DOCSLIB.ORG

Proinflammatory Molecule Follistatin-Like Protein-1 Is a Novel

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Proinflammatory Molecule Follistatin-Like Protein-1 Is a Novel Follistatin-Like Protein-1 Is a Novel Proinflammatory Molecule Takako Miyamae, Anthony D. Marinov, Dawn Sowders, David C. Wilson, Jason Devlin, Robert Boudreau, Paul This information is current as Robbins and Raphael Hirsch of September 28, 2021. J Immunol 2006; 177:4758-4762; ; doi: 10.4049/jimmunol.177.7.4758 http://www.jimmunol.org/content/177/7/4758 Downloaded from References This article cites 18 articles, 5 of which you can access for free at: http://www.jimmunol.org/content/177/7/4758.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on September 28, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2006 by The American Association of Immunologists All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Follistatin-Like Protein-1 Is a Novel Proinflammatory Molecule1 Takako Miyamae,* Anthony D. Marinov,* Dawn Sowders,† David C. Wilson,* Jason Devlin,‡ Robert Boudreau,§ Paul Robbins,¶ and Raphael Hirsch2* While analyzing gene expression in collagen-induced arthritis, we discovered that a poorly characterized gene, follistatin-like protein 1 (FSTL-1), is highly overexpressed in mouse paws during early arthritis, especially at the interface of synovial pannus and eroding bone. In this study, we show that FSTL-1 is a novel proinflammatory molecule with a previously unrecognized role in inflammation. Transfection of FSTL-1 into macrophages and fibroblasts leads to up-regulation of proinflammatory cytokines, including IL-1␤, TNF-␣, and IL-6. Overexpression of FSTL-1 in mouse paws by gene transfer results in severe paw swelling and arthritis. The Journal of Immunology, 2006, 177: 4758–4762. Downloaded from ollistatin-like protein 1 (FSTL-1)3 is a poorly character- (RA) synovial tissue, demonstrated anti-FSTL-1 Abs in the serum ized protein that has never previously been associated with and synovial fluid of RA patients, and suggested that FSTL-1 was F inflammation. FSTL-1, also known as FRP and TSC-36, is an autoantigen. an extracellular glycoprotein belonging to the BM-40/SPARC/os- teonectin family of proteins containing both extracellular calcium- Materials and Methods binding and follistatin-like domains. FSTL-1 was originally cloned Adenoviral vectors http://www.jimmunol.org/ ␤ from an osteoblastic cell line as a TGF- -inducible gene (1). The A recombinant, E1a-E3-deleted replication defective adenovirus type 5 protein occurs in two isoforms resulting from differential sialyla- vector encoding the mouse FSTL-1 gene (National Center for Biotechnol- tion. FSTL-1 was detected in the medium of all osteosarcoma and ogy Information Nucleotide Database accession number BC028921) was chondrosarcoma cell lines tested and in medium of some cells of generated through Cre-lox recombination as described by Hardy et al. (10). The control vector, Ad-BglII, is an E1a/E3-deleted replication-defective the fibroblast lineage. In mice, the highest expression of FSTL-1 adenovirus type 5 lacking an insert. The vectors were grown in 293 cells was observed in the lung (2). and purified by CsCl gradient ultracentrifugation, dialyzed at 4°C against The action of FSTL-1 is unclear, although a number of putative sterile virus buffer, aliquoted, and stored at Ϫ80°C. FSTL-1 expression was functions have been suggested. Both proliferative and antiprolif- verified by both RT-PCR and Western blot from infected COS-7 cells. erative effects have been reported. FRP may play a role in neural- Cell transfection by guest on September 28, 2021 ization during embryogenesis (3), and its expression is up-regu- lated by estrogen (4). In contrast to other BM-40 family members, U937 and COS-7 cells were electroporated with pRcCMV-hFSTL-1 using a Bio-Rad Gene Pulser (Bio-Rad) according to the manufacturer’s proto- the extracellular calcium-binding domain of FSTL-1 is nonfunc- col. Cells were maintained in G418 selection medium for a period of 3–4 tional (5), suggesting that, despite its sequence homology to BM- wk, and clones were isolated. 