Transforming Growth Factor Β Signaling in Uterine Development and Function Qinglei Li
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Gene Symbol Gene Description ACVR1B Activin a Receptor, Type IB
Table S1. Kinase clones included in human kinase cDNA library for yeast two-hybrid screening Gene Symbol Gene Description ACVR1B activin A receptor, type IB ADCK2 aarF domain containing kinase 2 ADCK4 aarF domain containing kinase 4 AGK multiple substrate lipid kinase;MULK AK1 adenylate kinase 1 AK3 adenylate kinase 3 like 1 AK3L1 adenylate kinase 3 ALDH18A1 aldehyde dehydrogenase 18 family, member A1;ALDH18A1 ALK anaplastic lymphoma kinase (Ki-1) ALPK1 alpha-kinase 1 ALPK2 alpha-kinase 2 AMHR2 anti-Mullerian hormone receptor, type II ARAF v-raf murine sarcoma 3611 viral oncogene homolog 1 ARSG arylsulfatase G;ARSG AURKB aurora kinase B AURKC aurora kinase C BCKDK branched chain alpha-ketoacid dehydrogenase kinase BMPR1A bone morphogenetic protein receptor, type IA BMPR2 bone morphogenetic protein receptor, type II (serine/threonine kinase) BRAF v-raf murine sarcoma viral oncogene homolog B1 BRD3 bromodomain containing 3 BRD4 bromodomain containing 4 BTK Bruton agammaglobulinemia tyrosine kinase BUB1 BUB1 budding uninhibited by benzimidazoles 1 homolog (yeast) BUB1B BUB1 budding uninhibited by benzimidazoles 1 homolog beta (yeast) C9orf98 chromosome 9 open reading frame 98;C9orf98 CABC1 chaperone, ABC1 activity of bc1 complex like (S. pombe) CALM1 calmodulin 1 (phosphorylase kinase, delta) CALM2 calmodulin 2 (phosphorylase kinase, delta) CALM3 calmodulin 3 (phosphorylase kinase, delta) CAMK1 calcium/calmodulin-dependent protein kinase I CAMK2A calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha CAMK2B calcium/calmodulin-dependent -
Recombinant Human TGF-Beta 2 Protein
ACROBiosystems Recombinant Human TGF-Beta 2 Protein Cat. # TG2-H4213 For Research and Further Cell Culture Manufacturing Use Source: Bioactivity: Recombinant Human TGF Beta 2 Protein (rhTGFB2) The bio-activity was determined by its ability to Ala 303 - Ser 414 (Accession # NP_003229.1) was inhibit IL-4 induced HT-2 cell proliferation. ED50<0.1 produced in human HEK293 cells at ACRObiosystems. ng/ml, corresponding to a specific activity of >1X107 Unit/mg Molecular Characterization: Formulation: rhTGFB2 contains no “tags” and has a calculated MW of 12.7 kDa (monomer). DTT-reduced protein migrates Lyophilized from 0.22 μm filtered solution in TFA, as a 13 kDa polypeptide and the non-reduced cystine- acetonitrile. Normally Mannitol or Trehalose are linked homodimer migrates as a 25 kDa protein. added as protectants before lyophilization. Contact us for customized product format or Endotoxin: formulation. Less than 1.0 EU per μg of the rhTGFB2 by the LAL Reconstitution : method. See Certificate of Analysis for details of Purity: reconstitution instruction and specific concentration. >98% as determined by SDS-PAGE of reduced (+) and Storage: non-reduced (-) rhTGFB2. Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at: SDS-PAGE: • 4-8℃ for 1 year in lyophilized state The purity of rhTGFB2 • 4-8℃ for 1 month under sterile conditions after was determined by SDS- reconstitution PAGE of reduced (+) and • -20 ℃ to -70 ℃ for 3 months under sterile non-reduced (-) rhTGFB2 conditions after reconstitution and staining overnight with Coomassie Blue. Background: Transforming growth factor beta 2 ( TGFB2) is also known as TGF-β2, TGF-beta2, Glioblastoma-derived T-cell suppressor factor, G-TSF, BSC-1 cell growth inhibitor, Polyergin, Cetermin, and is a polypeptide member of the transforming growth factor beta superfamily of cytokines. -
ACVR1 Antibody Cat
