DOCSLIB.ORG

Letter to the Editor Potential Function of MMP3 Gene in Degradation Of

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Letter to the Editor Potential Function of MMP3 Gene in Degradation Of 66 Biomed Environ Sci, 2021; 34(1): 66-70 Letter to the Editor Potential Function of MMP3 Gene in Degradation of Extracellular Matrix Complex in Colorectal Carcinoma* DAI Xiao Yong1,&, SONG An Yi1,2,&, MU Lan1, WANG Li Jun1, and HUANG Lai Qiang1,2,# Colorectal cancer (CRC) is a kind of malignant language software through special packages such as tumor that occurs in the digestive tract. CRC occurs bioconductors and limma[2]. In addition, analysis of globally and has high rates of morbidity and down-regulated genes may reveal functional defects mortality. Its incidence and mortality are second and mutations that trigger the occurrence of cancer. only to gastric cancer, esophageal cancer, and Meanwhile, over-expressed genes may be useful as primary liver cancer in digestive system biomarkers in the clinic or to identify potential malignancies. Most CRC cases are adenomas. A few antigen targets. Analysis using conventional are squamous epithelial cancers, which can spread methods, such as enrichment analysis and protein- to adjacent tissues and organs through lymph and protein interaction (PPI) networks, analysis of blood circulation, or directly. The occurrence of CRC differentially expressed genes (DEGs) may provide a is related to factors that include gene mutation, novel approach to reveal significant genes and dietary habits, family disease history, smoking, signaling pathways related to disease. drinking, and external carcinogens. Diagnostic Based on special experimental processing methods for CRC mainly include digital rectal conditions and uniform statistical method of examination, X-ray barium enema, sigmoidoscopy, samples, the refined GAE110224 gene chips were and fiber colonoscopy. However, low sensitivity of chosen for this study from the GEO database. The detection is a problem, and false positives still occur. original GSE110224 gene chip contains information Thus, screening for specific over-expressed genes as on gene expression in CRC tissue and normal tissue biomarkers is meaningful in the clinic for diagnosis. from 17 patients treated clinically. In total, 36,951 Additionally, several reports have discussed DEGs were identified. Of these, 20,006 that were molecular mechanisms associated with the over-expressed and 16,945 that were down- occurrence of CRC, such as the K-Ras and p53 regulated were included. By setting with the signaling pathways. The crucial pathways have not parameters |logFC| > 2 and P < 0.05, 71 markedly been identical. Data of clinical samples from over-expressed and 106 markedly down-regulated bioinformatics databases with information of gene genes were screened. The volcano map of DEGs expression on a large scale may reveal significant from the downloaded document was drawn using pathways that are involved in cancer development[1]. Prism 8 software (Figure 1). The top ten over- The Gene Expression Omnibus (GEO) database expressed genes according to value of log (fold includes information acquired globally using many change) expression levels are listed in gene chips. The data include clinically relevant Supplementary Table S1 available in www. expression of genes and several types of RNA, besjournal.com. including messenger RNA (mRNA), micro RNA In addition to the aforementioned GEO database, (miRNA), and long noncoding RNA (lncRNA), and online platforms including Gene Expression Profiling data of DNA methylation. Clinical data can be Interactive Analysis (GEPIA) and OncoLnc can be downloaded from the website and visualized by R useful to visualize gene expression and survival doi: 10.3967/bes2021.009 *This work was supported with funding awarded to LH from the National Natural Science Foundation of China (NSFC) [81872368]; Shenzhen Science Technology and Innovation Commission Key Projects [JCYJ20180508152130899]; State Key Lab Construction Project (GuoKeFaJi [2018]38); and Shenzhen Development and Reform Commission Subject Construction Project [2017]1434. 