40, it has evolved clearly distinct properties. Analysis of prostate Histologic analysis cancers revealed that overexpression of FSTL-1 was associated with higher metastatic potential (6). In contrast, FSTL-1 expres- Mouse knee joints were fixed in 10% neutral buffered formalin, decalcified, sion was extinguished in v-ras-transformed rat fibroblasts, and dehydrated in a gradient of alcohols, paraffin embedded, sectioned, mounted on glass slides, and stained with H&E. For immunohistochemis- transfection of FSTL-1 into these cells inhibited in vitro invasion try, knees were fixed in 2% paraformaldehyde, cut longitudinally with a (7) and led to growth inhibition in human lung cancer cells (8). In scalpel blade, mounted onto a cork disk with a small drop of Cryogel 1998, Tanaka et al. (9) cloned FSTL-1 from rheumatoid arthritis (Cancer Diagnostics), and placed in liquid nitrogen-cooled isopentane for 45 s. Sections of 7 ␮m were obtained using a cryostat. Slides containing knee sections were fixed with 2% paraformaldehyde for 20 min and washed with PBS followed by BSA buffer (0.5% BSA and 0.15% glycine *Division of Rheumatology, Children’s Hospital of Pittsburgh, University of Pitts- † in PBS). Slides were blocked for 45 min with a 1/20 dilution of normal burgh, School of Medicine, Pittsburgh, PA 15213; Cincinnati Children’s Hospital donkey serum (Sigma-Aldrich) in BSA buffer and washed three times with Medical Center, Cincinnati, OH 45229; ‡Department of Cell Biology and Physiology, § BSA buffer. The primary Ab goat anti-mouse FSTL-1 (R&D Systems) University of Pittsburgh School of Medicine, Pittsburgh, PA 15261; Department of ␮ Epidemiology, Graduate School of Public Health, Pittsburgh, PA 15261; and ¶De- diluted to 10 g/ml in BSA buffer was added, incubated for 2 h, and partment of Molecular Genetics and Biochemistry, University of Pittsburgh School of washed three times with BSA buffer. The secondary Ab Alexa Fluor 488 Medicine, Pittsburgh, PA 15261 donkey anti-goat IgG (Molecular Probes) diluted 1/500 in BSA buffer was Received for publication April 25, 2006. Accepted for publication July 11, 2006. added, incubated for 1 h, and washed three times with BSA buffer and three times with PBS. The nucleus stain DRAQ5 (Biostatus) diluted 1/1000 in The costs of publication of this article were defrayed in part by the payment of page PBS was added, incubated for 30 min, and washed three times with PBS. charges. This article must therefore be hereby marked advertisement in accordance A coverslip containing a drop of gelvatol was added, and slides were stored with 18 U.S.C. Section 1734 solely to indicate this fact. at 4°C until observation with confocal microscope. For the double staining 1 This work was supported in part by National Institutes of Health Grants AI44566 (to of fibroblast-like synoviocytes and FSTL-1, the primary Ab rat anti-mouse R.H) and AI 56374 (to P.D.R). Thy-1.2 (BD Pharmingen) was included at the same time as the goat anti- 2 Address correspondence and reprint requests to Dr. Raphael Hirsch, Division of mouse FSTL-1 at a concentration of 1.5 ␮g/ml. The secondary Ab Alexa Rheumatology, Children’s Hospital of Pittsburgh, 3705 Fifth Avenue, Pittsburgh, PA Fluor 594 donkey anti-rat IgG was used at 1/1000 dilution. Appropriate 15213. E-mail address: [email protected] isotype control primary Abs were used each time immunohistochemistry 3 Abbreviations used in this paper: FSTL-1, follistatin-like protein 1; RA, rheumatoid was performed. Immunohistochemistry slides were observed using a arthritis; CII, type II collagen; CIA, collagen-induced arthritis. Olympus Fluroview 500 (Olympus) confocal