Invited Review: Genetic and Genomic Mouse Models for Livestock Research
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Comparative Biochemistry and Physiology, Part D, Vol. 5, Pp. 45-54 (2010)
Comparative genomics and proteomics of vertebrate diacylglycerol acyltransferase (DGAT), acyl CoA wax alcohol acyltransferase (AWAT) and monoacylglycerol acyltransferase (MGAT) Author Holmes, Roger S Published 2010 Journal Title Comparative Biochemistry and Physiology, Part D DOI https://doi.org/10.1016/j.cbd.2009.09.004 Copyright Statement © 2010 Elsevier. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal's website for access to the definitive, published version. Downloaded from http://hdl.handle.net/10072/36786 Griffith Research Online https://research-repository.griffith.edu.au Comparative Biochemistry and Physiology, Part D, Vol. 5, pp. 45-54 (2010) COMPARATIVE GENOMICS AND PROTEOMICS OF VERTEBRATE DIACYLGLYCEROL ACYLTRANSFERASE (DGAT), ACYL CoA WAX ALCOHOL ACYLTRANSFERASE (AWAT) AND MONOACYLGLYCEROL ACYLTRANSFERASE (MGAT) Roger S Holmes School of Biomolecular and Physical Sciences, Griffith University, Nathan 4111 Brisbane Queensland Australia Email: [email protected] Keywords: Diacylglycerol acyltransferase-Monoacylglycerol transferase-Human- Mouse-Opossum-Zebrafish-Genetics-Evolution-X chromosome Running Head: Genomics and proteomics of vertebrate acylglycerol acyltransferases ABSTRACT BLAT (BLAST-Like Alignment Tool) analyses of the opossum (Monodelphis domestica) and zebrafish (Danio rerio) genomes were undertaken using amino acid sequences of the acylglycerol acyltransferase (AGAT) superfamily. Evidence is reported for 8 opossum monoacylglycerol acyltransferase-like (MGAT) (E.C. 2.3.1.22) and diacylglycerol acyltransferase-like (DGAT) (E.C. 2.3.1.20) genes and proteins, including DGAT1, DGAT2, DGAT2L6 (DGAT2-like protein 6), AWAT1 (acyl-CoA wax alcohol acyltransferase 1), AWAT2, MGAT1, MGAT2 and MGAT3. Three of these genes (AWAT1, AWAT2 and DGAT2L6) are closely localized on the opossum X chromosome. -
Supporting Information
Supporting Information Seo et al. 10.1073/pnas.0910268107 SI Materials and Methods of Iowa Proteomics Facility and analyzed with LTQ XL linear Plasmids and Antibodies. All expression plasmids were constructed ion trap mass spectrometer (Thermo Scientific). with human BBS genes in pCS2 and phCMV2 backbone with fi fi fi indicated tags at the N terminus. Deletion and point mutagenesis Tandem Af nity Puri cation. Constructs for tandem af nity puri- fi was performed using PfuUltra II Fusion HS DNA polymerase cation of BBS5 and BBS7 were generated with N-terminal (Stratagene) and appropriate primers (Integrated DNA Tech- 3xFLAG tag and S tag in CS2 plasmid (FS-BBS5 and FS-BBS7, nology). Primer sequences are available upon request. For RNAi respectively). Stable HEK293T cell lines expressing these genes of BBS6 and BBS12, we generated stable HEK293T cell lines were established and proteins associated with BBS5 and BBS7 fi fi expressing shRNAs against these genes (GIPZ shRNAmir; were tandem af nity puri ed using anti-FLAG and S-protein OpenBiosystems). Expression of BBS10, CCT1, CCT2, and (Novagen) affinity gels. Others are same as above. Protein CCT3 was blocked by transient transfection of siRNAs (ON- identities were determined by Western blotting. TARGETplus SMARTpool; Dharmacon). For RNAi control, we used Nonsilencing GIPZ vector (OpenBiosystems) and ON- Quantitative RT-PCR. Total RNA was extracted from HEK293T TARGETplus Non-Targeting Pool siRNAs (Dharmacon). Anti- cells or mouse testis and eye with TRIzol Reagent (Invitrogen) ’ μ bodies against BBS1, BBS2, BBS4, and BBS7 were described following the manufacturer s instructions. A 1- g quantity of previously (1). -
Knockdown of the BBS10 Gene Product
