Smarcc1 Crebbp Smarcc1 Ar Smarcc1 Gata1 Smarcc1
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Peripheral T Cells Ets-1 Maintains IL-7 Receptor Expression In
The Journal of Immunology Ets-1 Maintains IL-7 Receptor Expression in Peripheral T Cells Roland Grenningloh,*,† Tzong-Shyuan Tai,* Nicole Frahm,†,‡,1 Tomoyuki C. Hongo,‡ Adam T. Chicoine,‡ Christian Brander,†,‡,x,{ Daniel E. Kaufmann,†,‡,‖ and I-Cheng Ho*,† The expression of CD127, the IL-7–binding subunit of the IL-7 R, is tightly regulated during the development and activation of T cells and is reduced during chronic viral infection. However, the molecular mechanism regulating the dynamic expression of CD127 is still poorly understood. In this study, we report that the transcription factor Ets-1 is required for maintaining the expression of CD127 in murine peripheral T cells. Ets-1 binds to and activates the CD127 promoter, and its absence leads to reduced CD127 expression, attenuated IL-7 signaling, and impaired IL-7–dependent homeostatic proliferation of T cells. The expression of CD127 and Ets-1 is strongly correlated in human T cells. Both CD127 and Ets-1 expression are decreased in CD8+ T cells during HIV infection. In addition, HIV-associated loss of CD127 is only observed in Ets-1low effector memory and central memory but not in Ets-1high naive CD8+ T cells. Taken together, our data identify Ets-1 as a critical regulator of CD127 expression in T cells. The Journal of Immunology, 2011, 186: 969–976. nterleukin-7 signals are required for T cell development, GABPa or another Ets protein is responsible for maintaining maintaining the naive T cell pool, mounting proper primary CD127 expression in peripheral T cells is unknown. I responses, and inducing and maintaining CD4+ and CD8+ Ets-1 (E26 transformation-specific sequence) is the founding T cell memory (1–3). -
Human RET Kinase Protein (His Tag)
Human RET Kinase Protein (His Tag) Catalog Number: 11997-H08H1 General Information SDS-PAGE: Gene Name Synonym: CDHF12; CDHR16; HSCR1; MEN2A; MEN2B; MTC1; PTC; RET-ELE1; RET51 Protein Construction: A DNA sequence encoding the extracellular domain of human RET (P07949-1) (Met 1-Arg 635) was fused with a polyhistidine tag at the N- terminus. Source: Human Expression Host: HEK293 Cells QC Testing Purity: > 92 % as determined by SDS-PAGE Protein Description Endotoxin: RET proto-oncogene, also known as RET, is a cell-surface molecule that < 1.0 EU per μg of the protein as determined by the LAL method transduce signals for cell growth and differentiation. It contains 1 cadherin domain and 1 protein kinase domain. RET proto-oncogene belongs to the Stability: protein kinase superfamily, tyr protein kinase family. RET proto-oncogene is involved in numerous cellular mechanisms including cell proliferation, ℃ Samples are stable for up to twelve months from date of receipt at -70 neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. It phosphorylates Leu 29 Predicted N terminal: PTK2/FAK1 and regulates both cell death/survival balance and positional Molecular Mass: information. RET is required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric The recombinant human RET consists of 618 amino acids and has a nervous system and renal organogenesis during embryonic life; promotes calculated molecular mass of 69.1 kDa. The apparent molecular mass of the formation of Peyer's patch-like structures; modulates cell adhesion via the protein is approximately 110-120 kDa in SDS-PAGE under reducing its cleavage; involved in the development of the neural crest. -
Promoter Janus Kinase 3 Proximal Characterization and Analysis Of
