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[PMID]: 29227167
[Au] Autor:Andres O; Henning K; Strauß G; Pflug A; Manukjan G; Schulze H
[Ad] Address:a University Children's Hospital , Würzburg , Germany.
[Ti] Title:Diagnosis of platelet function disorders: A standardized, rational, and modular flow cytometric approach.
[So] Source:Platelets;:1-10, 2017 Dec 11.
[Is] ISSN:1369-1635
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:A high proportion of patients with mucocutaneous bleeding diathesis and suspected inherited or acquired platelet disorder remain without diagnosis even after comprehensive laboratory testing. Since flow cytometry allows investigation of resting and activated platelets on the single cell level by requiring only minimal amounts of blood, this method has become an important assay within the diagnostic algorithm, especially in pediatrics. We therefore developed a standardized and modular flow cytometric approach that contributes to clarify impaired platelet function in a rational step-by-step manner. Due to simultaneous analysis of four fluorophores in a basic panel design, we are able to readily detect the most common and clinically significant platelet disorders: Glanzmann thrombasthenia or Glanzmann-like diseases (fibrinogen receptor GPIIb-IIIa), Bernard-Soulier syndrome (von Willebrand-factor receptor complex GPIb-IX-V) and less well characterized ß1-integrins that serve as the collagen, laminin or fibronectin receptor (CD29-CD49b, e and f, respectively). Platelet reactivity was investigated in response to the agonists adenosine diphosphate (ADP) and thrombin receptor activator peptide 6 (TRAP6) in suboptimal and optimal concentrations by quantifying surface expression of activation markers CD62P and CD63 as well as binding of PAC-1 antibody to the high affinity conformation of the fibrinogen receptor. For advanced diagnostic questions, several further modules were implemented: (i) calcium mobilization for evaluation of early signal transduction, (ii) a kinetically resolved mepacrine assay for estimation of delta-granule content and release, and (iii) a module to determine platelet reactivity upon additional agonists like the thromboxane A -analogue U46619 or collagen. Blood withdrawn from a healthy control cohort allowed generating preliminary standard values for all parameters. The modules were validated by analysis of patients with known or suspected platelet defects (leukocyte-adhesion deficiency type III, Wiskott-Aldrich syndrome, acute myeloid leukemia, sickle cell disease and chronic immune thrombocytopenia).
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 171211
[Lr] Last revision date:171211
[St] Status:Publisher
[do] DOI:10.1080/09537104.2017.1386297

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[PMID]: 28739949
[Au] Autor:Li H; Deng Y; Sun K; Yang H; Liu J; Wang M; Zhang Z; Lin J; Wu C; Wei Z; Yu C
[Ad] Address:Department of Biology, Southern University of Science and Technology, Shenzhen 518055, China.
[Ti] Title:Structural basis of kindlin-mediated integrin recognition and activation.
[So] Source:Proc Natl Acad Sci U S A;114(35):9349-9354, 2017 Aug 29.
[Is] ISSN:1091-6490
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Kindlins and talins are integrin-binding proteins that are critically involved in integrin activation, an essential process for many fundamental cellular activities including cell-matrix adhesion, migration, and proliferation. As FERM-domain-containing proteins, talins and kindlins, respectively, bind different regions of ß-integrin cytoplasmic tails. However, compared with the extensively studied talin, little is known about how kindlins specifically interact with integrins and synergistically enhance their activation by talins. Here, we determined crystal structures of kindlin2 in the apo-form and the ß1- and ß3-integrin bound forms. The apo-structure shows an overall architecture distinct from talins. The complex structures reveal a unique integrin recognition mode of kindlins, which combines two binding motifs to provide specificity that is essential for integrin activation and signaling. Strikingly, our structures uncover an unexpected dimer formation of kindlins. Interrupting dimer formation impairs kindlin-mediated integrin activation. Collectively, the structural, biochemical, and cellular results provide mechanistic explanations that account for the effects of kindlins on integrin activation as well as for how kindlin mutations found in patients with Kindler syndrome and leukocyte-adhesion deficiency may impact integrin-mediated processes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1707
[Cu] Class update date: 170922
[Lr] Last revision date:170922
[St] Status:In-Data-Review
[do] DOI:10.1073/pnas.1703064114

  3 / 445 MEDLINE  
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[PMID]: 28328326
[Au] Autor:Moutsopoulos NM; Zerbe CS; Wild T; Dutzan N; Brenchley L; DiPasquale G; Uzel G; Axelrod KC; Lisco A; Notarangelo LD; Hajishengallis G; Notarangelo LD; Holland SM
[Ad] Address:From the National Institute of Dental and Craniofacial Research (N.M.M., T.W., N.D., L.B., G.D.), the Laboratory of Clinical Infectious Diseases (C.S.Z., G.U., S.M.H.), and the Laboratory of Immunoregulation (A.L.), National Institute of Allergy and Infectious Diseases, and the Wound-Ostomy Care Nur
[Ti] Title:Interleukin-12 and Interleukin-23 Blockade in Leukocyte Adhesion Deficiency Type 1.