microscope. Copyright © 2006 by The American Association of Immunologists, Inc. 0022-1767/06/$02.00 The Journal of Immunology 4759 FIGURE 1. FSTL-1 is overexpressed in fi- broblast-like synoviocytes in early CIA. Mouse knee joints were harvested from mice before immunization with CII (day 0), during acute arthritis (day 28), or during late arthritis (day 49). Tissues were sectioned and stained for FSTL-1 and observed under a confocal mi- croscope at ϫ40 (A–C). Higher magnification (ϫ100) views of day 28 synovium (D–F) show CD90ϩ fibroblasts in red (D), FSTL-1 in green (F), and double staining of CD90 and FSTL-1 (E). Colocalization of FSTL-1 with CD90ϩ fi- broblasts is indicated by the arrows in E. Quantitative RT-PCR of entire paw and digits). The arthritic index for each mouse was calculated Downloaded from by adding the score of the four individual paws. The statistical significance Total RNA was isolated from frozen liver using the ToTALLY RNA Iso- of difference was determined using the exact Wilcoxon test. p Ͻ 0.05 was lation Kit (Ambion) according to the manufacturer’s instructions. To re- considered significant. Mice were sacrificed at various times, and joints move possible genomic DNA contamination, RNA was treated with DNase were used for histopathology, whereas livers were snap frozen and stored I (Ambion). cDNA was synthesized with random hexamer oligonucleotides in a liquid nitrogen freezer. using the SuperScript II Reverse Transcriptase Kit (Invitrogen Life Tech- nologies). PCR was performed in a LightCycler (Mx3000P; Stratagene) http://www.jimmunol.org/ using the Brilliant SYBR Green QPCR Master Mix (Stratagene) according Results to the protocol (95°C hot start for 10 min followed by 40 amplification FSTL-1 is overexpressed in acute CIA by fibroblast-like cycles, denaturation at 95°C, primer annealing at 59°C, and amplicon ex- synoviocytes tension at 72°C) using oligonucleotide primer sets for IL-1␤, IL-6, and TNF-␣ (11).
Load more

Recommended publications
  • (FSTL1) Is a Prognostic Biomarker and Correlated with Immune Cell
    Li et al. World Journal of Surgical Oncology (2020) 18:324 https://doi.org/10.1186/s12957-020-02070-9 RESEARCH Open Access Follistatin-like 1 (FSTL1) is a prognostic biomarker and correlated with immune cell infiltration in gastric cancer Li Li1,2, Shanshan Huang1,2, Yangyang Yao1,2, Jun Chen1,2, Junhe Li1,2, Xiaojun Xiang1,2, Jun Deng1,2* and Jianping Xiong1,2* Abstract Background: Follistatin-like 1 (FSTL1) plays a central role in the progression of tumor and tumor immunity. However, the effect of FSTL1 on the prognosis and immune infiltration of gastric cancer (GC) remains to be elucidated. Methods: The expression of FSTL1 data was analyzed in Oncomine and TIMER databases. Analyses of clinical parameters and survival data were conducted by Kaplan-Meier plotter and immunohistochemistry. Western blot assay and real-time quantitative PCR (RT-qPCR) were used to analyze protein and mRNA expression, respectively. The correlations between FSTL1 and cancer immune infiltrates were analyzed by Tumor Immune Estimation Resource (TIME), Gene Expression Profiling Interactive Analysis (GEPIA), and LinkedOmics database. Results: The expression of FSTL1 was significantly higher in GC tissues than in normal tissues, and bioinformatic analysis and immunohistochemistry (IHC) indicated that high FSTL1 expression significantly correlated with poor prognosis in GC. Moreover, FSTL1 was predicted as an independent prognostic factor in GC patients. Bioinformatics analysis results suggested that FSTL1 mainly involved in tumor progression and tumor immunity. And significant correlations were found between FSTL1 expression and immune cell infiltration in GC. Conclusions: The study effectively revealed useful information about FSTL1 expression, prognostic values, potential functional networks, and impact of tumor immune infiltration in GC.
