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Article ; Online: Chronic lymphocytic leukemia transdifferentiated to blastic neoplasm with T/plasmacytoid dendritic cell immunophenotype.

Argyropoulos, Kimon V / Aypar, Umut / Ewalt, Mark D / Roshal, Mikhail / Dogan, Ahmet / Sen, Filiz

2023 Volume 64, Issue 3, Page(s) 734–737

MeSH term(s)	Humans ; Leukemia, Lymphocytic, Chronic, B-Cell/diagnosis ; Hematologic Neoplasms/genetics ; Leukocytes ; Dendritic Cells ; Skin Neoplasms
Language	English
Publishing date	2023-02-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	1042374-6
ISSN	1029-2403 ; 1042-8194
ISSN (online)	1029-2403
ISSN	1042-8194
DOI	10.1080/10428194.2022.2161819
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Article ; Online: Cytological features of NUT-carcinoma harbouring an NSD3-NUTM1 fusion.

Argyropoulos, Kimon V / Lin, Lawrence Hsu / Moreira, Andre L / Krock, Bryan / Simsir, Aylin / Brandler, Tamar C

Cytopathology : official journal of the British Society for Clinical Cytology

2022 Volume 33, Issue 4, Page(s) 540–543

MeSH term(s)	Carcinoma ; Humans ; Oncogene Proteins, Fusion/genetics ; Transcription Factors
Chemical Substances	Oncogene Proteins, Fusion ; Transcription Factors
Language	English
Publishing date	2022-04-04
Publishing country	England
Document type	Case Reports
ZDB-ID	1034190-0
ISSN	1365-2303 ; 0956-5507 ; 1350-4037
ISSN (online)	1365-2303
ISSN	0956-5507 ; 1350-4037
DOI	10.1111/cyt.13120
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Article ; Online: First-Generation and Second-Generation Bruton Tyrosine Kinase Inhibitors in Waldenström Macroglobulinemia.

Argyropoulos, Kimon V / Palomba, M Lia

Hematology/oncology clinics of North America

2018 Volume 32, Issue 5, Page(s) 853–864

Abstract: Waldenström macroglobulinemia (WM) is an indolent B-cell lymphoma that is heavily dependent on Bruton tyrosine kinase (BTK) hyperactivation. Ibrutinib is a first-generation BTK inhibitor that has shown high activity and durable responses in patients with ...

Abstract	Waldenström macroglobulinemia (WM) is an indolent B-cell lymphoma that is heavily dependent on Bruton tyrosine kinase (BTK) hyperactivation. Ibrutinib is a first-generation BTK inhibitor that has shown high activity and durable responses in patients with relapsed/refractory WM. Newer and more selective BTK inhibitors are currently being tested in several clinical trials and are expected to address the toxicity and the acquired resistance observed in patients receiving ibrutinib. Updates on ibrutinib and second-generation BTK inhibitors are summarized in this review.
MeSH term(s)	Agammaglobulinaemia Tyrosine Kinase/antagonists & inhibitors ; Agammaglobulinaemia Tyrosine Kinase/genetics ; Agammaglobulinaemia Tyrosine Kinase/metabolism ; Drug Resistance, Neoplasm/drug effects ; Drug Resistance, Neoplasm/genetics ; Humans ; Protein Kinase Inhibitors/therapeutic use ; Pyrazoles/therapeutic use ; Pyrimidines/therapeutic use ; Waldenstrom Macroglobulinemia/drug therapy ; Waldenstrom Macroglobulinemia/enzymology ; Waldenstrom Macroglobulinemia/genetics ; Waldenstrom Macroglobulinemia/pathology
Chemical Substances	Protein Kinase Inhibitors ; Pyrazoles ; Pyrimidines ; ibrutinib (1X70OSD4VX) ; Agammaglobulinaemia Tyrosine Kinase (EC 2.7.10.2)
Language	English
Publishing date	2018-07-19
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	93115-9
ISSN	1558-1977 ; 0889-8588
ISSN (online)	1558-1977
ISSN	0889-8588
DOI	10.1016/j.hoc.2018.05.012
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Article: Integrating Ligand-Receptor Interactions and In Vitro Evolution for Streamlined Discovery of Artificial Nucleic Acid Ligands.