ndrom Sy es tic & e G n e e n G e f T o Zacchia et al., J Genet Syndr Gene Ther 2014, 5:3 Journal of Genetic Syndromes h l e a r n a DOI: 10.4172/2157-7412.1000222 r p u y o J ISSN: 2157-7412 & Gene Therapy Research Article Open Access Knockdown of the BBS10 Gene Product Affects Apical Targeting of AQP2 in Renal Cells: A Possible Explanation for the Polyuria Associated with Bardet-Biedl Syndrome Miriam Zacchia1, Gabriella Esposito2,3, Monica Carmosino7, Claudia Barbieri7, Enza Zacchia1,5, Alessia Anna Crispo2, Tiziana Fioretti2,3, Francesco Trepiccione1, Valentina Di Iorio6, Francesca Simonelli6, Francesco Salvatore2,4, Giovambattista Capasso1, Maria Svelto7,8 and Giuseppe Procino7,8* 1Chair of Nephrology, Second University of Naples, Italy 2CEINGE-Biotecnologie Avanzate s.c. a r.l., Naples, Italy 3Department of Molecular Medicine and Medical Biotechnologies, University of Naples Federico II, Italy 4IRCCS SDN Foundation Naples, Italy 5Institute of Genetics and Biophysics of the National Research Council (CNR), Naples, Italy 6Eye Clinic, Multidisciplinary Department of Medical, Surgical and Dental Sciences - Second University of Naples, Italy 7Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari, Italy 8Center of Excellence in Comparative Genomics, Bari, Italy Abstract Objective: Bardet-Biedl syndrome (BBS) is a rare genetic disorder whose clinical features include renal abnormalities, which ranges from renal malformations to renal failure. Polyuria and iso-hyposthenuria are common renal dysfunctions in BBS patients even in the presence of normal GFR. The mechanism underlying this defect is unknown and no genotype-phenotype correlation has yet been reported. -
Transmission Distortion and Genetic Incompatibilities Between Alleles in A
bioRxiv preprint doi: https://doi.org/10.1101/2021.06.09.447720; this version posted June 10, 2021. 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-ND 4.0 International license. 1 Transmission distortion and genetic incompatibilities between alleles in a 2 multigenerational mouse advanced intercross line 3 Danny Arends, [email protected], Albrecht Daniel Thaer-Institut für Agrar- und 4 Gartenbauwissenschaften, Humboldt-Universität zu Berlin, Invalidenstraße 42, D-10115 Berlin, 5 Germany 6 Stefan Kärst, [email protected], Albrecht Daniel Thaer-Institut für Agrar- und 7 Gartenbauwissenschaften, Humboldt-Universität zu Berlin, Invalidenstraße 42, D-10115 Berlin, 8 Germany 9 Sebastian Heise, [email protected], Albrecht Daniel Thaer-Institut für Agrar- und 10 Gartenbauwissenschaften, Humboldt-Universität zu Berlin, Invalidenstraße 42, D-10115 Berlin, 11 Germany 12 Paula Korkuc, [email protected], Albrecht Daniel Thaer-Institut für Agrar- und 13 Gartenbauwissenschaften, Humboldt-Universität zu Berlin, Invalidenstraße 42, D-10115 Berlin, 14 Germany 15 Deike Hesse, [email protected], Albrecht Daniel Thaer-Institut für Agrar- und 16 Gartenbauwissenschaften, Humboldt-Universität zu Berlin, Invalidenstraße 42, D-10115 Berlin, 17 Germany 18 Gudrun A. Brockmann†, [email protected], Albrecht Daniel Thaer-Institut für Agrar- 19 und Gartenbauwissenschaften, Humboldt-Universität zu Berlin, Invalidenstraße 42, D-10115 Berlin, 20 Germany 21 † To whom correspondence should be addressed. 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.06.09.447720; this version posted June 10, 2021. -
BBS7 Is Required for Bbsome Formation and Its Absence in Mice
2372 Research Article BBS7 is required for BBSome formation and its absence in mice results in Bardet-Biedl syndrome phenotypes and selective abnormalities in membrane protein trafficking Qihong Zhang1, Darryl Nishimura1, Tim Vogel2, Jianqiang Shao3, Ruth Swiderski1, Terry Yin4, Charles Searby1, Calvin S. Carter5, GunHee Kim1, Kevin Bugge1, Edwin M. Stone6 and Val C. Sheffield1,* 1Department of Pediatrics, Howard Hughes Medical Institute, University of Iowa, Iowa City, IA 52242, USA 2Department of Neurosurgery, University of Iowa, Iowa City, IA 52242, USA 3Central Microscopy Research Facilities, University of Iowa, Iowa City, IA 52242, USA 4Department of Internal Medicine, University of Iowa, Iowa City, IA 52242, USA 5Program in Neuroscience, University of Iowa, Iowa City, IA 52242, USA 6Department of Ophthalmology and Visual Sciences, Howard Hughes Medical Institute, University of Iowa, Iowa City 52242, USA *Author for correspondence ([email protected]) Accepted 18 March 2013 Journal of Cell Science 126, 2372–2380 ß 2013. Published by The Company of Biologists Ltd doi: 10.1242/jcs.111740 Summary Bardet-Biedl Syndrome (BBS) is a pleiotropic and genetically heterozygous disorder caused independently by numerous genes (BBS1– BBS17). Seven highly conserved BBS proteins (BBS1, 2, 4, 5, 7, 8 and 9) form a complex known as the BBSome, which functions in ciliary membrane biogenesis. BBS7 is both a unique subunit of the BBSome and displays direct physical interaction with a second BBS complex, the BBS chaperonin complex. To examine the in vivo function of BBS7, we generated Bbs7 knockout mice. Bbs72/2 mice show similar phenotypes to other BBS gene mutant mice including retinal degeneration, obesity, ventriculomegaly and male infertility characterized by abnormal spermatozoa flagellar axonemes. -