1. Shenzhen Key Laboratory of Gene and Antibody Therapy, Center for Biotechnology and Biomedicine, State Key Laboratory of Chemical Oncogenomics, Tsinghua-Berkeley Shenzhen Institute (TBSI), Tsinghua Shenzhen International Graduate School, Tsinghua University, Shenzhen 518055, Guangdong, China; 2. Department of Chemistry, Tsinghua University, Beijing 100084, China Function of MMP3 in colorectal cancer 67 curves based on clinical data from The Cancer besjournal.com). In addition, MMP3 and CXCL5 were Genome Atlas (TCGA) website. The Human Protein comparatively over-expressed in CRC tissue with Atlas database contains a variety of immune- significant differences. These genes could be histochemical patches for significant genes in several potential biomarkers for diagnosis in clinical settings types of cancer tissues and normal tissues. based on the high accuracy of their ROC curves as Functional protein association networks (STRING) is reported. an online platform for the analysis of gene Survival analysis revealed log-rank P values of enrichment and PPI. The Functional Annotation 0.0106, 0.0051, 0.1552, and 0.2861 for MMP3, Bioinformatics Microarray Analysis (DAVID) website TIMP1, KRT80, and CXCL5, respectively is useful for Gene Ontology enrichment analyses of (Supplementary Figure S3 available in www. DEGs identified from gene chips. Presently, the besjournal.com). Therefore, expression of MMP3 functions and involved signaling pathways of and TIMP1 might be closely associated with patient significant genes were searched from GeneCards and survival. In particular, the MMP3 gene is important the Kyoto Encyclopedia of Genes and Genomes for collagen degradation, extracellular matrix (ECM) website for further demonstration. Volcano maps of structure, wound repair, and tissue remodeling. It is DEGs, expression histograms, survival curves, and closely related to cancer occurrence and cancer cell receiver operating characteristic (ROC) curves were migration. The TIMP1 protein is an inhibitor of plotted using Prism 8 software. Bubble charts of matrix metallopeptidase and has a negative pathway enrichment were constructed using R 3.6.3 relationship with MMP3. Immunohistochemical software based on the results of enrichment analysis examinations of pathological and normal tissues from the DAVID website[3]. revealed less frequent gene expression of TIMP1, Based on a survey of relevant reports, four genes while MMP3 gene expression in CRC tissues was (MMP3, TIMP1, KRT80, and CXCL5) with high levels comparatively increased. The findings were of expression and significant differences were consistent with the analysis results from the GEO selected for further analysis as shown in and TCGA databases (Supplementary Figure S4 Supplementary Figure S1 available in www. available in www.besjournal.com). Thus, MMP3 was besjournal.com. The area under the ROC curve for implicated as being functionally important in the MMP3, TIMP1, KRT80, and CXCL5 was 0.8616, development of CRC. 0.9308, 0.9204, and 0.8062, respectively Concerning DEGs, 71 markedly over-expressed (Supplementary Figure S2 available in www. genes were selected for enrichment analysis using the parameters of logFC > 2 and P < 0.05. PPI Genes network and pathway enrichment were performed 8 [4] TIMP1 using the STRING website (Figure 2) . Processes KRT80 related to chemokine receptors CXCL1, CXCL5, and 6 MMP3 CXCL11, and the function of ECM related to matrix AQP8 value) CA4 metalloproteinase (MMPs) were relatively P CA1 4 CXCL5 concentrated from PPI network. In addition, the MS4A12 MMP1, MMP3, MMP7, and MMP10 were located in CLCA4 −log10 ( the kernel of the PPI network, and so may be 2 influential on the development of CRC. We also imported 71 markedly over-expressed genes into the 0 DAVID website for enrichment analysis. The genes 0 2 4 6 −6 −4 −2 included those associated with important signaling logFC pathways of biological process, molecular functions, Figure 1. Volcano map of differentially and cellular components. The results were analyzed [5] expressed genes. The X-axis displays values of and visualized with R language software (Figure 3) . −logFC for each gene. The y-axis displays the Generally, the processes of inflammatory −log10 (P value). Genes with positive logFC are response, immune response, collagen catabolic over-expressed, and genes with negative logFC process, chemokine-mediated signaling pathway, are down-regulated. Four remarkably over- cell-cell signaling, and chemotaxis were more expressed and significantly down-regulated concentrated in the enrichment analysis. In addition, genes are denoted in red and blue, the enrichment analysis revealed the association of respectively. the processes of extracellular matrix organization, 68 Biomed Environ Sci, 2021; 34(1): 66-70 extracellular matrix disassembly, and collagen fibril The MMP