ACVR1 Antibody Cat. No.: 4791 Western blot analysis of ACVR1 in A549 cell lysate with ACVR1 antibody at 1 μg/mL in (A) the absence and (B) the presence of blocking peptide. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse HOMOLOGY: Predicted species reactivity based on immunogen sequence: Bovine: (100%), Rat: (93%) ACVR1 antibody was raised against a 14 amino acid synthetic peptide near the amino terminus of the human ACVR1. IMMUNOGEN: The immunogen is located within the first 50 amino acids of ACVR1. TESTED APPLICATIONS: ELISA, WB ACVR1 antibody can be used for detection of ACVR1 by Western blot at 1 μg/mL. APPLICATIONS: Antibody validated: Western Blot in human samples. All other applications and species not yet tested. At least four isoforms of ACVR1 are known to exist. This antibody is predicted to have no SPECIFICITY: cross-reactivity to ACVR1B or ACVR1C. POSITIVE CONTROL: 1) Cat. No. 1203 - A549 Cell Lysate Properties October 1, 2021 1 https://www.prosci-inc.com/acvr1-antibody-4791.html PURIFICATION: ACVR1 Antibody is affinity chromatography purified via peptide column. CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: ACVR1 Antibody is supplied in PBS containing 0.02% sodium azide. CONCENTRATION: 1 mg/mL ACVR1 antibody can be stored at 4˚C for three months and -20˚C, stable for up to one STORAGE CONDITIONS: year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Additional Info OFFICIAL SYMBOL: ACVR1 ACVR1 Antibody: FOP, ALK2, SKR1, TSRI, ACTRI, ACVR1A, ACVRLK2, Activin receptor type-1, ALTERNATE NAMES: Activin receptor type I, ACTR-I ACCESSION NO.: NP_001096 PROTEIN GI NO.: 4501895 GENE ID: 90 USER NOTE: Optimal dilutions for each application to be determined by the researcher. -
Role of TGF-Β3 in the Regulation of Immune Responses T
Role of TGF-β3 in the regulation of immune responses T. Okamura1,2, K. Morita1, Y. Iwasaki1, M. Inoue1, T. Komai1, K. Fujio1, K. Yamamoto1 1Department of Allergy and ABSTRACT ences, indicating their non-redundancy Rheumatology, Graduate School of Transforming growth factor-betas (12-16). The TGF-βs have opposite ef- Medicine, The University of Tokyo, (TGF-βs) are multifunctional cytokines fects on tissue fibrosis. Wound-healing Tokyo, Japan; that have been implicated in the regu- experiments revealed that TGF-β1 2Max Planck-The University of Tokyo Center for Integrative Inflammology, lation of a broad range of biological and TGF-β2 cause fibrotic scarring The University of Tokyo, Tokyo, Japan. processes, including cell proliferation, responses and that TGF-β3 induces a Tomohisa Okamura, MD, PhD cell survival, and cell differentiation. scar-free response (17). Both TGF-β1 Kaoru Morita, MD The three isoforms identified in mam- and -β2 activate the collagen α2 (I) Yukiko Iwasaki, MD, PhD mals, TGF-β1, TGF-β2, and TGF-β3, gene promoter, resulting in increased Mariko Inoue, MD have high sequence homology, bind to collagen synthesis (18). It was also re- Toshihiko Komai, MD the same receptors, and show similar ported that TGF-β1, but not TGF-β3, is Keishi Fujio, MD, PhD biological functions in many in vitro a crucial factor in the development of Kazuhiko Yamamoto, MD, PhD studies. However, analysis of the in vivo pulmonary fibrosis (19). Most of the in- Please address correspondence to: functions of the three isoforms and mice formation on the immunological activ- Keishi Fujio, MD, PhD, deficient for each cytokine reveals strik- Department of Allergy and ity of TGF-βs derives from studies of Rheumatology, ing differences, illustrating their unique TGF-β1 and, in part, TGF-β2, whereas Graduate School of Medicine, biological importance and functional recent investigations have begun to il- The University of Tokyo, non-redundancy. -
Signal Transduction Pathway Through Activin Receptors As a Therapeutic Target of Musculoskeletal Diseases and Cancer
Endocr. J./ K. TSUCHIDA et al.: SIGNALING THROUGH ACTIVIN RECEPTORS doi: 10.1507/endocrj.KR-110 REVIEW Signal Transduction Pathway through Activin Receptors as a Therapeutic Target of Musculoskeletal Diseases and Cancer KUNIHIRO TSUCHIDA, MASASHI NAKATANI, AKIYOSHI UEZUMI, TATSUYA MURAKAMI AND XUELING CUI Division for Therapies against Intractable Diseases, Institute for Comprehensive Medical Science (ICMS), Fujita Health University, Toyoake, Aichi 470-1192, Japan Received July 6, 2007; Accepted July 12, 2007; Released online September 14, 2007 Correspondence to: Kunihiro TSUCHIDA, Institute for Comprehensive Medical Science (ICMS), Fujita Health University, Toyoake, Aichi 