Zumrut, Hasan E / Batool, Sana / Argyropoulos, Kimon V / Williams, Nicole / Azad, Roksana / Mallikaratchy, Prabodhika R

Molecular therapy. Nucleic acids

2019 Volume 17, Page(s) 150–163

Abstract: To discover DNA ligands against a predetermined receptor protein complex, we introduce a comprehensive version of ligand-guided selection (LIGS). LIGS is, itself, a variant of systematic evolution of ligands by exponential enrichment (SELEX). Herein, we ... ...

Abstract	To discover DNA ligands against a predetermined receptor protein complex, we introduce a comprehensive version of ligand-guided selection (LIGS). LIGS is, itself, a variant of systematic evolution of ligands by exponential enrichment (SELEX). Herein, we have optimized LIGS to identify higher affinity aptamers with high specificity. In addition, we demonstrate the expandability of LIGS by performing specific aptamer elution at 25°C, utilizing multiple monoclonal antibodies (mAbs) against cultured cells and primary cells obtained from human donors expressing the same receptor. Eluted LIGS libraries obtained through Illumina high-throughput (HT) DNA sequencing were analyzed by bioinformatics tools to discover five DNA aptamers with apparent affinities ranging from 3.06 ± 0.485 nM to 325 ± 62.7 nM against the target, T cell receptor-cluster of differentiation epsilon (TCR-CD3ε) expressed on human T cells. The specificity of the aptamers was validated utilizing multiple strategies, including competitive binding analysis and a double-knockout Jurkat cell line generated by CRISPR technology. The cross-competition experiments using labeled and unlabeled aptamers revealed that all five aptamers compete for the same binding site. Collectively, the data in this report introduce a modified LIGS strategy as a universal platform to identify highly specific multiple aptamers toward multi-component receptor proteins in their native state without changing the cell-surface landscape.
Language	English
Publishing date	2019-06-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2662631-7
ISSN	2162-2531
ISSN	2162-2531
DOI	10.1016/j.omtn.2019.05.015
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Article: Dimerization of an aptamer generated from Ligand-guided selection (LIGS) yields a high affinity scaffold against B-cells

Batool, Sana / Argyropoulos, Kimon V / Azad, Roksana / Okeoma, Precious / Zumrut, Hasan / Bhandari, Sanam / Dekhang, Rigzin / Mallikaratchy, Prabodhika R

Biochimica et biophysica acta. 2019 Jan., v. 1863, no. 1

2019

Abstract: Nucleic Acid Aptamers (NAAs) are a class of synthetic DNA or RNA molecules that bind specifically to their target. We recently introduced an aptamer termed R1.2 against membrane Immunoglobulin M (mIgM) expressing B-cell neoplasms using Ligand Guided ... ...

Abstract	Nucleic Acid Aptamers (NAAs) are a class of synthetic DNA or RNA molecules that bind specifically to their target. We recently introduced an aptamer termed R1.2 against membrane Immunoglobulin M (mIgM) expressing B-cell neoplasms using Ligand Guided Selection (LIGS). While LIGS-generated aptamers are highly specific, their lower affinity prevents aptamers from being used for translational applications. Highly specific aptamers with higher affinity can increase targetability, boosting the application of aptamers as diagnostic and therapeutic molecules. Herein, we report that dimerization of R1.2, an aptamer generated from LIGS, leads to high affinity variants without compromising the specificity. Three dimeric aptamer analogues with variable linker lengths were designed to evaluate the effect of linker length in affinity. The optimized dimeric R1.2 against cultured B-cell neoplasms, four donor B-cell samples and mIgM-positive Waldenström's Macroglobulinemia (WM) showed specificity. Furthermore, confocal imaging of dimeric aptamer and anti-IgM antibody in purified B-cells suggests co-localization. Binding assays against IgM knockout Burkitt's Lymphoma cells utilizing CRISPR/Cas9 further validated specificity of dimeric R1.2. Collectively, our findings show that LIGS-generated aptamers can be re-engineered into dimeric aptamers with high specificity and affinity, demonstrating wide-range of applicability of LIGS in developing clinically practical diagnostic and therapeutic aptamers.
Keywords	B-lymphocytes ; DNA ; RNA ; antibodies ; confocal microscopy ; dimerization ; image analysis ; immunoglobulin M ; ligands ; neoplasm cells ; neoplasms ; oligonucleotides ; therapeutics
Language	English
Dates of publication	2019-01
Size	p. 232-240.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	840755-1
ISSN	0304-4165
ISSN	0304-4165
DOI	10.1016/j.bbagen.2018.10.006
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Article ; Online: Autoimmune anti-DNA and anti-phosphatidylserine antibodies predict development of severe COVID-19.