[So] Source:N Engl J Med;376(12):1141-1146, 2017 03 23.
[Is] ISSN:1533-4406
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:A patient with leukocyte adhesion deficiency type 1 (LAD1) had severe periodontitis and an intractable, deep, nonhealing sacral wound. We had previously found a dominant interleukin-23-interleukin-17 signature at inflamed sites in humans with LAD1 and in mouse models of the disorder. Blockade of this pathway in mouse models has resulted in resolution of the immunopathologic condition. We treated our patient with ustekinumab, an antibody that binds the p40 subunit of interleukin-23 and interleukin-12 and thereby blocks the activity of these cytokines, inhibiting interleukin-23-dependent production of interleukin-17. After 1 year of therapy, our patient had resolution of his inflammatory lesions without serious infections or adverse reactions. Inhibition of interleukin-23 and interleukin-17 may have a role in the management of LAD1. (Funded by the National Institute of Allergy and Infectious Diseases and others.).
[Mh] MeSH terms primary: Interleukin-12/antagonists & inhibitors
Interleukin-23/antagonists & inhibitors
Leukocyte-Adhesion Deficiency Syndrome/drug therapy
Ustekinumab/therapeutic use
[Mh] MeSH terms secundary: Gingiva/pathology
Humans
Injections, Subcutaneous
Interleukin-17/metabolism
Interleukin-23/metabolism
Leukocyte-Adhesion Deficiency Syndrome/complications
Male
Periodontal Diseases/drug therapy
Periodontal Diseases/etiology
Periodontal Diseases/pathology
RNA, Messenger/metabolism
Skin Ulcer/drug therapy
Skin Ulcer/etiology
Skin Ulcer/pathology
Ustekinumab/adverse effects
Young Adult
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Name of substance:0 (Interleukin-17); 0 (Interleukin-23); 0 (RNA, Messenger); 187348-17-0 (Interleukin-12); FU77B4U5Z0 (Ustekinumab)
[Em] Entry month:1704
[Cu] Class update date: 170923
[Lr] Last revision date:170923
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:170323
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMoa1612197

  4 / 445 MEDLINE  
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[PMID]: 27749372
[Au] Autor:Stadtmann A; Zarbock A
[Ad] Address:Department of Anaesthesiology, Intensive Care and Pain Medicine, University of Münster, Münster, Germany.
[Ti] Title:The role of kindlin in neutrophil recruitment to inflammatory sites.
[So] Source:Curr Opin Hematol;24(1):38-45, 2017 Jan.