470-1192, Japan Abstract. Activin, myostatin and other members of the TGF-β superfamily signal through a combination of type II and type I receptors, both of which are transmembrane serine/threonine kinases. Activin type II receptors, ActRIIA and ActRIIB, are primary ligand binding receptors for activins, nodal, myostatin and GDF11. ActRIIs also bind a subset of bone morphogenetic proteins (BMPs). Type I receptors that form complexes with ActRIIs are dependent on ligands. In the case of activins and nodal, activin receptor-like kinases 4 and 7 (ALK4 and ALK7) are the authentic type I receptors. Myostatin and GDF11 utilize ALK5, although ALK4 could also be activated by these growth factors. ALK4, 5 and 7 are structurally and functionally similar and activate receptor-regulated Smads for TGF-β, Smad2 and 3. BMPs signal through a combination of three type II receptors, BMPRII, ActRIIA, and ActRIIB and three type I receptors, ALK2, 3, and 6. BMPs activate BMP-specific Smads, Smad1, 5 and 8. Smad proteins undergo multimerization with co-mediator Smad, Smad4, and translocated into the nucleus to regulate the transcription of target genes in cooperation with nuclear cofactors. -
Transforming Growth Factor-Β Soluble Receptor III (TGF-Β Sriii)
Transforming Growth Factor-b Soluble Receptor III (TGF-b sRIII) Human, Recombinant Expressed in mouse NSO cells Product Number T4567 Product Description Reagent Transforming Growth Factor-b soluble Receptor III Recombinant human TGF-b sRIII is supplied as (TGF-b sRIII) is produced from a DNA sequence approximately 100 mg of protein lyophilized from a encoding the amino terminal (781 amino acid residue) 0.2 mm filtered solution in phosphate buffered saline extracellular domain of human TGF-b receptor type III (PBS) containing 5 mg of bovine serum albumin. protein.1 Mature human TGF-b sRIII, a 760 amino acid residue protein generated after cleavage of a 21 amino Preparation Instructions acid residue signal peptide, has a predicted molecular Reconstitute the contents of the vial using sterile mass of approximately 84 kDa. As a result of glycosy- phosphate-buffered saline (PBS) containing at least lation, recombinant TGF-b sRIII migrates as a 100 kDa 0.1% human serum albumin or bovine serum albumin. protein in SDS-PAGE. Prepare a stock solution of no less than 20 mg/ml. The transforming growth factor-b (TGF-b) family of Storage/Stability cytokines are multifunctional peptides; capable of Store at -20 °C. Upon reconstitution, store at 2 °C to influencing cell proliferation, growth, differentiation, and 8 °C for one month. For extended storage, freeze in other functions in a wide range of cell types. Most working aliquots. Repeated freezing and thawing is not mammalian cells express three abundant high affinity recommended. Do not store in a frost-free freezer. TGF receptors, which can bind and be cross-linked to 2 TGF-b. -
Lack of Tgfbr1 and Acvr1b Synergistically Stimulates Myofibre Hypertrophy And
bioRxiv preprint doi: https://doi.org/10.1101/2021.03.03.433740; this version posted March 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Lack of Tgfbr1 and Acvr1b synergistically stimulates myofibre hypertrophy and accelerates muscle regeneration *M.M.G. Hillege1, *A. Shi1,2 ,3, R.C. Galli Caro1, G. Wu4, P. Bertolino5, W.M.H. Hoogaars1,6, R.T. Jaspers1 1. Laboratory for Myology, Department of Human Movement Sciences, Faculty of Behavioural and Movement Sciences, Vrije Universiteit Amsterdam, Amsterdam Movement Sciences, Amsterdam, The Netherlands 2. Department of Oral and Maxillofacial Surgery/Pathology, Amsterdam UMC and Academic Center for Dentistry Amsterdam (ACTA), Vrije Universiteit Amsterdam (VU), Amsterdam Movement Sciences (AMS), Amsterdam, the Netherlands 3. Key Laboratory of Oral Medicine, Guangzhou Institute of Oral Disease, Affiliated Stomatology Hospital of Guangzhou Medical University, Guangzhou Medical University, Guangzhou, China 4. Department of Oral Implantology and Prosthetic Dentistry, Academic Centre for Dentistry Amsterdam (ACTA), University of Amsterdam (UvA) and Vrije Universiteit Amsterdam (VU), The Netherlands 5. Centre de Recherche en Cancérologie de Lyon, UMR INSERM U1052/CNRS 5286, Université de Lyon, Centre Léon Bérard, Lyon, France 6. European Research Institute for the Biology of Ageing (ERIBA), University Medical Center Groningen (UMCG), University of Groningen, Groningen, The Netherlands *Contributed equally to this manuscript **Correspondence: [email protected]; Tel.: +31 (0) 205988463 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.03.03.433740; this version posted March 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. -