Gomes, Claudia / Zuniga, Marisol / Crotty, Kelly A / Qian, Kun / Tovar, Nubia Catalina / Lin, Lawrence Hsu / Argyropoulos, Kimon V / Clancy, Robert / Izmirly, Peter / Buyon, Jill / Lee, David C / Yasnot-Acosta, Maria Fernanda / Li, Huilin / Cotzia, Paolo / Rodriguez, Ana

Life science alliance

2021 Volume 4, Issue 11

Abstract: High levels of autoimmune antibodies are observed in COVID-19 patients but their specific contribution to disease severity and clinical manifestations remains poorly understood. We performed a retrospective study of 115 COVID-19 hospitalized patients ... ...

Abstract	High levels of autoimmune antibodies are observed in COVID-19 patients but their specific contribution to disease severity and clinical manifestations remains poorly understood. We performed a retrospective study of 115 COVID-19 hospitalized patients with different degrees of severity to analyze the generation of autoimmune antibodies to common antigens: a lysate of erythrocytes, the lipid phosphatidylserine (PS) and DNA. High levels of IgG autoantibodies against erythrocyte lysates were observed in a large percentage (up to 36%) of patients. Anti-DNA and anti-PS antibodies determined upon hospital admission correlated strongly with later development of severe disease, showing a positive predictive value of 85.7% and 92.8%, respectively. Patients with positive values for at least one of the two autoantibodies accounted for 24% of total severe cases. Statistical analysis identified strong correlations between anti-DNA antibodies and markers of cell injury, coagulation, neutrophil levels and erythrocyte size. Anti-DNA and anti-PS autoantibodies may play an important role in the pathogenesis of COVID-19 and could be developed as predictive biomarkers for disease severity and specific clinical manifestations.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Antibodies, Antinuclear/blood ; Antibodies, Antinuclear/immunology ; Autoantibodies/blood ; Autoantibodies/immunology ; Biomarkers ; COVID-19/immunology ; COVID-19/metabolism ; DNA/chemistry ; DNA/immunology ; Erythrocytes/immunology ; Female ; Humans ; Male ; Middle Aged ; Phosphatidylserines/immunology ; Prognosis ; Retrospective Studies ; SARS-CoV-2/isolation & purification ; Severity of Illness Index
Chemical Substances	Antibodies, Antinuclear ; Autoantibodies ; Biomarkers ; Phosphatidylserines ; DNA (9007-49-2)
Language	English
Publishing date	2021-09-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202101180
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Article ; Online: Targeted genomic analysis of cutaneous T cell lymphomas identifies a subset with aggressive clinicopathological features.