    [Show full text]
  • Gene Regulation Underlies Environmental Adaptation in House Mice
    Downloaded from genome.cshlp.org on September 28, 2021 - Published by Cold Spring Harbor Laboratory Press Research Gene regulation underlies environmental adaptation in house mice Katya L. Mack,1 Mallory A. Ballinger,1 Megan Phifer-Rixey,2 and Michael W. Nachman1 1Department of Integrative Biology and Museum of Vertebrate Zoology, University of California, Berkeley, California 94720, USA; 2Department of Biology, Monmouth University, West Long Branch, New Jersey 07764, USA Changes in cis-regulatory regions are thought to play a major role in the genetic basis of adaptation. However, few studies have linked cis-regulatory variation with adaptation in natural populations. Here, using a combination of exome and RNA- seq data, we performed expression quantitative trait locus (eQTL) mapping and allele-specific expression analyses to study the genetic architecture of regulatory variation in wild house mice (Mus musculus domesticus) using individuals from five pop- ulations collected along a latitudinal cline in eastern North America. Mice in this transect showed clinal patterns of variation in several traits, including body mass. Mice were larger in more northern latitudes, in accordance with Bergmann’s rule. We identified 17 genes where cis-eQTLs were clinal outliers and for which expression level was correlated with latitude. Among these clinal outliers, we identified two genes (Adam17 and Bcat2) with cis-eQTLs that were associated with adaptive body mass variation and for which expression is correlated with body mass both within and between populations. Finally, we per- formed a weighted gene co-expression network analysis (WGCNA) to identify expression modules associated with measures of body size variation in these mice.
    [Show full text]
  • Transcriptional Recapitulation and Subversion Of
    Open Access Research2007KaiseretVolume al. 8, Issue 7, Article R131 Transcriptional recapitulation and subversion of embryonic colon comment development by mouse colon tumor models and human colon cancer Sergio Kaiser¤*, Young-Kyu Park¤†, Jeffrey L Franklin†, Richard B Halberg‡, Ming Yu§, Walter J Jessen*, Johannes Freudenberg*, Xiaodi Chen‡, Kevin Haigis¶, Anil G Jegga*, Sue Kong*, Bhuvaneswari Sakthivel*, Huan Xu*, Timothy Reichling¥, Mohammad Azhar#, Gregory P Boivin**, reviews Reade B Roberts§, Anika C Bissahoyo§, Fausto Gonzales††, Greg C Bloom††, Steven Eschrich††, Scott L Carter‡‡, Jeremy E Aronow*, John Kleimeyer*, Michael Kleimeyer*, Vivek Ramaswamy*, Stephen H Settle†, Braden Boone†, Shawn Levy†, Jonathan M Graff§§, Thomas Doetschman#, Joanna Groden¥, William F Dove‡, David W Threadgill§, Timothy J Yeatman††, reports Robert J Coffey Jr† and Bruce J Aronow* Addresses: *Biomedical Informatics, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA. †Departments of Medicine, and Cell and Developmental Biology, Vanderbilt University and Department of Veterans Affairs Medical Center, Nashville, TN 37232, USA. ‡McArdle Laboratory for Cancer Research, University of Wisconsin, Madison, WI 53706, USA. §Department of Genetics and Lineberger Cancer Center, University of North Carolina, Chapel Hill, NC 27599, USA. ¶Molecular Pathology Unit and Center for Cancer Research, Massachusetts deposited research General Hospital, Charlestown, MA 02129, USA. ¥Division of Human Cancer Genetics, The Ohio State University College of Medicine, Columbus, Ohio 43210-2207, USA. #Institute for Collaborative BioResearch, University of Arizona, Tucson, AZ 85721-0036, USA. **University of Cincinnati, Department of Pathology and Laboratory Medicine, Cincinnati, OH 45267, USA. ††H Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, USA. ‡‡Children's Hospital Informatics Program at the Harvard-MIT Division of Health Sciences and Technology (CHIP@HST), Harvard Medical School, Boston, Massachusetts 02115, USA.