[Is] ISSN:1531-7048
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:PURPOSE OF REVIEW: Since the discovery of the lack of kindlin-3 expression as the reason for the immunopathology leukocyte adhesion deficiency III syndrome, the role of kindlin-3 in inflammatory processes was investigated in a numerous studies. This review gives an overview about recent findings regarding the role of kindlin-3 in neutrophil activation and recruitment. RECENT FINDINGS: Kindlin-3, together with talin-1, contributes essentially to the activation of ß2-integrins in neutrophils. During inside-out signaling, kindlin-3 binds to the ß-cytoplasmic integrin tail and is indispensable for the integrin conformational shift into the high-affinity ligand binding conformation, but not for the intermediate (extended) conformation. During outside-in signaling (as a consequence of integrin ligand binding) kindlin-3 interacts with distinct signaling molecules and is required for cell-autonomous functions like migration and spreading. SUMMARY: Leukocyte adhesion deficiency III syndrome, which is caused by absence of kindlin-3, is a rarely occurring disease. However, the investigation of the clinical symptoms as well as the underlying molecular mechanisms gave rise to a huge amount of new insights into the processes of integrin activation in neutrophils and the consequences of defects in these processes.
[Mh] MeSH terms primary: Inflammation/etiology
Inflammation/metabolism
Neutrophil Infiltration
Neutrophils/physiology
[Mh] MeSH terms secundary: Animals
Carrier Proteins
Cell Adhesion Molecules/chemistry
Cell Adhesion Molecules/genetics
Cell Adhesion Molecules/metabolism
Chemotaxis, Leukocyte/genetics
Chemotaxis, Leukocyte/immunology
Gene Expression Regulation
Humans
Inflammation/pathology
Integrins/genetics
Integrins/metabolism
Leukocyte-Adhesion Deficiency Syndrome/etiology
Leukocyte-Adhesion Deficiency Syndrome/metabolism
Leukocytes/physiology
Protein Binding
Signal Transduction
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Carrier Proteins); 0 (Cell Adhesion Molecules); 0 (Integrins)
[Em] Entry month:1710
[Cu] Class update date: 171026
[Lr] Last revision date:171026
[Js] Journal subset:IM
[Da] Date of entry for processing:161018
[St] Status:MEDLINE

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[PMID]: 27803145
[Au] Autor:Sivathanu S; Sampath S; Sridhar I
[Ad] Address:ESIC Medical College and Post Graduate Institute of Medical Sciences and Research, Chennai, India.
[Ti] Title:Case 1: Recurrent Omphalitis and Nonhealing Ulcers in a 7-month-old Girl.
[So] Source:Pediatr Rev;37(11):491-493, 2016 Nov.
[Is] ISSN:1526-3347
[Cp] Country of publication:United States
[La] Language:eng
[Mh] MeSH terms primary: Leukocyte-Adhesion Deficiency Syndrome/diagnosis
Leukocyte-Adhesion Deficiency Syndrome/therapy
Scalp Dermatoses/diagnosis
Skin Ulcer/diagnosis
[Mh] MeSH terms secundary: Anti-Bacterial Agents/therapeutic use
Combined Modality Therapy
Diagnosis, Differential
Erythrocyte Transfusion/methods
Female
Follow-Up Studies
Humans
Infant
Leukocyte Transfusion/methods
Leukocyte-Adhesion Deficiency Syndrome/genetics
Rare Diseases
Risk Assessment
Scalp Dermatoses/etiology
Skin Ulcer/etiology
Treatment Outcome
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Anti-Bacterial Agents)
[Em] Entry month:1704
[Cu] Class update date: 170414
[Lr] Last revision date:170414
[Js] Journal subset:IM
[Da] Date of entry for processing:161103
[St] Status:MEDLINE

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[PMID]: 27056660
[Au] Autor:Leon-Rico D; Aldea M; Sanchez-Baltasar R; Mesa-Nuñez C; Record J; Burns SO; Santilli G; Thrasher AJ; Bueren JA; Almarza E
[Ad] Address:1 Division of Hematopoietic Innovative Therapies, Centro de Investigaciones Energéticas, Medioambientales y Tecnológicas (CIEMAT) , and Centro de Investigación Biomédica en Red de Enfermedades Raras (CIBERER), Madrid, Spain .
[Ti] Title:Lentiviral Vector-Mediated Correction of a Mouse Model of Leukocyte Adhesion Deficiency Type I.
[So] Source:Hum Gene Ther;27(9):668-78, 2016 Sep.
