chong Han Kim, Yeon Sun Seong, Mi Young Noh, Yong Pyo Shin, Yong Hun Jo, and In Hee Lee
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Lipopolysaccharides ,animal structures ,Hemocytes ,beta-Glucans ,Phagocytosis ,Immunology ,Biology ,Biochemistry ,Microbiology ,Tissue Culture Techniques ,Immune system ,Opsonin Proteins ,Hemolymph ,Candida albicans ,Escherichia coli ,Animals ,Molecular Biology ,Opsonin ,Reverse Transcriptase Polymerase Chain Reaction ,fungi ,Pattern recognition receptor ,Cell Biology ,biology.organism_classification ,Flow Cytometry ,Lepidoptera ,Teichoic Acids ,Larva ,Receptors, Pattern Recognition ,Insect Proteins ,Lipoteichoic acid ,Micrococcus luteus ,Protein Binding - Abstract
We characterize a novel pathogen recognition protein obtained from the lepidopteran Galleria mellonella. This protein recognizes Escherichia coli, Micrococcus luteus, and Candida albicans via specific binding to lipopolysaccharides, lipoteichoic acid, and beta-1,3-glucan, respectively. As a multiligand receptor capable of coping with a broad variety of invading pathogens, it is constitutively produced in the fat body, midgut, and integument but not in the hemocytes and is secreted into the hemolymph. The protein was confirmed to be relevant to cellular immune response and to further function as an opsonin that promotes the uptake of invading microorganisms into hemocytes. Our data reveal that the mechanism by which a multiligand receptor recognizes microorganisms contributes substantially to their phagocytosis by hemocytes. A better understanding of an opsonin with the required repertoire for detecting diverse invaders might provide us with critical insights into the mechanisms underlying insect phagocytosis.
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- 2010
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