    [Show full text]
  • Duke University Dissertation Template
    Gene-Environment Interactions in Cardiovascular Disease by Cavin Keith Ward-Caviness Graduate Program in Computational Biology and Bioinformatics Duke University Date:_______________________ Approved: ___________________________ Elizabeth R. Hauser, Supervisor ___________________________ William E. Kraus ___________________________ Sayan Mukherjee ___________________________ H. Frederik Nijhout Dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Graduate Program in Computational Biology and Bioinformatics in the Graduate School of Duke University 2014 i v ABSTRACT Gene-Environment Interactions in Cardiovascular Disease by Cavin Keith Ward-Caviness Graduate Program in Computational Biology and Bioinformatics Duke University Date:_______________________ Approved: ___________________________ Elizabeth R. Hauser, Supervisor ___________________________ William E. Kraus ___________________________ Sayan Mukherjee ___________________________ H. Frederik Nijhout An abstract of a dissertation submitted in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Graduate Program in Computational Biology and Bioinformatics in the Graduate School of Duke University 2014 Copyright by Cavin Keith Ward-Caviness 2014 Abstract In this manuscript I seek to demonstrate the importance of gene-environment interactions in cardiovascular disease. This manuscript contains five studies each of which contributes to our understanding of the joint impact of genetic variation
    [Show full text]
  • FSTL1 (C-Term) Rabbit Polyclonal Antibody – AP51731PU-N | Origene
    OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for AP51731PU-N FSTL1 (C-term) Rabbit Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: FC, IHC, WB Recommended Dilution: ELISA: 1/1000. Western Blot: 1/100-1/500. Flow Cytometry: 1/10-1/50. Immunohistochemistry on Paraffin Sections: 1/50-1/100. Reactivity: Human Host: Rabbit Isotype: Ig Clonality: Polyclonal Immunogen: KLH conjugated synthetic peptide between 285~318 amino acids from the C-terminal region of Human Follistatin-related protein 1 Specificity: This antibody recognizes Human Follistatin-related protein 1 (C-term). Formulation: PBS containing 0.09% (W/V) Sodium Azide as preservative State: Aff - Purified State: Liquid purified Ig fraction Concentration: lot specific Purification: Protein A column, followed by peptide affinity purification Conjugation: Unconjugated Storage: Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. Stability: Shelf life: one year from despatch. Gene Name: Homo sapiens follistatin like 1 (FSTL1) Database Link: Entrez Gene 11167 Human Q12841 Synonyms: FSTL1, FRP, Follistatin-like protein 1 Note: Molecular Weight: 35 kDa This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 FSTL1 (C-term) Rabbit Polyclonal Antibody – AP51731PU-N Protein Families: Secreted Protein Product images: Western blot analysis of FSTL1 Antibody (C-term) in A549 cell line lysates (35ug/lane).