The Journal of Immunology Characterization and Analysis of the Proximal Janus Kinase 3 Promoter1 Martin Aringer,2*† Sigrun R. Hofmann,2* David M. Frucht,* Min Chen,* Michael Centola,* Akio Morinobu,* Roberta Visconti,* Daniel L. Kastner,* Josef S. Smolen,† and John J. O’Shea3* Janus kinase 3 (Jak3) is a nonreceptor tyrosine kinase essential for signaling via cytokine receptors that comprise the common ␥-chain (␥c), i.e., the receptors for IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is preferentially expressed in hemopoietic cells and is up-regulated upon cell differentiation and activation. Despite the importance of Jak3 in lymphoid development and immune function, the mechanisms that govern its expression have not been defined. To gain insight into this issue, we set out to characterize the Jak3 promoter. The 5-untranslated region of the Jak3 gene is interrupted by a 3515-bp intron. Upstream of this intron and the transcription initiation site, we identified an ϳ1-kb segment that exhibited lymphoid-specific promoter activity and was responsive to TCR signals. Truncation of this fragment revealed that core promoter activity resided in a 267-bp fragment that contains putative Sp-1, AP-1, Ets, Stat, and other binding sites. Mutation of the AP-1 sites significantly diminished, whereas mutation of the Ets sites abolished, the inducibility of the promoter construct. Chromatin immunoprecipitation assays showed that histone acetylation correlates with mRNA expression and that Ets-1/2 binds this region. Thus, transcription factors that bind these sites, especially Ets family members, are likely to be important regulators of Jak3 expression. -
Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse
Welcome to More Choice CD Marker Handbook For more information, please visit: Human bdbiosciences.com/eu/go/humancdmarkers Mouse bdbiosciences.com/eu/go/mousecdmarkers Human and Mouse CD Marker Handbook Human and Mouse CD Marker Key Markers - Human Key Markers - Mouse CD3 CD3 CD (cluster of differentiation) molecules are cell surface markers T Cell CD4 CD4 useful for the identification and characterization of leukocytes. The CD CD8 CD8 nomenclature was developed and is maintained through the HLDA (Human Leukocyte Differentiation Antigens) workshop started in 1982. CD45R/B220 CD19 CD19 The goal is to provide standardization of monoclonal antibodies to B Cell CD20 CD22 (B cell activation marker) human antigens across laboratories. To characterize or “workshop” the antibodies, multiple laboratories carry out blind analyses of antibodies. These results independently validate antibody specificity. CD11c CD11c Dendritic Cell CD123 CD123 While the CD nomenclature has been developed for use with human antigens, it is applied to corresponding mouse antigens as well as antigens from other species. However, the mouse and other species NK Cell CD56 CD335 (NKp46) antibodies are not tested by HLDA. Human CD markers were reviewed by the HLDA. New CD markers Stem Cell/ CD34 CD34 were established at the HLDA9 meeting held in Barcelona in 2010. For Precursor hematopoetic stem cell only hematopoetic stem cell only additional information and CD markers please visit www.hcdm.org. Macrophage/ CD14 CD11b/ Mac-1 Monocyte CD33 Ly-71 (F4/80) CD66b Granulocyte CD66b Gr-1/Ly6G Ly6C CD41 CD41 CD61 (Integrin b3) CD61 Platelet CD9 CD62 CD62P (activated platelets) CD235a CD235a Erythrocyte Ter-119 CD146 MECA-32 CD106 CD146 Endothelial Cell CD31 CD62E (activated endothelial cells) Epithelial Cell CD236 CD326 (EPCAM1) For Research Use Only. -
Human Prion-Like Proteins and Their Relevance in Disease
ADVERTIMENT. Lʼaccés als continguts dʼaquesta tesi queda condicionat a lʼacceptació de les condicions dʼús establertes per la següent llicència Creative Commons: http://cat.creativecommons.org/?page_id=184 ADVERTENCIA. El acceso a los contenidos de esta tesis queda condicionado a la aceptación de las condiciones de uso establecidas por la siguiente licencia Creative Commons: http://es.creativecommons.org/blog/licencias/ WARNING. The access to the contents of this doctoral thesis it is limited to the acceptance of the use conditions set by the following Creative Commons license: https://creativecommons.org/licenses/?lang=en Universitat Autònoma de Barcelona Departament de