[Is] ISSN:1557-7422
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Leukocyte adhesion deficiency type I (LAD-I) is a primary immunodeficiency caused by mutations in the ITGB2 gene and is characterized by recurrent and life-threatening bacterial infections. These mutations lead to defective or absent expression of ß2 integrins on the leukocyte surface, compromising adhesion and extravasation at sites of infection. Three different lentiviral vectors (LVs) conferring ubiquitous or preferential expression of CD18 in myeloid cells were constructed and tested in human and mouse LAD-I cells. All three hCD18-LVs restored CD18 and CD11a membrane expression in LAD-I patient-derived lymphoblastoid cells. Corrected cells recovered the ability to aggregate and bind to sICAM-1 after stimulation. All vectors induced stable hCD18 expression in hematopoietic cells from mice with a hypomorphic Itgb2 mutation (CD18(HYP)), both in vitro and in vivo after transplantation of corrected cells into primary and secondary CD18(HYP) recipients. hCD18(+) hematopoietic cells from transplanted CD18(HYP) mice also showed restoration of mCD11a surface co-expression. The analysis of in vivo neutrophil migration in CD18(HYP) mice subjected to two different inflammation models demonstrated that the LV-mediated gene therapy completely restored neutrophil extravasation in response to inflammatory stimuli. Finally, these vectors were able to correct the phenotype of human myeloid cells derived from CD34(+) progenitors defective in ITGB2 expression. These results support for the first time the use of hCD18-LVs for the treatment of LAD-I patients in clinical trials.
[Mh] MeSH terms primary: CD18 Antigens/genetics
Genetic Therapy
Genetic Vectors/administration & dosage
Lentivirus/genetics
Leukocyte-Adhesion Deficiency Syndrome/therapy
[Mh] MeSH terms secundary: Animals
Antigens, CD34/metabolism
Cell Differentiation
Disease Models, Animal
Humans
Leukocyte-Adhesion Deficiency Syndrome/genetics
Mice
Neutrophils/cytology
Neutrophils/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Antigens, CD34); 0 (CD18 Antigens)
[Em] Entry month:1708
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:160409
[St] Status:MEDLINE
[do] DOI:10.1089/hum.2016.016

  7 / 445 MEDLINE  
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[PMID]: 26639818
[Au] Autor:Yassaee VR; Hashemi-Gorji F; Boosaliki S; Parvaneh N
[Ad] Address:Genomic Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran; Dept. of Medical Genetics, Faculty of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
[Ti] Title:Mutation spectra of the ITGB2 gene in Iranian families with leukocyte adhesion deficiency type 1.
[So] Source:Hum Immunol;77(2):191-5, 2016 Feb.
[Is] ISSN:1879-1166
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Leukocyte adhesion deficiency type 1 (LAD1) is an autosomal recessive disorder clinically characterized by severe, recurrent bacterial infections, impaired pus formation and wound healing. It is caused by mutation in the ITGB2 gene, encoding the ß2 integrin subunit of the leukocyte adhesion cell molecule. This study aimed to identify disease causing mutations in 19 consanguineous families diagnosed with LAD1. Blood samples were collected after informed and written consent was obtained. Genomic DNA was extracted from peripheral blood of patients and their parents. PCR amplification of the ITGB2 gene was done using specific primers followed by sequencing for mutation detection. A total number of 14 alterations scattered throughout the ITGB2 gene were ascertained in which 10 mutations were previously reported, including c.329-6C>A, c.382G>T, c.715G>A, c.843delC, c.897+1G>A, c.1062A>T, c.1143delC, c.1877+2T>C, c.1907delA and c.2147G>C. Four novel likely pathogenic mutations consisting of c.576dupC (Asn193GlnfsX72), c.706G>A (Gly236Arg), c.897+1G>T and c.1030G>T (Glu344(∗)), were identified. The majority of these mutations were located in exon six, suggesting this exon as a hotspot region probably. This study emphasis on allelic heterogeneity of the ITGB2 gene in Iranian patients diagnosed with LAD1. Our results suggest that every population should develop a mutation database for rare genetic disorders to take advantage in genetic counseling clinic as well as genetic testing for rapid diagnostic purposes.