    [Show full text]
  • The Human Gene Connectome As a Map of Short Cuts for Morbid Allele Discovery
    The human gene connectome as a map of short cuts for morbid allele discovery Yuval Itana,1, Shen-Ying Zhanga,b, Guillaume Vogta,b, Avinash Abhyankara, Melina Hermana, Patrick Nitschkec, Dror Friedd, Lluis Quintana-Murcie, Laurent Abela,b, and Jean-Laurent Casanovaa,b,f aSt. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, The Rockefeller University, New York, NY 10065; bLaboratory of Human Genetics of Infectious Diseases, Necker Branch, Paris Descartes University, Institut National de la Santé et de la Recherche Médicale U980, Necker Medical School, 75015 Paris, France; cPlateforme Bioinformatique, Université Paris Descartes, 75116 Paris, France; dDepartment of Computer Science, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel; eUnit of Human Evolutionary Genetics, Centre National de la Recherche Scientifique, Unité de Recherche Associée 3012, Institut Pasteur, F-75015 Paris, France; and fPediatric Immunology-Hematology Unit, Necker Hospital for Sick Children, 75015 Paris, France Edited* by Bruce Beutler, University of Texas Southwestern Medical Center, Dallas, TX, and approved February 15, 2013 (received for review October 19, 2012) High-throughput genomic data reveal thousands of gene variants to detect a single mutated gene, with the other polymorphic genes per patient, and it is often difficult to determine which of these being of less interest. This goes some way to explaining why, variants underlies disease in a given individual. However, at the despite the abundance of NGS data, the discovery of disease- population level, there may be some degree of phenotypic homo- causing alleles from such data remains somewhat limited. geneity, with alterations of specific physiological pathways under- We developed the human gene connectome (HGC) to over- come this problem.
    [Show full text]
  • Loss of FSTL1-Expressing Adipocyte Progenitors Drives the Age-Related Involution of Brown Adipose Tissue
    bioRxiv preprint doi: https://doi.org/10.1101/2020.05.14.096990; this version posted May 16, 2020. 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. Loss of FSTL1-expressing adipocyte progenitors drives the age-related involution of brown adipose tissue Zan Huang1,2,3,12,*, Zengdi Zhang3,12, Ryan Heck3, Ping Hu4, Hezkiel Nanda5, Kaiqun Ren3,6, Zequn Sun7, Alessandro Bartolomucci3, Yan Gao8, Dongjun Chung9, Weiyun Zhu1,2, Steven Shen5,10, Hai-Bin Ruan3,11,*,# 1Laboratory of Gastrointestinal Microbiology, Jiangsu Key Laboratory of Gastrointestinal Nutrition and Animal Health, College of Animal Science and Technology, Nanjing Agriculture University, Nanjing, Jiangsu, China 2National Center for International Research on Animal Gut Nutrition, Nanjing Agriculture University, Nanjing, Jiangsu, China 3Department of Integrative Biology and Physiology, University of Minnesota Medical School, Minneapolis, MN, USA 4Department of Prenatal Diagnosis, Women's Hospital of Nanjing Medical University, Nanjing Maternity and Child Health Care Hospital, Nanjing, Jiangsu, China 5Institute for Health Informatics, University of Minnesota Medical School, Minneapolis, MN, USA 6College of Medicine, Hunan Normal University, Changsha, Hunan, China 7Department of Public Health Sciences, Medical University of South Carolina, Charleston, SC 29425, USA 8Department of Human Anatomy, School of Basic Medical Sciences, Capital Medical University, Beijing, China 9Department of Biomedical Informatics, Ohio State University, Columbus, OH 43210, USA 10Clinical Translational Science Institute, University of Minnesota Medical School, Minneapolis, MN, USA 11Center for Immunology, University of Minnesota Medical School, Minneapolis, MN, USA 12These authors contributed equally. *Correspondence: H.-B. R. ([email protected]) or Z.