Bioquímica i Biologia Molecular Institut de Biotecnologia i Biomedicina HUMAN PRION-LIKE PROTEINS AND THEIR RELEVANCE IN DISEASE Doctoral thesis presented by Cristina Batlle Carreras for the degree of PhD in Biochemistry, Molecular Biology and Biomedicine from the Universitat Autònoma de Barcelona. The work described herein has been performed in the Department of Biochemistry and Molecular Biology and in the Institute of Biotechnology and Biomedicine, supervised by Prof. Salvador Ventura i Zamora. Cristina Batlle Carreras Prof. Salvador Ventura i Zamora Bellaterra, 2020 Protein Folding and Conformational Diseases Lab. This work was financed with the fellowship “Formación de Profesorado Universitario” by “Ministerio de Ciencia, Innovación y Universidades”. This work is licensed under a Creative Commons Attributions-NonCommercial-ShareAlike 4.0 (CC BY-NC- SA 4.0) International License. The extent of this license does not apply to the copyrighted publications and images reproduced with permission. (CC BY-NC-SA 4.0) Batlle, Cristina: Human prion-like proteins and their relevance in disease. Doctoral Thesis, Universitat Autònoma de Barcelona (2020) English summary ENGLISH SUMMARY Prion-like proteins have attracted significant attention in the last years. -
SF3B3) and Sin3a Associated Protein 130 (SAP130
cells Communication Ambiguity about Splicing Factor 3b Subunit 3 (SF3B3) and Sin3A Associated Protein 130 (SAP130) Paula I. Metselaar 1,* , Celine Hos 1, Olaf Welting 1, Jos A. Bosch 2,3, Aletta D. Kraneveld 4 , Wouter J. de Jonge 1 and Anje A. Te Velde 1 1 Tytgat Institute for Liver and Intestinal Research, AGEM, Amsterdam UMC, University of Amsterdam, 1105BK Amsterdam, The Netherlands; [email protected] (C.H.); [email protected] (O.W.); [email protected] (W.J.d.J.); [email protected] (A.A.T.V.) 2 Department of Psychology, University of Amsterdam, 1018WS Amsterdam, The Netherlands; [email protected] 3 Department of Medical Psychology, Amsterdam UMC, University of Amsterdam, 1001NK Amsterdam, The Netherlands 4 Division of Pharmacology, Utrecht Institute for Pharmaceutical Sciences, Faculty of Science, Utrecht University, 3584CG Utrecht, The Netherlands; [email protected] * Correspondence: [email protected] Abstract: In 2020, three articles were published on a protein that can activate the immune system by binding to macrophage-inducible C-type lectin receptor (Mincle). In the articles, the protein was referred to as ‘SAP130, a subunit of the histone deacetylase complex.’ However, the Mincle ligand the authors aimed to investigate is splicing factor 3b subunit 3 (SF3B3). This splicing factor is unrelated to SAP130 (Sin3A associated protein 130, a subunit of the histone deacetylase-dependent Sin3A corepressor complex). The conclusions in the three articles were formulated for SF3B3, Citation: Metselaar, P.I.; Hos, C.; while the researchers used qPCR primers and antibodies against SAP130. -
A Pathogenic Ctbp1 Missense Mutation Causes Altered Cofactor Binding and Transcriptional Activity
neurogenetics (2019) 20:129–143 https://doi.org/10.1007/s10048-019-00578-1 ORIGINAL ARTICLE A pathogenic CtBP1 missense mutation causes altered cofactor binding and transcriptional activity David B. Beck1 & T. Subramanian2 & S. Vijayalingam2 & Uthayashankar R. Ezekiel3 & Sandra Donkervoort4 & Michele L. Yang5 & Holly A. Dubbs6 & Xilma R. Ortiz-Gonzalez7 & Shenela Lakhani8 & Devorah Segal9 & Margaret Au10 & John M. Graham Jr10 & Sumit Verma11 & Darrel Waggoner12 & Marwan Shinawi13 & Carsten G. Bönnemann4 & Wendy K. Chung14 & G. Chinnadurai2 Received: 23 October 2018 /Revised: 18 March 2019 /Accepted: 9 April 2019 /Published online: 30 April 2019 # Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract We previously reported a pathogenic de novo p.R342W mutation in the transcriptional corepressor CTBP1 in four independent patients with neurodevelopmental disabilities [1]. Here, we report the clinical phenotypes of seven additional