[Mh] MeSH terms primary: CD18 Antigens/genetics
Leukocyte-Adhesion Deficiency Syndrome/genetics
Mutation/genetics
[Mh] MeSH terms secundary: Consanguinity
DNA Mutational Analysis
Exons/genetics
Gene Frequency
Genetic Association Studies
Genetic Predisposition to Disease
Genotype
Humans
Iran
Leukocyte-Adhesion Deficiency Syndrome/immunology
Pedigree
Polymorphism, Genetic
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (CD18 Antigens)
[Em] Entry month:1611
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:151208
[St] Status:MEDLINE

  8 / 445 MEDLINE  
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[PMID]: 26434744
[Au] Autor:Levy-Mendelovich S; Rechavi E; Abuzaitoun O; Vernitsky H; Simon AJ; Lev A; Somech R
[Ad] Address:Pediatric Department and the Immunology Service, "Edmond and Lily Safra" Children's Hospital, Chaim Sheba Medical Center, 52621, Tel Hashomer, Israel.
[Ti] Title:Highlighting the problematic reliance on CD18 for diagnosing leukocyte adhesion deficiency type 1.
[So] Source:Immunol Res;64(2):476-82, 2016 Apr.
[Is] ISSN:1559-0755
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Leukocyte adhesion deficiency type 1 (LAD-1) is an autosomal recessive primary immunodeficiency, hallmarked by defective polymorphonuclear transmigration. It is caused by mutations in the gene encoding CD18, which interfere with the CD18/CD11 heterodimerization and expression on leukocyte cell surface. LAD-1 diagnosis rests primarily on the measurement of CD18 expression. However, CD18 measurement entails its pitfalls. Here we present a cohort of ten LAD patients and a review of the relevant literature illustrating the difficulties in sole reliance on CD18 measurement for initial diagnosis. These include normal range expression in some mutations, great variability between patients with the same mutation and subjective interpretation of results. We think there is a need for additional markers as part of the initial LAD diagnostic algorithm. We suggest CD11a expression, which was near absent in all patients in our cohort. The dual use of CD18 and CD11a can increase testing sensitivity and prevent delayed diagnosis of LAD-1.
[Mh] MeSH terms primary: CD18 Antigens/metabolism
Leukocyte-Adhesion Deficiency Syndrome/diagnosis
Leukocyte-Adhesion Deficiency Syndrome/metabolism
[Mh] MeSH terms secundary: Biomarkers
CD18 Antigens/genetics
Case-Control Studies
Female
Hematopoietic Stem Cell Transplantation
Humans
Immunophenotyping
Infant
Infant, Newborn
Leukocyte Count
Leukocyte-Adhesion Deficiency Syndrome/genetics
Leukocyte-Adhesion Deficiency Syndrome/therapy
Leukocytes/immunology
Leukocytes/metabolism
Male
Mutation
Phenotype
Reproducibility of Results
Transplantation, Homologous
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Biomarkers); 0 (CD18 Antigens)
[Em] Entry month:1612
[Cu] Class update date: 171116
[Lr] Last revision date:171116
[Js] Journal subset:IM
[Da] Date of entry for processing:151006
[St] Status:MEDLINE
[do] DOI:10.1007/s12026-015-8706-5

  9 / 445 MEDLINE  
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[PMID]: 26375893
[Au] Autor:Hajishengallis G; Moutsopoulos NM
[Ad] Address:Department of Microbiology, University of Pennsylvania Penn Dental Medicine, Philadelphia, PA 19104, USA. Electronic address: geoh@upenn.edu.
[Ti] Title:Role of bacteria in leukocyte adhesion deficiency-associated periodontitis.
[So] Source:Microb Pathog;94:21-6, 2016 May.