family of proteins are involved in the organization with the MMP3 gene according to a breakdown of the extracellular matrix during disease previous survey from the Genecards website. As processes, such as arthritis and cancer metastasis[7]. reported, MMPs has appreciable impacts on collagen MMP3 is a zinc-dependent endopeptidase that can degradation, maintenance of the structure of the degrade several extracellular components and extracellular matrix, tissue remodeling, wound molecules, including transferrin, laminin, collagen, healing, and cancer migration, which may play a and chondroitin. The extracellular matrix is mainly significant role in the development of colorectal composed of collagen, elastin, proteoglycans, and cancer according to PPI network
Load more

Recommended publications
  • Dual Proteome-Scale Networks Reveal Cell-Specific Remodeling of the Human Interactome
    bioRxiv preprint doi: https://doi.org/10.1101/2020.01.19.905109; this version posted January 19, 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. Dual Proteome-scale Networks Reveal Cell-specific Remodeling of the Human Interactome Edward L. Huttlin1*, Raphael J. Bruckner1,3, Jose Navarrete-Perea1, Joe R. Cannon1,4, Kurt Baltier1,5, Fana Gebreab1, Melanie P. Gygi1, Alexandra Thornock1, Gabriela Zarraga1,6, Stanley Tam1,7, John Szpyt1, Alexandra Panov1, Hannah Parzen1,8, Sipei Fu1, Arvene Golbazi1, Eila Maenpaa1, Keegan Stricker1, Sanjukta Guha Thakurta1, Ramin Rad1, Joshua Pan2, David P. Nusinow1, Joao A. Paulo1, Devin K. Schweppe1, Laura Pontano Vaites1, J. Wade Harper1*, Steven P. Gygi1*# 1Department of Cell Biology, Harvard Medical School, Boston, MA, 02115, USA. 2Broad Institute, Cambridge, MA, 02142, USA. 3Present address: ICCB-Longwood Screening Facility, Harvard Medical School, Boston, MA, 02115, USA. 4Present address: Merck, West Point, PA, 19486, USA. 5Present address: IQ Proteomics, Cambridge, MA, 02139, USA. 6Present address: Vor Biopharma, Cambridge, MA, 02142, USA. 7Present address: Rubius Therapeutics, Cambridge, MA, 02139, USA. 8Present address: RPS North America, South Kingstown, RI, 02879, USA. *Correspondence: [email protected] (E.L.H.), [email protected] (J.W.H.), [email protected] (S.P.G.) #Lead Contact: [email protected] bioRxiv preprint doi: https://doi.org/10.1101/2020.01.19.905109; this version posted January 19, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder.
    [Show full text]
  • 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.
    [Show full text]
  • REG Gene Expression in Inflamed and Healthy Colon Mucosa Explored by in Situ Hybridisation
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Crossref Cell Tissue Res (2013) 352:639–646 DOI 10.1007/s00441-013-1592-z REGULAR ARTICLE REG gene expression in inflamed and healthy colon mucosa explored by in situ hybridisation Atle van Beelen Granlund & Ann Elisabet Østvik & Øystein Brenna & Sverre H. Torp & Bjørn I. Gustafsson & Arne Kristian Sandvik Received: 10 December 2012 /Accepted: 14 February 2013 /Published online: 22 March 2013 # The Author(s) 2013. This article is published with open access at Springerlink.com Abstract The regenerating islet-derived (REG) gene family used in situ hybridisation to demonstrate the cellular encodes a group of proteins highly expressed in several localisation of REG expression in healthy and diseased human pathologies, many of which are associated with colonic mucosa. Samples drawn from an IBD cohort includ- epithelial inflammation. All human family members, name- ing both inflamed and un-inflamed colonic mucosa are ly REG1A, REG1B, REG3A and REG4, are closely related described, as are samples from non-IBD inflammation and in genomic sequence and all are part of the c-type lectin healthy controls. Immunohistochemistry against known superfamily. REGs are highly expressed during inflamma- cell-type markers on serial sections has localised the expres- tory bowel disease (IBD)-related colonic inflammation and sion of REGs to metaplastic Paneth cells (REG1A, REG1B the in vivo expression pattern of REG1A and REG4 has and REG3A) and enteroendocrine cells (REG4), with a been localised by using immunohistochemistry. However, marked expansion of expression during inflammation. The the function of the encoded proteins is largely unknown and group of REGs can, based on gene expression patterns, be the cellular localisation of REG expression during colonic divided into at least two groups; REG1A, REG1B and inflammation has not been described.
