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KAAACI Allergic Rhinitis Guidelines: Part 1. Update in Pharmacotherapy
Yang Song-I,Lee Il Hwan,Kim Minji,Ryu Gwanghui,강성윤,Kim Mi-Ae,이상민,Kim Hyun-Jung,Park Do-Yang,Lee Yong Ju,Kim Dong-Kyu,Kim Soo Whan,Kim Do Hyun,Jun Young Joon,박상철,Kim Bong-Seong,Chung Soo Jie,Lee Hyun J 대한천식알레르기학회 2023 Allergy, Asthma & Immunology Research Vol.15 No.1
The prevalence of allergic rhinitis (AR) and the socioeconomic burden associated with the medical cost and quality of life (QOL) of AR have progressively increased. Therefore, practical guidelines for the appropriate management of AR need to be developed based on scientific evidence while considering the real-world environment, values, and preferences of patients and physicians. The Korean Academy of Asthma, Allergy and Clinical Immunology revised clinical guidelines of AR to address key clinical questions of the management of AR. Part 1 of the revised guideline covers the pharmacological management of patients with AR in Korea. Through a meta-analysis and systematic review, we made 4 recommendations for AR pharmacotherapy, including intranasal corticosteroid (INCS)/intranasal antihistamine (INAH) combination therapy, oral antihistamine/INCS combination therapy, leukotriene receptor antagonist treatment in AR patients with asthma, and prophylactic treatment for patients with pollen-induced AR. However, all recommendations are conditional because of the low or very low evidence of certainty. Well-designed and strictly executed randomized controlled trials are needed to measure and report appropriate outcomes.
Interleukin-33 stimulates formation of functional osteoclasts from human CD14(+) monocytes.
Mun, Se Hwan,Ko, Na Young,Kim, Hyuk Soon,Kim, Jie Wan,Kim, Do Kyun,Kim, A-Ram,Lee, Seung Hyun,Kim, Yong-Gil,Lee, Chang Keun,Lee, Seoung Hoon,Kim, Bo Kyung,Beaven, Michael A,Kim, Young Mi,Choi, Wahn So Birkhäuser ; Springer 2010 Cellular and molecular life sciences Vol.67 No.22
<P>Interleukin (IL)-33 is a recently described pro-inflammatory cytokine. Here we demonstrate IL-33 as a regulator of functional osteoclasts (OCs) from human CD14(+) monocytes. IL-33 stimulates formation of tartrate-resistant acid phosphatase (TRAP)(+) multinuclear OCs from monocytes. This action was suppressed by anti-ST2 antibody, suggesting that IL-33 acts through its receptor ST2, but not by the receptor activator of NF-κB ligand (RANKL) decoy, osteoprotegerin, or anti-RANKL antibody. IL-33 stimulated activating phosphorylations of signaling molecules in monocytes that are critical for OC development. These included Syk, phospholipase Cγ2, Gab2, MAP kinases, TAK-1, and NF-κB. IL-33 also enhanced expression of OC differentiation factors including TNF-α receptor-associated factor 6 (TRAF6), nuclear factor of activated T cells cytoplasmic 1, c-Fos, c-Src, cathepsin K, and calcitonin receptor. IL-33 eventually induced bone resorption. This study suggests that the osteoclastogenic property of IL-33 is mediated through TRAF6 as well as the immunoreceptor tyrosine-based activation motif-dependent Syk/PLCγ pathway in human CD14(+) monocytes.</P>
Kim Su Jeong,Choi Min Yeong,Min Keun Young,Jo Min Geun,Kim Jie Min,Kim Hyung Sik,Kim Young Mi 한국응용약물학회 2022 Biomolecules & Therapeutics(구 응용약물학회지) Vol.30 No.6
Mast cells are an effector cell that plays a pivotal role in type I hypersensitive immune responses. Mast cells exist in connective tissues, such as skin and mucosal tissue, and contain granules which contain bioactive substances such as histamine and heparin in cells. The granules of mast cells are secreted by antigen stimulation to cause the type I allergic hypersensitivity. In addition, stimulated by antigen, mast cells synthesize and secrete various eicosanoids and cytokines. While AT9283 is known to have anticancer effects, the therapeutic effect of AT9283 on allergic disorders is completely unknown. In this study, it was found that AT9283 reversibly inhibited antigen-IgE binding-induced degranulation in mast cells (IC50, approx. 0.58 μM) and suppressed the secretion of the inflammatory cytokines IL-4 (IC50, approx. 0.09 μM) and TNF-α (IC50, approx. 0.19 μM). For a mechanism of mast cell inhibition, while not inhibiting Syk phosphorylation, AT9283 suppressed the activation of LAT, a downstream substrate protein of Syk, in a dose-dependent manner. As expected, AT9283 also inhibited the activation of PLCγ1 and Akt, downstream signaling molecules of Syk/LAT, and MAP kinases such as JNK, Erk1/2, and P38. In an in vitro protein tyrosine kinase assay, AT9283 directly inhibited Syk activity. Next, AT9283 dose-dependently inhibited passive cutaneous anaphylaxis (PCA), an IgE-mediated allergic acute response, in mice (ED50, approx. 34 mg/kg, p.o.). These findings suggest that AT9283 has potential to use as a new drug for alleviating the symptoms of IgE-mediated allergic disorders.