Development and Validation of a Protein-Based Risk Score for Cardiovascular Outcomes Among Patients with Stable Coronary Heart Disease
Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................ -
Augmented and Accelerated Nephrogenesis in TGF-2 Heterozygous Mutant Mice
0031-3998/08/6306-0607 Vol. 63, No. 6, 2008 PEDIATRIC RESEARCH Printed in U.S.A. Copyright © 2008 International Pediatric Research Foundation, Inc. Augmented and Accelerated Nephrogenesis in TGF-2 Heterozygous Mutant Mice SUNDER SIMS-LUCAS, GEORGINA CARUANA, JOHN DOWLING, MICHELLE M. KETT, AND JOHN F. BERTRAM Department of Anatomy and Developmental Biology [S.S.-L., G.C., J.F.B.], Monash University, Melbourne 3800, Australia; Department of Anatomical Pathology [J.D.], Alfred Hospital, Prahran 3181, Australia; Department of Physiology [M.M.K.], Monash University, Melbourne 3800, Australia ABSTRACT: Several members of the transforming growth factor- development than TGF-1 and TGF-3 (21). TGF-2 gene (TGF-) superfamily play key roles in kidney development, either expression has been detected in the kidney at embryonic day directly or indirectly regulating nephron number. Although low (E) 11.5 (22) and the protein localized in and around the nephron number is a risk factor for cardiovascular and renal disease, ureteric epithelium and nephron structures from E12.5 the implications of increased nephron number has not been examined (21,23). TGF-2 homozygous null mutant mice (TGF-2Ϫ/Ϫ) due to the absence of appropriate animal models. Here, using unbi- die within 24 h of birth due to defective lung development ased stereology we demonstrated that kidneys from TGF-2 het- erozygous (TGF-2ϩ/Ϫ) mice have approximately 60% more (24). The kidneys of these mice display progressive deterio- nephrons than wild-type mice at postnatal day 30. To determine ration of the ureteric tubules and an enlarged renal pelvis after whether augmented nephron number involved accelerated ureteric E15. -
TGF Beta Signaling Pathway 1 TGF Beta Signaling Pathway
TGF beta signaling pathway 1 TGF beta signaling pathway The Transforming growth factor beta (TGFβ) signaling pathway is involved in many cellular processes in both the adult organism and the developing embryo including cell growth, cell differentiation, apoptosis, cellular homeostasis and other cellular functions. In spite of the wide range of cellular processes that the TGFβ signaling pathway regulates, the process is relatively simple. TGFβ superfamily ligands bind to a type II receptor, which recruits and phosphorylates a type I receptor. The type I receptor then phosphorylates receptor-regulated SMADs (R-SMADs) which can now bind the coSMAD SMAD4. R-SMAD/coSMAD complexes accumulate in the nucleus where they act as transcription factors and participate in the regulation of target gene expression. Mechanism Ligand Binding The TGF Beta superfamily of ligands include: Bone morphogenetic proteins (BMPs), Growth and differentiation factors (GDFs), Anti-müllerian hormone (AMH), Activin, Nodal and TGFβ's[1] . Signalling begins with the binding of a TGF beta superfamily ligand to a TGF beta type II receptor. The type II receptor is a serine/threonine receptor kinase, which catalyses the phosphorylation of the Type I receptor. Each class of ligand binds to a specific type II receptor[2] .In mammals there are seven known type I receptors and five type II receptors[3] . There are three activins: Activin A, Activin B and Activin AB. Activins are involved in embryogenesis and osteogenesis. They also regulate many hormones including pituitary, gonadal and hypothalamic hormones as well as insulin. They are also nerve cell survival factors. The BMPs bind to the Bone morphogenetic protein receptor type-2 (BMPR2). -