    [Show full text]
  • Reg Proteins Promote Acinar-To-Ductal Metaplasia and Act As Novel Diagnostic and Prognostic Markers in Pancreatic Ductal Adenocarcinoma
    www.impactjournals.com/oncotarget/ Oncotarget, Vol. 7, No. 47 Research Paper Reg proteins promote acinar-to-ductal metaplasia and act as novel diagnostic and prognostic markers in pancreatic ductal adenocarcinoma Qing Li1,*, Hao Wang2,*, George Zogopoulos3,4, Qin Shao5, Kun Dong6, Fudong Lv6, Karam Nwilati1, Xian-yong Gui7, Adeline Cuggia4, Jun-Li Liu1, Zu-hua Gao5 1Fraser Laboratories for Diabetes Research, Department of Medicine, McGill University Health Centre, Montreal, QC, Canada 2Department of Oncology, Qingdao Municipal Hospital, School of Medicine, Qingdao University, Qingdao, China 3Department of Surgery, McGill University Health Centre, Montreal, QC, Canada 4Quebec Pancreas Cancer Study, McGill University Health Centre, Montreal, QC, Canada 5Department of Pathology, McGill University Health Centre, Montreal, QC, Canada 6Department of Pathology, You An Hospital, Capital Medical University, Beijing, China 7Department of Pathology, University of Calgary, Calgary, AB, Canada *These authors have contributed equally Correspondence to: Zu-hua Gao, email: [email protected] Jun-Li Liu, email: [email protected] Keywords: Reg family proteins, pancreatic ductal adenocarcinoma, acinar-to-ductal metaplasia, pancreatic intraepithelial neoplasia, cholangiocarcinoma Received: March 01, 2016 Accepted: October 13, 2016 Published: October 24, 2016 ABSTRACT Pancreatic ductal adenocarcinoma (PDAC) is a highly aggressive malignant tumor. Acinar-to-ductal metaplasia (ADM) and pancreatic intraepithelial neoplasia (PanIN) are both precursor lesions that lead to the development of PDAC. Reg family proteins (Reg1A, 1B, 3A/G, 4) are a group of calcium-dependent lectins that promote islet growth in response to inflammation and/or injuries. The aim of this study was to establish a role for Reg proteins in the development of PDAC and their clinical value as biomarkers.
    [Show full text]
  • Recombinant Human Reg1b Catalog Number: 2090-RG
    Recombinant Human Reg1B Catalog Number: 2090-RG DESCRIPTION Source E. coli­derived Gln23­Asn166, with an N­terminal Met Accession # P48304 N­terminal Sequence Met Analysis Predicted Molecular 16 kDa Mass SPECIFICATIONS SDS­PAGE 16 kDa, reducing conditions Activity Measured in a cell proliferation assay using RT4­D6P2T rat schwannoma cells. The ED50 for this effect is 0.15­0.75 μg/mL. Endotoxin Level <0.10 EU per 1 μg of the protein by the LAL method. Purity >95%, by SDS­PAGE with silver staining. Formulation Lyophilized from a 0.2 μm filtered solution in PBS. See Certificate of Analysis for details. PREPARATION AND STORAGE Reconstitution Reconstitute at 500 μg/mL in PBS. Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. Stability & Storage Use a manual defrost freezer and avoid repeated freeze­thaw cycles. l 12 months from date of receipt, ­20 to ­70 °C as supplied. l 1 month, 2 to 8 °C under sterile conditions after reconstitution. l 3 months, ­20 to ­70 °C under sterile conditions after reconstitution. DATA Bioactivity SDS­PAGE Recombinant Human Reg1B 1 μg/lane of Recombinant Human Reg1B (Catalog # 2090­RG) stimulates (Catalog # 2090­RG) was resolved with cell proliferation in RT4­D6P2T SDS­PAGE under reducing (R) and non­ rat schwannoma cells. The reducing (NR) conditions and visualized by ED50 for this effect is 0.15­0.75 silver staining, showing bands at 17.2 and μg/mL. 16.7 kDa, respectively. BACKGROUND Reg1B also called Lithostatine­1­β or Pancreatic stone protein 2 (PSP2) is a type I subclass member of the Reg gene family.
