E. Bergen, S. Mastbergen, F. Lafeber, R. Schutgens, L. Vulpen
{"title":"Joint Health Markers in Hemophilia: The State of the Art","authors":"E. Bergen, S. Mastbergen, F. Lafeber, R. Schutgens, L. Vulpen","doi":"10.33696/immunology.3.124","DOIUrl":"https://doi.org/10.33696/immunology.3.124","url":null,"abstract":"Hemophilia is a rare congenital bleeding disorder caused by a lack of or diminished activity of clotting factor VIII (hemophilia A) or IX (hemophilia B). This deficiency leads to an increase in spontaneous and traumatic bleeding especially in the large hinged joints. Joint bleeding may result in synovial inflammation and cartilage/bone damage, ultimately leading to irreversible hemophilic arthropathy (HA) [1]. Preventing hemarthroses and accurately monitoring joint status once arthropathy has developed, is of utmost importance to prevent invalidating arthropathy and subsequent major orthopedic interventions.","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2021-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41455245","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Glycogen Synthase Kinase-3 (GSK-3) Regulation of Inhibitory Coreceptor Expression in T-cell Immunity","authors":"Mark E Issa, C. Rudd","doi":"10.33696/immunology.3.115","DOIUrl":"https://doi.org/10.33696/immunology.3.115","url":null,"abstract":"The serine/threonine kinase, glycogen synthase kinase 3 (GSK-3) has been implicated in immune cell activation and function. Our recent studies have shown that the abrogation of GSK-3 activity down-regulates the expression of key inhibitory receptors PD-1 and LAG-3. It also regulates the expression of the transcription factor NFAT which, in turn, is responsible for inhibiting PD-1/LAG-3 transcription as well as activating the expression of cytolytic effector proteins such as perforin and granzyme B. The role of components of the Wnt signaling pathway in these events remains to be fully uncovered. This mini-review discusses the recent discoveries that have elucidated the role of the GSK-3 signaling pathway in cancer immunotherapy.","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":"3 1","pages":"336 - 342"},"PeriodicalIF":0.0,"publicationDate":"2021-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46848278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Megalin-Mediated Trafficking of Mitochondrial Intracrines: Relevance to Signaling and Metabolism","authors":"D. Sheikh-Hamad, Michael W. Holliday, Qingtian Li","doi":"10.33696/immunology.3.118","DOIUrl":"https://doi.org/10.33696/immunology.3.118","url":null,"abstract":"The multi-ligand binding protein megalin (LRP2) is ubiquitously expressed and facilitates cell uptake of hormones, nutrients and vitamins. We have recently shown megalin is present in the mitochondria of cultured epithelial and mesenchymal cells, as well as many organs and tissues. Mitochondrial megalin associates with stanniocalcin-1 and SIRT3; two proteins that promote anti-oxidant defenses. Megalin shuttles mitochondrial intracrines (angiotensin II, stanniocalcin-1 and TGF-β) from the cell surface to the mitochondria through the retrograde early endosome to Golgi pathway and requires Rab32. Deletion of megalin impairs mitochondrial respiration and glycolysis. This pathway overlaps molecular and vesicular trafficking defects common to Donai Barrow and Lowe syndromes, suggesting that mitochondrial intracrine signaling defects may contribute to the pathogenesis of these diseases.","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":"3 1","pages":"364 - 369"},"PeriodicalIF":0.0,"publicationDate":"2021-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47858126","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Megalin-Mediated Trafficking of Mitochondrial Intracrines: Relevance to Signaling and Metabolism.","authors":"David Sheikh-Hamad, Michael Holliday, Qingtian Li","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The multi-ligand binding protein megalin (LRP2) is ubiquitously expressed and facilitates cell uptake of hormones, nutrients and vitamins. We have recently shown megalin is present in the mitochondria of cultured epithelial and mesenchymal cells, as well as many organs and tissues. Mitochondrial megalin associates with stanniocalcin-1 and SIRT3; two proteins that promote anti-oxidant defenses. Megalin shuttles mitochondrial intracrines (angiotensin II, stanniocalcin-1 and TGF-β) from the cell surface to the mitochondria through the retrograde early endosome to Golgi pathway and requires Rab32. Deletion of megalin impairs mitochondrial respiration and glycolysis. This pathway overlaps molecular and vesicular trafficking defects common to Donai Barrow and Lowe syndromes, suggesting that mitochondrial intracrine signaling defects may contribute to the pathogenesis of these diseases.</p>","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":"364-369"},"PeriodicalIF":0.0,"publicationDate":"2021-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8793748/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39873894","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Erwan Poivet, M. Daniel, F. Bozza, T. Sharshar, Pierre-Marie, Lledó