BBS6, BBS10, and BBS12 Form a Complex with CCT/Tric Family Chaperonins and Mediate Bbsome Assembly
BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly Seongjin Seoa,c, Lisa M. Bayeb, Nathan P. Schulza,c, John S. Becka,c, Qihong Zhanga,c, Diane C. Slusarskib, and Val C. Sheffielda,c,1 aDepartment of Pediatrics, bDepartment of Biology, and cHoward Hughes Medical Institute, University of Iowa, Iowa City, IA 52242 Edited by Kathryn V. Anderson, Sloan-Kettering Institute, New York, NY, and approved November 25, 2009 (received for review September 9, 2009) Bardet-Biedl syndrome (BBS) is a human genetic disorder resulting one component of the BBSome, BBS1, directly interacts with the in obesity, retinal degeneration, polydactyly, and nephropathy. leptin receptor and that leptin signaling is attenuated in BBS Recent studies indicate that trafficking defects to the ciliary mem- gene knockout mice, implicating BBS function in a broad range brane are involved in this syndrome. Here, we show that a novel of membrane receptor signaling (33). complex composed of three chaperonin-like BBS proteins (BBS6, Three of the remaining BBS proteins (BBS6, BBS10, and BBS10, and BBS12) and CCT/TRiC family chaperonins mediates BBS12) have sequence homology to the CCT (also known as BBSome assembly, which transports vesicles to the cilia. Chaperonin- TRiC) family of group II chaperonins (17, 24, 25). CCT proteins like BBS proteins interact with a subset of BBSome subunits and form an ≈900 kDa hetero-oligomeric complex that mediates promote their association with CCT chaperonins. CCT activity is protein folding in an ATP-dependent manner (34, 35). The CCT essential for BBSome assembly, and knockdown of CCT chaperonins complex consists of two stacked rings, each of which is composed in zebrafish results in BBS phenotypes. -
UC San Francisco Previously Published Works
UCSF UC San Francisco Previously Published Works Title FitSNPs: highly differentially expressed genes are more likely to have variants associated with disease. Permalink https://escholarship.org/uc/item/91k8p2km Journal Genome biology, 9(12) ISSN 1474-7596 Authors Chen, Rong Morgan, Alex A Dudley, Joel et al. Publication Date 2008 DOI 10.1186/gb-2008-9-12-r170 Peer reviewed eScholarship.org Powered by the California Digital Library University of California Open Access Research2008ChenetVolume al. 9, Issue 12, Article R170 FitSNPs: highly differentially expressed genes are more likely to have variants associated with disease Rong Chen*†‡, Alex A Morgan*†‡, Joel Dudley*†‡, Tarangini Deshpande§, Li Li†, Keiichi Kodama*†‡, Annie P Chiang*†‡ and Atul J Butte*†‡ Addresses: *Stanford Center for Biomedical Informatics Research, 251 Cmpus Drive, Stanford, CA 94305, USA. †Department of Pediatrics, Stanford University School of Medicine, Stanford, CA 94305, USA. ‡Lucile Packard Children's Hospital, 725 Welch Road, Palo Alto, CA 94304, USA. §NuMedii Inc., Menlo Park, CA 94025, USA. Correspondence: Atul J Butte. Email: [email protected] Published: 5 December 2008 Received: 17 June 2008 Revised: 26 September 2008 Genome Biology 2008, 9:R170 (doi:10.1186/gb-2008-9-12-r170) Accepted: 5 December 2008 The electronic version of this article is the complete one and can be found online at http://genomebiology.com/2008/9/12/R170 © 2008 Chen et al.; licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. -
Microrna-124-3P Suppresses Mouse Lip Mesenchymal Cell Proliferation