    [Show full text]
  • Human Lectins, Their Carbohydrate Affinities and Where to Find Them
    biomolecules Review Human Lectins, Their Carbohydrate Affinities and Where to Review HumanFind Them Lectins, Their Carbohydrate Affinities and Where to FindCláudia ThemD. Raposo 1,*, André B. Canelas 2 and M. Teresa Barros 1 1, 2 1 Cláudia D. Raposo * , Andr1 é LAQVB. Canelas‐Requimte,and Department M. Teresa of Chemistry, Barros NOVA School of Science and Technology, Universidade NOVA de Lisboa, 2829‐516 Caparica, Portugal; [email protected] 12 GlanbiaLAQV-Requimte,‐AgriChemWhey, Department Lisheen of Chemistry, Mine, Killoran, NOVA Moyne, School E41 of ScienceR622 Co. and Tipperary, Technology, Ireland; canelas‐ [email protected] NOVA de Lisboa, 2829-516 Caparica, Portugal; [email protected] 2* Correspondence:Glanbia-AgriChemWhey, [email protected]; Lisheen Mine, Tel.: Killoran, +351‐212948550 Moyne, E41 R622 Tipperary, Ireland; [email protected] * Correspondence: [email protected]; Tel.: +351-212948550 Abstract: Lectins are a class of proteins responsible for several biological roles such as cell‐cell in‐ Abstract:teractions,Lectins signaling are pathways, a class of and proteins several responsible innate immune for several responses biological against roles pathogens. such as Since cell-cell lec‐ interactions,tins are able signalingto bind to pathways, carbohydrates, and several they can innate be a immuneviable target responses for targeted against drug pathogens. delivery Since sys‐ lectinstems. In are fact, able several to bind lectins to carbohydrates, were approved they by canFood be and a viable Drug targetAdministration for targeted for drugthat purpose. delivery systems.Information In fact, about several specific lectins carbohydrate were approved recognition by Food by andlectin Drug receptors Administration was gathered for that herein, purpose. plus Informationthe specific organs about specific where those carbohydrate lectins can recognition be found by within lectin the receptors human was body.
    [Show full text]
  • A Draft Map of the Human Proteome
    ARTICLE doi:10.1038/nature13302 A draft map of the human proteome Min-Sik Kim1,2, Sneha M. Pinto3, Derese Getnet1,4, Raja Sekhar Nirujogi3, Srikanth S. Manda3, Raghothama Chaerkady1,2, Anil K. Madugundu3, Dhanashree S. Kelkar3, Ruth Isserlin5, Shobhit Jain5, Joji K. Thomas3, Babylakshmi Muthusamy3, Pamela Leal-Rojas1,6, Praveen Kumar3, Nandini A. Sahasrabuddhe3, Lavanya Balakrishnan3, Jayshree Advani3, Bijesh George3, Santosh Renuse3, Lakshmi Dhevi N. Selvan3, Arun H. Patil3, Vishalakshi Nanjappa3, Aneesha Radhakrishnan3, Samarjeet Prasad1, Tejaswini Subbannayya3, Rajesh Raju3, Manish Kumar3, Sreelakshmi K. Sreenivasamurthy3, Arivusudar Marimuthu3, Gajanan J. Sathe3, Sandip Chavan3, Keshava K. Datta3, Yashwanth Subbannayya3, Apeksha Sahu3, Soujanya D. Yelamanchi3, Savita Jayaram3, Pavithra Rajagopalan3, Jyoti Sharma3, Krishna R. Murthy3, Nazia Syed3, Renu Goel3, Aafaque A. Khan3, Sartaj Ahmad3, Gourav Dey3, Keshav Mudgal7, Aditi Chatterjee3, Tai-Chung Huang1, Jun Zhong1, Xinyan Wu1,2, Patrick G. Shaw1, Donald Freed1, Muhammad S. Zahari2, Kanchan K. Mukherjee8, Subramanian Shankar9, Anita Mahadevan10,11, Henry Lam12, Christopher J. Mitchell1, Susarla Krishna Shankar10,11, Parthasarathy Satishchandra13, John T. Schroeder14, Ravi Sirdeshmukh3, Anirban Maitra15,16, Steven D. Leach1,17, Charles G. Drake16,18, Marc K. Halushka15, T. S. Keshava Prasad3, Ralph H. Hruban15,16, Candace L. Kerr19{, Gary D. Bader5, Christine A. Iacobuzio-Donahue15,16,17, Harsha Gowda3 & Akhilesh Pandey1,2,3,4,15,16,20 The availability of human genome sequence has transformed biomedical research over the past decade. However, an equiv- alent map for the human proteome with direct measurements of proteins and peptides does not exist yet. Here we present a draft map of the human proteome using high-resolution Fourier-transform mass spectrometry.