[Is] ISSN:1096-1208
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Leukocyte adhesion deficiency Type I (LAD-I)-associated periodontitis is an aggressive form of inflammatory bone loss that has been historically attributed to lack of neutrophil surveillance of the periodontal infection. However, this form of periodontitis has proven unresponsive to antibiotics and/or mechanical removal of the tooth-associated biofilm. Recent studies in LAD-I patients and relevant animal models have shown that the fundamental cause of LAD-I periodontitis involves dysregulation of a granulopoietic cytokine cascade. This cascade includes interleukin IL-23 (IL-23) and IL-17 that drive inflammatory bone loss in LAD-I patients and animal models and, moreover, foster a nutritionally favorable environment for bacterial growth and development of a compositionally unique microbiome. Although the lack of neutrophil surveillance in the periodontal pockets might be expected to lead to uncontrolled bacterial invasion of the underlying connective tissue, microbiological analyses of gingival biopsies from LAD-I patients did not reveal tissue-invasive infection. However, bacterial lipopolysaccharide was shown to translocate into the lesions of LAD-I periodontitis. It is concluded that the bacteria serve as initial triggers for local immunopathology through translocation of bacterial products into the underlying tissues where they unleash the dysregulated IL-23-IL-17 axis. Subsequently, the IL-23/IL-17 inflammatory response sustains and shapes a unique local microbiome which, in turn, can further exacerbate inflammation and bone loss in the susceptible host.
[Mh] MeSH terms primary: Bacterial Physiological Phenomena
Leukocyte-Adhesion Deficiency Syndrome/microbiology
Periodontitis/microbiology
[Mh] MeSH terms secundary: Alveolar Bone Loss/immunology
Alveolar Bone Loss/microbiology
Alveolar Bone Loss/pathology
Animals
Gingiva/immunology
Gingiva/microbiology
Gingiva/pathology
Humans
Interleukin-17/immunology
Interleukin-23/immunology
Leukocyte-Adhesion Deficiency Syndrome/immunology
Leukocyte-Adhesion Deficiency Syndrome/pathology
Lipopolysaccharides
Neutrophils/immunology
Periodontitis/diagnostic imaging
Periodontitis/immunology
Periodontitis/pathology
Radiography, Panoramic
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (IL17A protein, human); 0 (Interleukin-17); 0 (Interleukin-23); 0 (Lipopolysaccharides)
[Em] Entry month:1704
[Cu] Class update date: 170501
[Lr] Last revision date:170501
[Js] Journal subset:IM
[Da] Date of entry for processing:150917
[St] Status:MEDLINE

  10 / 445 MEDLINE  
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[PMID]: 26359933
[Au] Autor:Suratannon N; Yeetong P; Srichomthong C; Amarinthnukrowh P; Chatchatee P; Sosothikul D; van Hagen PM; van der Burg M; Wentink M; Driessen GJ; Suphapeetiporn K; Shotelersuk V
[Ad] Address:Division of Allergy and Immunology, Department of Pediatrics, Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand.
[Ti] Title:Adaptive immune defects in a patient with leukocyte adhesion deficiency type III with a novel mutation in FERMT3.
[So] Source:Pediatr Allergy Immunol;27(2):214-7, 2016 Mar.
[Is] ISSN:1399-3038
[Cp] Country of publication:England
[La] Language:eng
[Mh] MeSH terms primary: B-Lymphocytes/physiology
Leukocyte-Adhesion Deficiency Syndrome/genetics
Membrane Proteins/genetics
Neoplasm Proteins/genetics
Pneumonia, Bacterial/genetics
[Mh] MeSH terms secundary: Adaptive Immunity/genetics
Antibodies/blood
Cell Differentiation/genetics
Child, Preschool
Female
Humans
Immunoglobulin Class Switching/genetics
Infant
Leukocyte-Adhesion Deficiency Syndrome/diagnosis
Mutation/genetics
Pedigree
Pneumonia, Bacterial/diagnosis
[Pt] Publication type:CASE REPORTS; LETTER; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Antibodies); 0 (MIG2B protein, human); 0 (Membrane Proteins); 0 (Neoplasm Proteins)
[Em] Entry month:1612
[Cu] Class update date: 161230
[Lr] Last revision date:161230
[Js] Journal subset:IM
[Da] Date of entry for processing:150912
[St] Status:MEDLINE
[do] DOI:10.1111/pai.12485


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