    [Show full text]
  • Follistatin-Like Proteins: Structure, Functions and Biomedical Importance
    biomedicines Review Follistatin-Like Proteins: Structure, Functions and Biomedical Importance Olga K. Parfenova 1, Vladimir G. Kukes 2 and Dmitry V. Grishin 1,* 1 Institute of Biomedical Chemistry (IBMC), 10 Pogodinskaya St., 119121 Moscow, Russia; [email protected] 2 Scientific Centre for Expert Evaluation of Medicinal Products, 8/2 Petrovsky Blvd, 127051 Moscow, Russia; [email protected] * Correspondence: [email protected] Abstract: Main forms of cellular signal transmission are known to be autocrine and paracrine signaling. Several cells secrete messengers called autocrine or paracrine agents that can bind the corresponding receptors on the surface of the cells themselves or their microenvironment. Follistatin and follistatin-like proteins can be called one of the most important bifunctional messengers capable of displaying both autocrine and paracrine activity. Whilst they are not as diverse as protein hormones or protein kinases, there are only five types of proteins. However, unlike protein kinases, there are no minor proteins among them; each follistatin-like protein performs an important physiological function. These proteins are involved in a variety of signaling pathways and biological processes, having the ability to bind to receptors such as DIP2A, TLR4, BMP and some others. The activation or experimentally induced knockout of the protein-coding genes often leads to fatal consequences for individual cells and the whole body as follistatin-like proteins indirectly regulate the cell cycle, tissue differentiation, metabolic pathways, and participate in the transmission chains of the pro- inflammatory intracellular signal. Abnormal course of these processes can cause the development of Citation: Parfenova, O.K.; Kukes, oncology or apoptosis, programmed cell death.
    [Show full text]
  • Goat Anti-FSTL1 Antibody Peptide-Affinity Purified Goat Antibody Catalog # Af1445a
    10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 Goat Anti-FSTL1 Antibody Peptide-affinity purified goat antibody Catalog # AF1445a Specification Goat Anti-FSTL1 Antibody - Product Information Application WB Primary Accession Q12841 Other Accession NP_009016, 11167 Reactivity Human Predicted Cow Host Goat Clonality Polyclonal Concentration 0.5mg/ml Isotype IgG Calculated MW 34986 AF1445a (0.3 µg/ml) staining of Placenta Goat Anti-FSTL1 Antibody - Additional lysate (35 µg protein in RIPA buffer). Primary Information incubation was 1 hour. Detected by chemiluminescence.chemiluminescence. Gene ID 11167 Other Names Goat Anti-FSTL1 Antibody - Background Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP This gene encodes a protein with similarity to follistatin, an activin-binding protein. It Format contains an FS module, a follistatin-like 0.5 mg IgG/ml in Tris saline (20mM Tris sequence containing 10 conserved cysteine pH7.3, 150mM NaCl), 0.02% sodium azide, residues. This gene product is thought to be an with 0.5% bovine serum albumin autoantigen associated with rheumatoid Storage arthritis. Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at Goat Anti-FSTL1 Antibody - References -20°C in small aliquots to prevent freeze-thaw cycles. MicroRNAs and target site screening reveals a pre-microRNA-30e variant associated with Precautions schizophrenia. Xu Y, et al. Schizophr Res, 2010 Goat Anti-FSTL1 Antibody is for research Jun. PMID 20347265. Inherited genetic variant use only and not for use in diagnostic or predisposes to aggressive but not indolent therapeutic procedures.
    [Show full text]
  • FSTL1 (NM 007085) Human Recombinant Protein Product Data
    OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TP300586 FSTL1 (NM_007085) Human Recombinant Protein Product data: Product Type: Recombinant Proteins Description: Recombinant protein of human follistatin-like 1 (FSTL1) Species: Human Expression Host: HEK293T Tag: C-Myc/DDK Predicted MW: 32.6 kDa Concentration: >50 ug/mL as determined by microplate BCA method Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining Buffer: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol Preparation: Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps. Storage: Store at -80°C. Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. RefSeq: NP_009016 Locus ID: 11167 UniProt ID: Q12841 RefSeq Size: 3840 Cytogenetics: 3q13.33 RefSeq ORF: 924 Synonyms: FRP; FSL1; MIR198; OCC-1; OCC1; tsc36 Summary: This gene encodes a protein with similarity to follistatin, an activin-binding protein. It contains an FS module, a follistatin-like sequence containing 10 conserved cysteine residues. This gene product is thought to be an autoantigen associated with rheumatoid arthritis. [provided by RefSeq, Jul 2008] Protein Families: Secreted Protein This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 FSTL1 (NM_007085) Human Recombinant Protein – TP300586 Product images: Coomassie blue staining of purified FSTL1 protein (Cat# TP300586).