    [Show full text]
  • Human REG1B / PSPS2 Protein (His Tag)
    Human REG1B / PSPS2 Protein (His Tag) Catalog Number: 11638-H08H General Information SDS-PAGE: Gene Name Synonym: PSPS2; REGH; REGI-BETA; REGL Protein Construction: A DNA sequence encoding the human REG1B (NP_006498.1) (Met 1-Asn 166) was fused with a polyhistidine tag at the C-terminus. Source: Human Expression Host: HEK293 Cells QC Testing Purity: > 95 % as determined by SDS-PAGE Endotoxin: Protein Description < 1.0 EU per μg of the protein as determined by the LAL method Regenerating gene (Reg), first isolated from a regenerating islet cDNA Stability: library, encodes a secretory protein with a growth stimulating effect on pancreatic beta cells, and could be associated with fibrocalculous Samples are stable for up to twelve months from date of receipt at -70 ℃ pancreatopathy. Reg and Reg-related genes which were expressed in various organs have been revealed to constitute a multigene family, the Predicted N terminal: Gln 23 Reg family consisting of four subtypes (types I, II, III, IV) and are involved Molecular Mass: in cancers and neurodegenerative diseases. Regenerating islet-derived 1 beta (REG1B), also known as Lithostathine-1-beta and Pancreatic stone The recombinant human REG1B consists of 155 amino acids and protein 2 (PSPS2), is a types I Reg protein and contains one typical C-type predictes a molecular mass of 17.7 kDa. In SDS-PAGE under reducing lectin domain. REG1B is a 166-amino acid protein which has 22 amino acid conditions, the apparent molecular mass of rh REG1B is approximately 19- substitutions in comparison with the previously isolated human REG1A, 21 kDa due to different glycosylation.
    [Show full text]
  • Mouse REG1A Antibody
    Published on Cell Applications (https://www.cellapplications.com) Home > Anti-REG1A: Mouse REG1A Antibody Anti-REG1A: Mouse REG1A Antibody Description Details Products Resources Product Sheet CP10353 Description ACKGROUND Regenerating gene (Reg), which is expressed in regenerating pancreatic islet, was first identified in the screening of regenerating islet-derived cDNA library taken from 90% depancreatized rat. Reg and Reg-related genes constitute a family within the superfamily of calcium-dependent lectin (C-type lectin). The C-type lectins are involved in several complex events, such as human malignancy and other diseases. The Reg gene family consists of a group of acute phase reactants, lectins, antiapoptotic factors, or growth factors for pancreatic islet cells, neural cells, and epithelial cells in the digestive system. Until now, 17 members of the Reg family have been identified and classified into four classes (Reg I-IV), based on the primary structures of the encoded proteins. Reg I proteins have two members of human REG I gene, REG1A and REG1B. Regenerating gene I alpha (REG1A) encodes a 166-amino-acid protein with a 22-amino-acid signal sequence. The REG1A protein is identical to the pancreatic thread protein, pancreatic stone protein, or protein X, and is highly represented in human pancreatic secretion. REG1A protein is a known growth factor affecting pancreatic islet beta cells and is secreted by the exocrine pancreas. It is associated with islet cell regeneration and diabetogenesis and may be involved in pancreatic lithogenesis. The REG1B gene codes for a transcript with 87% homology to the REG1A transcript. The secretory Reg I protein is synthesized in the regenerating beta cells, and through the Reg I receptor, stimulates the proliferation of pancreatic beta cells, leading to an increase in the beta cells mass in 90% depancreatized rats and nonobese diabetic mice and hence amelioration of experimental diabetes.