Argyropoulos, Kimon V / Pulitzer, Melissa / Maura, Francesco / Mohanty, Abhinita / Mondello, Patrizia / Horwitz, Steven M / Myskowski, Patricia / Moskowitz, Alison / Dogan, Ahmet / Querfeld, Christiane / Rapaport, Franck / Siakantaris, Marina / Louis, Peter C / Galasso, Natasha / van den Brink, Marcel R M / Palomba, M Lia

Blood cancer journal

2020 Volume 10, Issue 11, Page(s) 116

MeSH term(s)	Aged ; Female ; Genomics ; Humans ; Lymphoma, T-Cell, Cutaneous/genetics ; Lymphoma, T-Cell, Cutaneous/metabolism ; Lymphoma, T-Cell, Cutaneous/pathology ; Male ; Middle Aged ; Skin Neoplasms/genetics ; Skin Neoplasms/metabolism ; Skin Neoplasms/pathology
Language	English
Publishing date	2020-11-09
Publishing country	United States
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2600560-8
ISSN	2044-5385 ; 2044-5385
ISSN (online)	2044-5385
ISSN	2044-5385
DOI	10.1038/s41408-020-00380-5
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Article ; Online: WITHDRAWN: ASSOCIATION OF INITIAL VIRAL LOAD IN SARS-CoV-2 PATIENTS WITH OUTCOME AND SYMPTOMS.

Argyropoulos, Kimon V / Serrano, Antonio / Hu, Jiyuan / Black, Margaret / Feng, Xiaojun / Shen, Guomiao / Call, Melissa / Kim, Min Jae / Lytle, Andrew / Belovarac, Brendan / Vougiouklakis, Theodore / Lin, Lawrence Hsu / Moran, Una / Heguy, Adriana / Troxel, Andrea / Snuderl, Matija / Osman, Iman / Cotzia, Paolo / Jour, George

The American journal of pathology

2020

Abstract: The Publisher regrets that this article is an accidental duplication of an article that has already been published, https://doi.org/10.1016/j.ajpath.2020.07.001. The duplicate article has therefore been withdrawn. The full Elsevier Policy on Article ... ...

Abstract	The Publisher regrets that this article is an accidental duplication of an article that has already been published, https://doi.org/10.1016/j.ajpath.2020.07.001. The duplicate article has therefore been withdrawn. The full Elsevier Policy on Article Withdrawal can be found at https://www.elsevier.com/about/our-business/policies/article-withdrawal.
Keywords	covid19
Language	English
Publishing date	2020-07-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2943-9
ISSN	1525-2191 ; 0002-9440
ISSN (online)	1525-2191
ISSN	0002-9440
DOI	10.1016/j.ajpath.2020.06.012
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Article ; Online: Dimerization of an aptamer generated from Ligand-guided selection (LIGS) yields a high affinity scaffold against B-cells.

Batool, Sana / Argyropoulos, Kimon V / Azad, Roksana / Okeoma, Precious / Zumrut, Hasan / Bhandari, Sanam / Dekhang, Rigzin / Mallikaratchy, Prabodhika R

Biochimica et biophysica acta. General subjects

2018 Volume 1863, Issue 1, Page(s) 232–240

Abstract	Nucleic Acid Aptamers (NAAs) are a class of synthetic DNA or RNA molecules that bind specifically to their target. We recently introduced an aptamer termed R1.2 against membrane Immunoglobulin M (mIgM) expressing B-cell neoplasms using Ligand Guided Selection (LIGS). While LIGS-generated aptamers are highly specific, their lower affinity prevents aptamers from being used for translational applications. Highly specific aptamers with higher affinity can increase targetability, boosting the application of aptamers as diagnostic and therapeutic molecules. Herein, we report that dimerization of R1.2, an aptamer generated from LIGS, leads to high affinity variants without compromising the specificity. Three dimeric aptamer analogues with variable linker lengths were designed to evaluate the effect of linker length in affinity. The optimized dimeric R1.2 against cultured B-cell neoplasms, four donor B-cell samples and mIgM-positive Waldenström's Macroglobulinemia (WM) showed specificity. Furthermore, confocal imaging of dimeric aptamer and anti-IgM antibody in purified B-cells suggests co-localization. Binding assays against IgM knockout Burkitt's Lymphoma cells utilizing CRISPR/Cas9 further validated specificity of dimeric R1.2. Collectively, our findings show that LIGS-generated aptamers can be re-engineered into dimeric aptamers with high specificity and affinity, demonstrating wide-range of applicability of LIGS in developing clinically practical diagnostic and therapeutic aptamers.
MeSH term(s)	Aptamers, Nucleotide/chemistry ; B-Lymphocytes/metabolism ; Burkitt Lymphoma/metabolism ; CRISPR-Cas Systems ; Cells, Cultured ; Dimerization ; Epitopes/chemistry ; HEK293 Cells ; Humans ; Immunoglobulin M/chemistry ; Lentivirus/genetics ; Leukocytes, Mononuclear/cytology ; Ligands ; Lymphoma, B-Cell/metabolism ; Plasmids/metabolism ; Protein Binding ; Protein Engineering ; Puromycin/chemistry ; SELEX Aptamer Technique ; Temperature ; Waldenstrom Macroglobulinemia/metabolism
Chemical Substances	Aptamers, Nucleotide ; Epitopes ; Immunoglobulin M ; Ligands ; Puromycin (4A6ZS6Q2CL)
Language	English
Publishing date	2018-10-17
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2018.10.006
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Article ; Online: A new role for the SRC family kinase HCK as a driver of SYK activation in MYD88 mutated lymphomas.