    [Show full text]
  • FSTL1 Antibody (C-Term) Affinity Purified Rabbit Polyclonal Antibody (Pab) Catalog # Ap10534b
    10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 FSTL1 Antibody (C-term) Affinity Purified Rabbit Polyclonal Antibody (Pab) Catalog # AP10534b Specification FSTL1 Antibody (C-term) - Product Information Application WB, IHC-P, FC,E Primary Accession Q12841 Other Accession Q9GKY0, NP_009016.1 Reactivity Human, Mouse, Rat Predicted Monkey Host Rabbit Clonality Polyclonal Isotype Rabbit Ig Calculated MW 34986 Antigen Region 280-308 FSTL1 Antibody (C-term) - Additional Information Gene ID 11167 All lanes : Anti-FSTL1 Antibody (C-term) at 1:1000 dilution Lane 1: A549 whole cell Other Names lysate Lane 2: human heart lysate Follistatin-related protein 1, Follistatin-like Lysates/proteins at 20 µg per lane. protein 1, FSTL1, FRP Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Target/Specificity Predicted band size : 35 kDa This FSTL1 antibody is generated from Blocking/Dilution buffer: 5% NFDM/TBST. rabbits immunized with a KLH conjugated synthetic peptide between 280-308 amino acids from the C-terminal region of human FSTL1. Dilution WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. Storage Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C All lanes : Anti-FSTL1 Antibody (C-term) at in small aliquots to prevent freeze-thaw 1:1000 dilution Lane 1: Hela whole cell lysate cycles.
    [Show full text]
  • Hormone-Induced Protection Against Mammary Tumorigenesis Is Conserved in Multiple Rat Strains and Identifies a Core Gene Expression Signature Induced by Pregnancy
    Research Article Hormone-Induced Protection against Mammary Tumorigenesis Is Conserved in Multiple Rat Strains and Identifies a Core Gene Expression Signature Induced by Pregnancy Collin M. Blakely, Alexander J. Stoddard, George K. Belka, Katherine D. Dugan, Kathleen L. Notarfrancesco, Susan E. Moody, Celina M. D’Cruz, and Lewis A. Chodosh Departments of Cancer Biology, Cell and Developmental Biology, and Medicine, and The Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania Abstract 50% reduction in lifetime breast cancer risk compared with their Women who have their first child early in life have a nulliparous counterparts (2). Notably, the protective effects of an substantially lower lifetime risk of breast cancer. The early full-term pregnancy have been observed in multiple ethnic mechanism for this is unknown. Similar to humans, rats groups and geographic locations, suggesting that parity-induced exhibit parity-induced protection against mammary tumori- protection results from intrinsic biological changes in the breast genesis. To explore the basis for this phenomenon, we rather than specific socioeconomic or environmental factors. At identified persistent pregnancy-induced changes in mammary present, however, the biological mechanisms underlying this gene expression that are tightly associated with protection phenomenon are unknown. against tumorigenesis in multiple inbred rat strains. Four Several models to explain the protective effects of parity have inbred rat strains that exhibit marked differences in their been proposed. For instance, parity has been hypothesized to intrinsic susceptibilities to carcinogen-induced mammary induce the terminal differentiation of a subpopulation of mammary tumorigenesis were each shown to display significant protec- epithelial cells, thereby decreasing their susceptibility to oncogen- tion against methylnitrosourea-induced mammary tumori- esis (4).
    [Show full text]