individuals with the same recurrent de novo CTBP1 mutation. Within this cohort, we identified consistent CtBP1-related phenotypes of intellectual disability, ataxia, hypotonia, and tooth enamel defects present in most patients. The R342W mutation in CtBP1 is located within a region implicated in a high affinity-binding cleft for CtBP-interacting proteins. Unbiased proteomic analysis demonstrated reduced interaction of several chromatin-modifying factors with the CtBP1 W342 mutant. Genome-wide transcriptome analysis in human glioblastoma cell lines expressing -CtBP1 R342 (wt) or W342 mutation revealed changes in the expression profiles of genes controlling multiple cellular processes. Patient-derived dermal fibroblasts were found to be more sensitive to apoptosis during acute glucose deprivation compared to controls. Glucose deprivation strongly activated the BH3-only pro-apoptotic gene NOXA, suggesting a link between enhanced cell death and NOXA expression in patient fibroblasts. -
CRKL As a Lung Cancer Oncogene and Mediator Of
views in The spotliGhT CRKL as a Lung Cancer Oncogene and Mediator of Acquired Resistance to eGFR inhibitors: is it All That it is Cracked Up to Be? Marc Ladanyi summary: Cheung and colleagues demonstrate that amplified CRKL can function as a driver oncogene in lung adeno- carcinoma, activating both RAS and RAP1 to induce mitogen-activated protein kinase signaling. In addition, they show that CRKL amplification may be another mechanism for primary or acquired resistance to epidermal growth factor re- ceptor kinase inhibitors. Cancer Discovery; 1(7); 560–1. ©2011 AACR. Commentary on Cheung et al., p. 608 (1). In this issue of Cancer Discovery, Cheung and colleagues (1) mutual exclusivity. Cheung and colleagues (1) report that present extensive genomic and functional data supporting focal CRKL amplification is mutually exclusive with EGFR focal amplification of the CRKL gene at 22q11.21 as a driver mutation and EGFR amplification. However, of the 6 lung oncogene in lung adenocarcinoma. The report expands on cancer cell lines found in this study to have focal gains of data previously presented by Kim and colleagues (2). CRKL CRKL, 2 contain other major driver oncogenes (KRAS G13D is a signaling adaptor protein that contains SH2 and SH3 in HCC515, BRAF G469A in H1755; refs. 7, 8). Interestingly, domains that mediate protein–protein interactions linking both cell lines demonstrated clear dependence on CRKL in tyrosine-phosphorylated upstream signaling molecules (e.g., functional assays. Perhaps CRKL amplification is more akin BCAR1, paxillin, GAB1) to downstream effectors (e.g., C3G, to PIK3CA mutations, which often, but not always, are con- SOS) (3). -
PTK2B (Human) Recombinant Protein
PTK2B (Human) Recombinant PKB, PTK, PYK2, RAFTK Protein Gene Summary: This gene encodes a cytoplasmic protein tyrosine kinase which is involved in Catalog Number: P5800 calcium-induced regulation of ion channels and Regulation Status: For research use only (RUO) activation of the map kinase signaling pathway. The encoded protein may represent an important signaling Product Description: Human PTK2B (NP_775267.1, 1 intermediate between neuropeptide-activated receptors a.a. - 967 a.a.) full-length recombinant protein with GST or neurotransmitters that increase calcium flux and the tag expressed in Baculovirus infected Sf21 cells. downstream signals that regulate neuronal activity. The encoded protein undergoes rapid tyrosine Host: Insect phosphorylation and activation in response to increases in the intracellular calcium concentration, nicotinic Theoretical MW (kDa): 138 acetylcholine receptor activation, membrane depolarization, or protein kinase C activation. This Applications: Func, SDS-PAGE protein has been shown to bind CRK-associated (See our web site product page for detailed applications substrate, nephrocystin, GTPase regulator associated information) with FAK, and the SH2 domain of GRB2. The