Antitumor and Immunomodulatory Effect of Gastrodia elata on Colon Cancer In Vitro and In Vivo
Kim, Na-Hyung,Xin, Ming Jie,Cha, Ji-Yoon,Ji, Soo-Jeong,Kwon, Se-Uk,Jee, Ho-Kyun,Park, Mi-Ran,Park, Yong-Soo,Kim, Chong-Tai,Kim, Dae-Ki AMERICAN JOURNAL OF CHINESE MEDICINE INC 2017 The American journal of Chinese medicine Vol.45 No.2
Application of antihelix antibodies in protein structure determination
Kim, Ji Won,Kim, Songwon,Lee, Haerim,Cho, Geunyoung,Kim, Sun Chang,Lee, Hayyoung,Jin, Mi Sun,Lee, Jie-Oh National Academy of Sciences 2019 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.116 No.36
<P><B>Significance</B></P><P>Antibodies have been found to be helpful for structural studies of challenging proteins by X-ray crystallography and electron microscopy. They are being used to construct useful protein nanostructures as well. Antibodies suitable for structural study should recognize the 3-dimensional conformations of target proteins. However, generating such antibodies and characterizing structures of their complexes with antigens take months or even years of research. Here, we show that we can expand the application of well-characterized antibodies by “transplanting” the alpha-helical epitopes that they recognize to proteins with completely different structures and sequences. Systematic screening of more antihelix antibodies will greatly expand the scope of the method.</P><P>Antibodies are indispensable tools in protein engineering and structural biology. Antibodies suitable for structural studies should recognize the 3-dimensional (3D) conformations of target proteins. Generating such antibodies and characterizing their complexes with antigens take a significant amount of time and effort. Here, we show that we can expand the application of well-characterized antibodies by “transplanting” the epitopes that they recognize to proteins with completely different structures and sequences. Previously, several antibodies have been shown to recognize the alpha-helical conformation of antigenic peptides. We demonstrate that these antibodies can be made to bind to a variety of unrelated “off-target” proteins by modifying amino acids in the preexisting alpha helices of such proteins. Using X-ray crystallography, we determined the structures of the engineered protein–antibody complexes. All of the antibodies bound to the epitope-transplanted proteins, forming accurately predictable structures. Furthermore, we showed that binding of these antihelix antibodies to the engineered target proteins can modulate their catalytic activities by trapping them in selected functional states. Our method is simple and efficient, and it will have applications in protein X-ray crystallography, electron microscopy, and nanotechnology.</P>
Crystal Structure of the TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide
Jin, Mi Sun,Kim, Sung Eun,Heo, Jin Young,Lee, Mi Eun,Kim, Ho Min,Paik, Sang-Gi,Lee, Hayyoung,Lee, Jie-Oh Elsevier 2007 Cell Vol.130 No.6
<P><B>Summary</B></P><P>TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides. Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex. Binding of the tri-acylated lipopeptide, Pam<SUB>3</SUB>CSK<SUB>4</SUB>, induced the formation of an “m” shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam<SUB>2</SUB>CSK<SUB>4</SUB>, did not. The three lipid chains of Pam<SUB>3</SUB>CSK<SUB>4</SUB> mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1. An extensive hydrogen-bonding network, as well as hydrophobic interactions, between TLR1 and TLR2 further stabilize the heterodimer. We propose that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.</P>
( Yoo Mi Park ),( Hee Sun Kim ),( Jae Jun Park ),( Su Jung Baik ),( Kyung Hee Kim ),( Cho Rong Oh ),( Jie Hyun Kim ),( Young Hoon Yoon ),( Hyo Jin Park ),( Sang In Lee ) 대한내과학회 2014 대한내과학회 추계학술대회 Vol.2014 No.1
Background: Limited data are available for advanced colorectal neoplasm in asymptomatic individuals 40 to 49 years of age. We aimed to identify risk factors and develop simple prediction model for advanced colorectal neoplasm in these persons Methods: This study was conducted among 2,781 asymptomatic subjects, 40-49 year, who underwent colonoscopy for routine health examination. Clinical data was collected from physical examination and blood tests. Subjects were randomly allocated to either a development or validation set at a 2:1 ratio. Logistic Regression analysis was used to determine predictors of advanced colorectal neoplasm. Results: The prevalence of overall and advanced colorectal neoplasm was 20.2 % and 2.5% respectively. Older age (45-49 years), male gender, positive serology of Helicobacter pylori, high triglyceride and low HDL levels were independently associated with an increased risk of advanced colorectal neoplasm. We developed a simple scoring model for advanced colorectal neoplasms (range 0-9), and a cut point of =4 defined 45% of subjects as being at high risk for advanced colorectal neoplasm and yielded a sensitivity of 78%, specificity of 56%, and positive likelihood ratio of 1.8 (area under curve [AUC]=0.74). Comparable results were obtained in validation datasets (sensitivity 79%, specificity 58%, and AUC=0.72). Conclusions: Older age (45-49 years), male gender, positive serology of Helicobacter pylori, high triglyceride and low HDL levels were identified as an independent risk factors for advanced colorectal neoplasm. A simple scoring model that consist of these 5 parameters may be useful for selecting patients who benefit from screening colonoscopy.