Suzuki et al. BMC Genomics (2019) 20:852 https://doi.org/10.1186/s12864-019-6238-4 RESEARCH ARTICLE Open Access MicroRNA-124-3p suppresses mouse lip mesenchymal cell proliferation through the regulation of genes associated with cleft lip in the mouse Akiko Suzuki1,2, Hiroki Yoshioka1,2, Dima Summakia1, Neha G. Desai1,3, Goo Jun3,4, Peilin Jia5, David S. Loose4,6, Kenichi Ogata1,2, Mona V. Gajera1,3, Zhongming Zhao3,4,5 and Junichi Iwata1,2,4* Abstract Background: Cleft lip (CL), one of the most common congenital birth defects, shows considerable geographic and ethnic variation, with contribution of both genetic and environmental factors. Mouse genetic studies have identified several CL-associated genes. However, it remains elusive how these CL-associated genes are regulated and involved in CL. Environmental factors may regulate these genes at the post-transcriptional level through the regulation of non-coding microRNAs (miRNAs). In this study, we sought to identify miRNAs associated with CL in mice. Results: Through a systematic literature review and a Mouse Genome Informatics (MGI) database search, we identified 55 genes that were associated with CL in mice. Subsequent bioinformatic analysis of these genes predicted that a total of 33 miRNAs target multiple CL-associated genes, with 20 CL-associated genes being potentially regulated by multiple miRNAs. To experimentally validate miRNA function in cell proliferation, we conducted cell proliferation/viability assays for the selected five candidate miRNAs (miR-124-3p, let-7a-5p, let-7b-5p, let-7c-5p, and let-7d-5p). Overexpression of miR-124-3p, but not of the others, inhibited cell proliferation through suppression of CL-associated genes in cultured mouse embryonic lip mesenchymal cells (MELM cells) isolated from the developing mouse lip region. -
Defects and Compromised Intraflagellar Transport BBS-7 and BBS-8 Protein Function Results in Cilia C. Elegans Loss Of
Downloaded from www.genesdev.org on April 17, 2007 Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport Oliver E. Blacque, Michael J. Reardon, Chunmei Li, Jonathan McCarthy, Moe R. Mahjoub, Stephen J. Ansley, Jose L. Badano, Allan K. Mah, Philip L. Beales, William S. Davidson, Robert C. Johnsen, Mark Audeh, Ronald H.A. Plasterk, David L. Baillie, Nicholas Katsanis, Lynne M. Quarmby, Stephen R. Wicks and Michel R. Leroux Genes & Dev. 2004 18: 1630-1642 Access the most recent version at doi:10.1101/gad.1194004 Supplementary "Supplemental Research Data-1" data http://www.genesdev.org/cgi/content/full/18/13/1630/DC1 References This article cites 41 articles, 16 of which can be accessed free at: http://www.genesdev.org/cgi/content/full/18/13/1630#References Article cited in: http://www.genesdev.org/cgi/content/full/18/13/1630#otherarticles Email alerting Receive free email alerts when new articles cite this article - sign up in the box at the service top right corner of the article or click here Notes To subscribe to Genes and Development go to: http://www.genesdev.org/subscriptions/ © 2004 Cold Spring Harbor Laboratory Press Downloaded from www.genesdev.org on April 17, 2007 Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport Oliver E. Blacque,1 Michael J. Reardon,2 Chunmei Li,1 Jonathan McCarthy,1 Moe R. Mahjoub,3 Stephen J. Ansley,4 Jose L. Badano,4 Allan K. Mah,1 Philip L. -
BBS6, BBS10, and BBS12 Form a Complex with CCT/Tric Family Chaperonins and Mediate Bbsome Assembly
BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly Seongjin Seoa,c, Lisa M. Bayeb, Nathan P. Schulza,c, John S. Becka,c, Qihong Zhanga,c, Diane C. Slusarskib, and Val C. Sheffielda,c,1 aDepartment of Pediatrics, bDepartment of Biology, and cHoward Hughes Medical Institute, University of Iowa, Iowa City, IA 52242 Edited by Kathryn V. Anderson, Sloan-Kettering Institute, New York, NY, and approved November 25, 2009 (received for review September 9, 2009) Bardet-Biedl syndrome (BBS) is a human genetic disorder resulting one component of the BBSome, BBS1, directly interacts with the in obesity, retinal degeneration, polydactyly, and nephropathy. leptin receptor and that leptin signaling is attenuated in BBS Recent studies indicate that trafficking defects to the ciliary mem- gene knockout mice, implicating BBS function in a broad range brane are involved in this syndrome. Here, we show that a novel of membrane receptor signaling (33). complex composed of three chaperonin-like BBS proteins (BBS6, Three of the remaining BBS