{"title":"Neurological Manifestations Associated with SARS-CoV-2 Invasion of the Autonomous Nervous System","authors":"Erwan Poivet, M. Daniel, F. Bozza, T. Sharshar, Pierre-Marie, Lledó","doi":"10.33696/immunology.3.107","DOIUrl":"https://doi.org/10.33696/immunology.3.107","url":null,"abstract":"Erwan Poivet1#, Matthieu Daniel2#, Fernando A. Bozza3, Tarek Sharshar2*, Pierre-Marie Lledo1* 1Laboratory for Perception and Memory, Institut Pasteur, CNRS UMR3571, 25, rue du Docteur Roux, Paris, 75724, Cedex 15, France 2Neuro-anesthesiology and Intensive Care Medicine, GHU-Psychiatrie et Neurosciences, Université de Paris, Paris, France 3National Institute of Infectious Diseases Evandro Chagas, Oswaldo Cruz Foundation (FIOCRUZ), and D’Or Institute for Research and Education (IDOR), Rio de Janeiro, Brazil #These authors contributed equally","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2021-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48247778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Commentary on “A Vaccine for Photodynamic Immunogenic Cell Death: Tumor Cell Caged b y Cellular Disulfide–Thiol Exchange for Immunotherapy”","authors":"J. Zang, Haiqing Dong","doi":"10.33696/immunology.3.109","DOIUrl":"https://doi.org/10.33696/immunology.3.109","url":null,"abstract":"Tumor immunotherapy, including monoclonal antibody of immune checkpoint blockade, therapeutic antibody, cancer vaccine and cell therapy, etc., is to restart and maintain the tumor immune cycle, restore the normal antitumor immune response of the body, so as to control and eliminate the tumor [1,2]. Among them, tumor vaccine, which can elicit robust immune response and produce sustained immune memory effect, is particularly favored in the treatment and prevention of tumor recurrence [3,4]. Notably, compared with specific antigen vaccine, whole cell vaccine does not need complex antigen screening and purification process, and can provide all antigens of specific tumor, so it has great prospects [5,6]. Nevertheless, the immune effect of whole cell vaccine is not satisfactory because of its low immunogenicity and limitation efficiency of antigen presentation [7,8].","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2021-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44565009","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
G. Zakiryanova, E. Kustova, N. Urazalieva, Emile T. Baimukhametov, V. A. Makarov, G. Shurin, Narymzhan N. Nakisbekov, M. Shurin
{"title":"Expression of Pu.1, C/Ebp? and Bach1 Transcription Factors in Immune Cells in Patients with Cancer","authors":"G. Zakiryanova, E. Kustova, N. Urazalieva, Emile T. Baimukhametov, V. A. Makarov, G. Shurin, Narymzhan N. Nakisbekov, M. Shurin","doi":"10.33696/immunology.3.106","DOIUrl":"https://doi.org/10.33696/immunology.3.106","url":null,"abstract":"Gulnur K. Zakiryanova1*, Elena Kustova2, Nataliya T. Urazalieva2, Emile T. Baimukhametov3, Valeriy A. Makarov4, Galina V. Shurin6, Narymzhan N. Nakisbekov5, Michael R. Shurin6* 1Al-Farabi Kazakh National University, Almaty, Kazakhstan 2Laboratory of Immunology, Scientific Center of Pediatric and Children Surgery, Almaty, Kazakhstan 3Kazakh Medical University of Continuing Education, Department of Oncology, Almaty, Kazakhstan 4Almaty Oncology Center, Department of Oncosurgery, Almaty, Kazakhstan 5Joint Use Center, Atchabarov Scientific Research Institute of Fundamental and Applied Medicine, Asfendiyarov Kazakh National Medical University, Almaty, Kazakhstan 6Departments of Pathology and Immunology, University of Pittsburgh Medical Center, Pittsburgh, PA, USA","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2021-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43441719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Novel Combination Treatments for AML","authors":"","doi":"10.33696/immunology.3.105","DOIUrl":"https://doi.org/10.33696/immunology.3.105","url":null,"abstract":"","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2021-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46340556","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ji Ma, Xianping Ma, Rang Wang, Fang Li, T. Hu, Huashan Yi
{"title":"Establishment of an Indirect Enzyme-linked Immunosorbent Assay for Detection of the NS4 Protein of Bluetongue Virus","authors":"Ji Ma, Xianping Ma, Rang Wang, Fang Li, T. Hu, Huashan Yi","doi":"10.33696/immunology.4.148","DOIUrl":"https://doi.org/10.33696/immunology.4.148","url":null,"abstract":"for Detection of the NS4","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2021-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46865439","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
W. L. Gluck, Wesley M. Smith, S. P. Callahan, Robert A. Brevetta, A. Stenbit, J. Martin, Anna V. Blenda, S. Arce, W. Edenfield
{"title":"Efficacy of Therapeutic Plasma Exchange Alone or in Combination with Ruxolitinib for the Treatment of Penn Class 3 and 4 Cytokine Release Syndrome Complicating COVID-19","authors":"W. L. Gluck, Wesley M. Smith, S. P. Callahan, Robert A. Brevetta, A. Stenbit, J. Martin, Anna V. Blenda, S. Arce, W. Edenfield","doi":"10.33696/immunology.3.100","DOIUrl":"https://doi.org/10.33696/immunology.3.100","url":null,"abstract":"Observations early in the viral pandemic of 2020 noted the resemblance between severe coronavirus disease 2019 (COVID-19) infection and the hypercytokinemic state of secondary hemophagocytic lymphohistiocytosis (sHLH) [1]. Conti and colleagues [2] have outlined the binding of COVID-19 to the Toll-like receptor with subsequent cytokine driven fever and pneumonitis, while in Kenderian’s [3] murine model of CRS, ruxolitinib abrogated the development of cytokine excess. Cao [4] reported faster clinical recovery with JAK inhibition and Capochiani’s RESPIRE trial reported an 89% overall response rate (ORR) with ruxolitinib therapy [5]. Discordant findings regarding JAK inhibition have been reported on the superiority of baricitinib plus remdesivir over remdesivir alone in shortening recovery times in hospitalized patients [6] while the randomized RUXCOVID trial failed to impact severe complications of the disease by adding ruxolitinib to standard of care [7]. Other groups [8,9] have reported inflammatory cytokine profiles along with evidence that elevated IL-6 and TNFα are strong predictors of disease severity and survival. While cytokine excess could be an epiphenomenal surrogate for another process, therapeutic strategies have evolved around addressing the excessive cytokine levels complicating a significant fraction of COVID-19 patients.","PeriodicalId":73644,"journal":{"name":"Journal of cellular immunology","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2021-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46372997","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}