Growth Factors and Signaling Proteins in Craniofacial Development Robert Spears and Kathy K.H
Growth Factors and Signaling Proteins in Craniofacial Development Robert Spears and Kathy K.H. Svoboda Regulation of growth and development is controlled by the interactions of cells with each other and the extracellular environment through signal transduction pathways that control the differentiation process by stimulating proliferation or causing cell death. This review will define the common signaling molecules and provide an overview of the general principles of signal transduction events. We also review the signal transduction pathways controlling one specific mechanism found in craniofacial development termed epithelial- mesenchymal transformation (EMT) employed during gastrulation, cranial neural crest migration, and secondary palate formation. Semin Orthod 11:184–198 © 2005 Elsevier Inc. All rights reserved. Growth Factors and receptors (GPCR, Fig 1A), ion-channel receptors, tyrosine Signal Transduction kinase-linked receptors, and receptors with intrinsic enzy- matic activity.2 The GPCRs are characterized by multiple ntracellular signaling is usually triggered by a cell surface transmembrane domains (usually seven) that wind the pro- Ievent such as a specific protein (ligand) binding to a cell tein in and out of the membrane in a serpentine conformation surface receptor to form a receptor-ligand interaction. Cells (Fig 1A, GPCR). The ion-channel receptors are closely re- contacting neighboring cells or their surrounding noncellular lated and actually open a membrane channel when the tissue are termed cell-cell or cell-extracellular matrix (ECM) ligand binds. Many cytokine receptors are in the tyrosine contacts (Fig 1A).1 Interactions of cells with other cells or the kinase-linked class as they lack intrinsic activity; but when ECM can stimulate many reactions, including: increased cell the ligand binds, intracellular tyrosine kinases become division, cell movement, differentiation, and even pro- activated to generate cellular changes. -
The TGF-Β Family in the Reproductive Tract
Downloaded from http://cshperspectives.cshlp.org/ on September 25, 2021 - Published by Cold Spring Harbor Laboratory Press The TGF-b Family in the Reproductive Tract Diana Monsivais,1,2 Martin M. Matzuk,1,2,3,4,5 and Stephanie A. Pangas1,2,3 1Department of Pathology and Immunology, Baylor College of Medicine, Houston, Texas 77030 2Center for Drug Discovery, Baylor College of Medicine, Houston, Texas 77030 3Department of Molecular and Cellular Biology, Baylor College of Medicine Houston, Texas 77030 4Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030 5Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030 Correspondence: [email protected]; [email protected] The transforming growth factor b (TGF-b) family has a profound impact on the reproductive function of various organisms. In this review, we discuss how highly conserved members of the TGF-b family influence the reproductive function across several species. We briefly discuss how TGF-b-related proteins balance germ-cell proliferation and differentiation as well as dauer entry and exit in Caenorhabditis elegans. In Drosophila melanogaster, TGF-b- related proteins maintain germ stem-cell identity and eggshell patterning. We then provide an in-depth analysis of landmark studies performed using transgenic mouse models and discuss how these data have uncovered basic developmental aspects of male and female reproductive development. In particular, we discuss the roles of the various TGF-b family ligands and receptors in primordial germ-cell development, sexual differentiation, and gonadal cell development. We also discuss how mutant mouse studies showed the contri- bution of TGF-b family signaling to embryonic and postnatal testis and ovarian development.