proteins (BBS6, BBS10, and BBS10, and BBS12) and CCT/TRiC family chaperonins mediates BBS12) have sequence homology to the CCT (also known as BBSome assembly, which transports vesicles to the cilia. Chaperonin- TRiC) family of group II chaperonins (17, 24, 25). CCT proteins like BBS proteins interact with a subset of BBSome subunits and form an ≈900 kDa hetero-oligomeric complex that mediates promote their association with CCT chaperonins. CCT activity is protein folding in an ATP-dependent manner (34, 35). The CCT essential for BBSome assembly, and knockdown of CCT chaperonins complex consists of two stacked rings, each of which is composed in zebrafish results in BBS phenotypes. -
Ciliary Genes in Renal Cystic Diseases
cells Review Ciliary Genes in Renal Cystic Diseases Anna Adamiok-Ostrowska * and Agnieszka Piekiełko-Witkowska * Department of Biochemistry and Molecular Biology, Centre of Postgraduate Medical Education, 01-813 Warsaw, Poland * Correspondence: [email protected] (A.A.-O.); [email protected] (A.P.-W.); Tel.: +48-22-569-3810 (A.P.-W.) Received: 3 March 2020; Accepted: 5 April 2020; Published: 8 April 2020 Abstract: Cilia are microtubule-based organelles, protruding from the apical cell surface and anchoring to the cytoskeleton. Primary (nonmotile) cilia of the kidney act as mechanosensors of nephron cells, responding to fluid movements by triggering signal transduction. The impaired functioning of primary cilia leads to formation of cysts which in turn contribute to development of diverse renal diseases, including kidney ciliopathies and renal cancer. Here, we review current knowledge on the role of ciliary genes in kidney ciliopathies and renal cell carcinoma (RCC). Special focus is given on the impact of mutations and altered expression of ciliary genes (e.g., encoding polycystins, nephrocystins, Bardet-Biedl syndrome (BBS) proteins, ALS1, Oral-facial-digital syndrome 1 (OFD1) and others) in polycystic kidney disease and nephronophthisis, as well as rare genetic disorders, including syndromes of Joubert, Meckel-Gruber, Bardet-Biedl, Senior-Loken, Alström, Orofaciodigital syndrome type I and cranioectodermal dysplasia. We also show that RCC and classic kidney ciliopathies share commonly disturbed genes affecting cilia function, including VHL (von Hippel-Lindau tumor suppressor), PKD1 (polycystin 1, transient receptor potential channel interacting) and PKD2 (polycystin 2, transient receptor potential cation channel). Finally, we discuss the significance of ciliary genes as diagnostic and prognostic markers, as well as therapeutic targets in ciliopathies and cancer. -
DGAT1 Missense Mutation Associated with Congenital Diarrhea[S]
Identification and characterization of a novel DGAT1 missense mutation associated with congenital diarrhea[S] The Harvard community has made this article openly available. Please share how this access benefits you. Your story matters Citation Gluchowski, N. L., C. Chitraju, J. A. Picoraro, N. Mejhert, S. Pinto, W. Xin, D. S. Kamin, et al. 2017. “Identification and characterization of a novel DGAT1 missense mutation associated with congenital diarrhea[S].” Journal of Lipid Research 58 (6): 1230-1237. doi:10.1194/jlr.P075119. http://dx.doi.org/10.1194/jlr.P075119. Published Version doi:10.1194/jlr.P075119 Citable link http://nrs.harvard.edu/urn-3:HUL.InstRepos:33490961 Terms of Use This article was downloaded from Harvard University’s DASH repository, and is made available under the terms and conditions applicable to Other Posted Material, as set forth at http:// nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of- use#LAA patient-oriented and epidemiological research Author’s Choice Identification and characterization of a novel DGAT1 missense mutation associated with congenital diarrhea Nina L. Gluchowski,*,†,§ Chandramohan Chitraju,†,§ Joseph A. Picoraro,** Niklas Mejhert,†,§ Shirly Pinto,†† Winnie Xin,§,§§ Daniel S. Kamin,*,§ Harland S. Winter,§,*** Wendy K. Chung,††† Tobias C. Walther,1,2,†,§,§§§,**** and Robert V. Farese, Jr.1,2,†,§,§§§ Division of Gastroenterology and Nutrition,* Boston Children’s Hospital, Boston, MA 02115; Department of Genetics and Complex Diseases,† Harvard T. H. Chan School of Public Health, Boston, MA