    [Show full text]
  • LJELSR: a Strengthened Version of JELSR for Feature Selection and Clustering
    Article LJELSR: A Strengthened Version of JELSR for Feature Selection and Clustering Sha-Sha Wu 1, Mi-Xiao Hou 1, Chun-Mei Feng 1,2 and Jin-Xing Liu 1,* 1 School of Information Science and Engineering, Qufu Normal University, Rizhao 276826, China; [email protected] (S.-S.W.); [email protected] (M.-X.H.); [email protected] (C.-M.F.) 2 Bio-Computing Research Center, Harbin Institute of Technology, Shenzhen 518055, China * Correspondence: [email protected]; Tel.: +086-633-3981-241 Received: 4 December 2018; Accepted: 7 February 2019; Published: 18 February 2019 Abstract: Feature selection and sample clustering play an important role in bioinformatics. Traditional feature selection methods separate sparse regression and embedding learning. Later, to effectively identify the significant features of the genomic data, Joint Embedding Learning and Sparse Regression (JELSR) is proposed. However, since there are many redundancy and noise values in genomic data, the sparseness of this method is far from enough. In this paper, we propose a strengthened version of JELSR by adding the L1-norm constraint on the regularization term based on a previous model, and call it LJELSR, to further improve the sparseness of the method. Then, we provide a new iterative algorithm to obtain the convergence solution. The experimental results show that our method achieves a state-of-the-art level both in identifying differentially expressed genes and sample clustering on different genomic data compared to previous methods. Additionally, the selected differentially expressed genes may be of great value in medical research. Keywords: differentially expressed genes; feature selection; L1-norm; sample clustering; sparse constraint 1.
    [Show full text]
  • ATAP00191-Recombinant Human Reg1b Protein
    ATAGENIX LABORATORIES Catalog Number:ATAP00191 Recombinant Human REG1b protein Product Details Summary English name Recombinant Human REG1b protein Purity >90% as determined by SDS-PAGE Endotoxin level Please contact with the lab for this information. Construction A DNA sequence encoding the human REG1b (Gln23-Asn166) was fused with His tag Accession # P48304 Host E.coli Species Homo sapiens (Human) Predicted Molecular Mass 18.12 kDa Formulation Supplied as solution form in PBS pH 7.5 or lyophilized from PBS pH 7.5. Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. Stability &Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8 °C for one week . Store at -20 to -80 °C for twelve months from the date of receipt. Reconstitution Reconstitute in sterile water for a stock solution.A copy of datasheet will be provided with the products, please refer to it for details. Background Background Regenerating gene (Reg), first isolated from a regenerating islet cDNA library, encodes a secretory protein with a growth stimulating effect on pancreatic beta cells, and could be associated with fibrocalculous pancreatopathy. Reg and Reg- related genes which were expressed in various organs have been revealed to constitute a multigene family, the Reg family consisting of four subtypes (types I, II, III, IV) and are involved in cancers and neurodegenerative diseases. Regenerating islet-derived 1 beta (REG1B), also known as Lithostathine-1-beta and Pancreatic stone protein 2 (PSPS2), is a types I Reg protein and contains one typical C-type lectin domain.
    [Show full text]
  • Molecular Changes in the Non-Inflamed Terminal Ileum Of
    cells Article Molecular Changes in the Non-Inflamed Terminal Ileum of Patients with Ulcerative Colitis 1,2, 3, 1 1 3,4 Ho-Su Lee y , Maaike Vancamelbeke y, Sare Verstockt , Tom Wilms , Bram Verstockt , João Sabino 3,4, Marc Ferrante 3,4 ,Séverine Vermeire 3,4 and Isabelle Cleynen 1,* 1 Laboratory of Complex Genetics, Department of Human Genetics, KU Leuven, 3000 Leuven, Belgium; [email protected] (H.-S.L.); [email protected] (S.V.); [email protected] (T.W.) 2 Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine, Seoul 05505, Korea 3 Translational Research Center for Gastrointestinal Disorders (TARGID), Department Chronic Diseases, Metabolism & Ageing (CHROMETA), KU Leuven, 3000 Leuven, Belgium; [email protected] (M.V.); [email protected] (B.V.); [email protected] (J.S.); [email protected] (M.F.); [email protected] (S.V.) 4 Department of Gastroenterology and Hepatology, University Hospitals Leuven, KU Leuven, 3000 Leuven, Belgium * Correspondence: [email protected]; Tel.: +32-1637-7480 These authors have contributed equally to this work. y Received: 22 June 2020; Accepted: 24 July 2020; Published: 28 July 2020 Abstract: Ulcerative colitis is a chronic inflammatory disease confined to the colon. Although the etiopathogenesis remains unknown, small bowel dysfunctions like histological and permeability alterations have been described in ulcerative colitis. We evaluated the molecular gene signature in the non-inflamed terminal ileum of 36 ulcerative colitis patients (7 active, with Mayo endoscopic subscore 2, and 29 inactive) as compared to 15 non-inflammatory bowel disease controls.
    [Show full text]