encoded protein is a member of the FAK subfamily of protein Protocols: See our web site at tyrosine kinases but lacks significant sequence similarity http://www.abnova.com/support/protocols.asp or product to kinases from other subfamilies. Four transcript page for detailed protocols variants encoding two different isoforms have been Form: Liquid found for this gene. [provided by RefSeq] Preparation Method: Baculovirus infected insect cell (Sf21) expression system Purification: Glutathione sepharose chromatography Purity: 74 % by SDS-PAGE/CBB staining Activity: The activity was measured by off-chip mobility shift assay. -
Mediator of DNA Damage Checkpoint 1 (MDC1) Is a Novel Estrogen Receptor Co-Regulator in Invasive 6 Lobular Carcinoma of the Breast 7 8 Evelyn K
bioRxiv preprint doi: https://doi.org/10.1101/2020.12.16.423142; this version posted December 16, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. 1 Running Title: MDC1 co-regulates ER in ILC 2 3 Research article 4 5 Mediator of DNA damage checkpoint 1 (MDC1) is a novel estrogen receptor co-regulator in invasive 6 lobular carcinoma of the breast 7 8 Evelyn K. Bordeaux1+, Joseph L. Sottnik1+, Sanjana Mehrotra1, Sarah E. Ferrara2, Andrew E. Goodspeed2,3, James 9 C. Costello2,3, Matthew J. Sikora1 10 11 +EKB and JLS contributed equally to this project. 12 13 Affiliations 14 1Dept. of Pathology, University of Colorado Anschutz Medical Campus 15 2Biostatistics and Bioinformatics Shared Resource, University of Colorado Comprehensive Cancer Center 16 3Dept. of Pharmacology, University of Colorado Anschutz Medical Campus 17 18 Corresponding author 19 Matthew J. Sikora, PhD.; Mail Stop 8104, Research Complex 1 South, Room 5117, 12801 E. 17th Ave.; Aurora, 20 CO 80045. Tel: (303)724-4301; Fax: (303)724-3712; email: [email protected]. Twitter: 21 @mjsikora 22 23 Authors' contributions 24 MJS conceived of the project. MJS, EKB, and JLS designed and performed experiments. JLS developed models 25 for the project. EKB, JLS, SM, and AEG contributed to data analysis and interpretation. SEF, AEG, and JCC 26 developed and performed informatics analyses. MJS wrote the draft manuscript; all authors read and revised the 27 manuscript and have read and approved of this version of the manuscript. -
Supplementary Table S1. Control Capsules (CC) and Study Capsules (CR) Composition
Supplementary Table S1. Control Capsules (CC) and Study Capsules (CR) composition CC Capsules Composition mg Bioactive compound Sunflower oil 1.100 Gelatin 318,019 Glycerin 118,750 Clorophill E-140 1,923 CAPSULE TOTAL WEIGHT 1.538,692 CR Capsules Composition mg Bioactive compound Shark liver oil 20% 750 150 mg alkylglycerols alkylglycerols (Gustav Heess) Rosemary Antioxidant 11,25 mg Diterpene Phenols extract, 25 % Diterpene 45 Phenols, Type Nº 027.020 (Rosmarinus officinalis L.) Glyceril-monoestearate 30 Sunflower oil 263 Soy lecithin VEROLEC 56 12 Gelatin 318,019 Glycerin 118,750 Clorophill E-140 1,923 CAPSULE TOTAL WEIGHT 1.538,692 Supplementary Table S2. Table of the selected genes and pathways analyzed in the study Pathway Gen Gene name Inflammation, IL1B Interleukin 1, Beta Immunomodulation TNF (TNFA) Tumor Necrosis Factor MAPK1 Mitogen-Activated Protein Kinase 1 PTK2B Protein Tyrosine Kinase 2 Beta STAT3 Signal Transducer Activator Of Transcription 3 JAK1 Janus Kinase 1 JAK3 Janus Kinase 3 NFKB Nuclear Factor Of Kappa Light Polypeptide Gene Enhancer In B-Cells 1 NLRP3 NLR Family, Pyrin Domain Containing 3 CCL2 (MCP-1) Chemokine (C-C Motif) Ligand 2 CXCR1 Chemokine (C-X-C Motif) Receptor 1 CSF2 Colony Stimulating Factor 2 (Granulocyte-Macrophage) CCL5(RANTES) Chemokine (C-C Motif) Ligand 5 CCR5 Chemokine (C-C Motif) Receptor 5 (Gene/Pseudogene) PLCG1 Phospholipase C, Gamma 1 PRKCD Protein Kinase C, Delta ADIPOQ Adiponectin, C1Q And Collagen Domain Containing BMP2 Bone Morphogenetic Protein 2 LIF Leukemia Inhibitory Factor TGFB2 -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.