Blood advances

2022 Volume 6, Issue 11, Page(s) 3332–3338

Abstract: The SRC family kinase (SFK) HCK is transcriptionally upregulated and activated by mutated MYD88 (MYD88Mut), a key adaptor for Toll-receptor signaling. HCK activates BTK, AKT, and ERK in MYD88Mut lymphomas. SYK, a B-cell receptor (BCR) component, is ... ...

Abstract	The SRC family kinase (SFK) HCK is transcriptionally upregulated and activated by mutated MYD88 (MYD88Mut), a key adaptor for Toll-receptor signaling. HCK activates BTK, AKT, and ERK in MYD88Mut lymphomas. SYK, a B-cell receptor (BCR) component, is activated in MYD88Mut lymphoma cells. Although the SFK LYN serves as a trigger for SYK activation in MYD88Mut ABC DLBCL cells, LYN activity is muted in MYD88Mut Waldenstrom macroglobulinemia (WM) cells. We therefore investigated a role for HCK in mediating SYK activation. Overexpression of wild-type (WT) (HCKWT) or gatekeeper mutated (HCKThr333Met) HCK in MYD88Mut lymphoma cells triggered SYK activation. Conversely, HCK knockdown reduced p-SYK in MYD88Mut lymphoma cells. Coimmunoprecipitation experiments showed that HCK was complexed with p-SYK in MYD88Mut BCWM.1 and TMD8 cells, but not in MYD88 WT Ramos cells. Rescue experiments in MYD88Mut lymphoma cells expressing HCKThr333Met led to persistent HCK and SYK activation and resistance to the HCK inhibitor A419259. Treatment of primary MYD88Mut WM cells with A419259 reduced p-HCK and p-SYK expression. Taken together, our findings show that SYK is activated by HCK in MYD88Mut B-cell lymphomas cells, broaden the prosurvival signaling generated by aberrant HCK expression in response to MYD88Mut, and help define HCK as an important therapeutic target in MYD88Mut B-cell lymphomas.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Humans ; Lymphoma, B-Cell/enzymology ; Lymphoma, B-Cell/genetics ; Lymphoma, B-Cell/metabolism ; Myeloid Differentiation Factor 88/genetics ; Myeloid Differentiation Factor 88/metabolism ; Proto-Oncogene Proteins c-hck/metabolism ; Syk Kinase/genetics ; Syk Kinase/metabolism ; src-Family Kinases/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; MYD88 protein, human ; Myeloid Differentiation Factor 88 ; HCK protein, human (EC 2.7.10.2) ; Proto-Oncogene Proteins c-hck (EC 2.7.10.2) ; SYK protein, human (EC 2.7.10.2) ; Syk Kinase (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2)
Language	English
Publishing date	2022-03-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2915908-8
ISSN	2473-9537 ; 2473-9529
ISSN (online)	2473-9537
ISSN	2473-9529
DOI	10.1182/bloodadvances.2021006147
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