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Collagen and Elastin Fibres
J Clin Pathol: first published as 10.1136/jcp.s3-12.1.49 on 1 January 1978. Downloaded from J. clin. Path., 31, Suppl. (Roy. Coll. Path.), 12, 49-58 Collagen and elastin fibres A. J. BAILEY From the Agricultural Research Council, Meat Research Institute, Langford, Bristol Although an understanding of the intracellular native collagen was generated from type I pro- biosynthesis of both collagen and elastin is of collagen. Whether this means that the two pro- considerable importance it is the subsequent extra- collagens are converted by different enzyme systems cellular changes involving fibrogenesis and cross- and the type III enzyme was deficient in these linking that ensure that these proteins ultimately fibroblast cultures, or that the processing of pro become the major supporting tissues of the body. type III is extremely slow, is not known. The latter This paper summarises the formation and stability proposal is consistent with the higher proportion of collagen and elastin fibres. of soluble pro type III extractable from tissue (Lenaers and Lapiere, 1975; Timpl et al., 1975). Collagen Basement membrane collagens, on the other hand, do not form fibres and this property may be The non-helical regions at the ends of the triple due to the retention of the non-helical extension helix of procollagen probably provide a number of peptides (Kefalides, 1973). In-vivo biosynthetic different intracellular functions-that is, initiating studies showing the absence of any extension peptide rapid formation of the triple helix; inhibiting intra- removal support this (Minor et al., 1976), but other cellular fibrillogenesis; and facilitating transmem- workers have reported that there is some cleavage brane movement. -
Synthetic Polynucleotides Synthetische Polynukleotide Polynucleotides Synthetiques
Europäisches Patentamt *EP000960192B1* (19) European Patent Office Office européen des brevets (11) EP 0 960 192 B1 (12) EUROPEAN PATENT SPECIFICATION (45) Date of publication and mention (51) Int Cl.7: C12N 9/02, C12N 15/53, of the grant of the patent: A61K 38/43, C12N 9/06 09.11.2005 Bulletin 2005/45 (86) International application number: (21) Application number: 97933592.4 PCT/AU1997/000505 (22) Date of filing: 11.08.1997 (87) International publication number: WO 1998/006830 (19.02.1998 Gazette 1998/07) (54) SYNTHETIC POLYNUCLEOTIDES SYNTHETISCHE POLYNUKLEOTIDE POLYNUCLEOTIDES SYNTHETIQUES (84) Designated Contracting States: • SHARP P M ET AL: "The codon Adaptation AT BE CH DE DK ES FI FR GB GR IE IT LI LU MC Index--a measure of directional synonymous NL PT SE codon usage bias, and its potential applications." NUCLEIC ACIDS RESEARCH. (30) Priority: 09.08.1996 AU PO156596 ENGLAND 11 FEB 1987, vol. 15, no. 3, 11 February 1987 (1987-02-11), pages 1281-1295, (43) Date of publication of application: XP001122356 ISSN: 0305-1048 01.12.1999 Bulletin 1999/48 • DATABASE SWISSPROT [Online] 1 December 1992 (1992-12-01) MARIANI T.J. ET AL.: (60) Divisional application: "Protein-lysine 6-oxidase precursor (EC 05000327.6 1.4.3.13) (Lysyl oxidase)." Database accession no. P28300 XP002229125 (73) Proprietor: THE UNIVERSITY OF SYDNEY • DATABASE EMBL [Online] EBI; 16 May 1992 Sydney, New South Wales 2006 (AU) (1992-05-16) MARIANI T.J. ET AL.: "Human lysyl oxidase (LOX) mRNA, complete cds." Database (72) Inventor: WEISS, Anthony, Steven accession no. M94054 XP002229126 Randwick, NSW 2031 (AU) • DATABASE EMBL [Online] EBI; 26 November 1993 (1993-11-26) HAMALAINEN E.R. -
Protein Import Into Isolated Pea Root Leucoplasts
ORIGINAL RESEARCH published: 04 September 2015 doi: 10.3389/fpls.2015.00690 Protein import into isolated pea root leucoplasts Chiung-Chih Chu and Hsou-min Li* Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan Leucoplasts are important organelles for the synthesis and storage of starch, lipids and proteins. However, molecular mechanism of protein import into leucoplasts and how it differs from that of import into chloroplasts remain unknown. We used pea seedlings for both chloroplast and leucoplast isolations to compare within the same species. We further optimized the isolation and import conditions to improve import efficiency and to permit a quantitative comparison between the two plastid types. The authenticity of the import was verified using a mitochondrial precursor protein. Our results show that, when normalized to Toc75, most translocon proteins are less abundant in leucoplasts than in chloroplasts. A precursor shown to prefer the receptor Toc132 indeed had relatively more similar import efficiencies between chloroplasts and leucoplasts compared to precursors that prefer Toc159. Furthermore we found two precursors that exhibited very high import efficiency into leucoplasts. Their transit peptides may be candidates Edited by: for delivering transgenic proteins into leucoplasts and for analyzing motifs important for Bo Liu, University of California, Davis, USA leucoplast import. Reviewed by: Keywords: leucoplasts, plastid, root, protein import, translocon Kentaro Inoue, University of California, Davis, USA Danny Schnell, Introduction University of Massachusetts, USA *Correspondence: Plastids are essential plant organelles responsible for functions ranging from photosynthesis and Hsou-min Li, biosynthesis of amino acids and fatty acids to assimilation of nitrogen and sulfur (Leister, 2003; Institute of Molecular Biology, Sakamoto et al., 2008). -
Methods, Compounds, Compositions and Vehicles for Delivering 3-Amino-1-Propanesulfonic Acid
(19) TZZ _ T (11) EP 2 862 581 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 22.04.2015 Bulletin 2015/17 A61K 47/48 (2006.01) C07K 5/06 (2006.01) C07K 5/08 (2006.01) C07C 309/15 (2006.01) (2006.01) (2006.01) (21) Application number: 14200552.9 C07D 207/16 C07D 209/20 C07D 217/24 (2006.01) C07D 233/64 (2006.01) (2006.01) (2006.01) (22) Date of filing: 12.10.2007 C07D 291/02 C07D 333/24 C12P 11/00 (2006.01) A61K 38/07 (2006.01) A61K 38/08 (2006.01) A61P 25/28 (2006.01) (84) Designated Contracting States: (72) Inventor: The designation of the inventor has not AT BE BG CH CY CZ DE DK EE ES FI FR GB GR yet been filed HU IE IS IT LI LT LU LV MC MT NL PL PT RO SE SI SK TR (74) Representative: Hoffmann Eitle Patent- und Rechtsanwälte PartmbB (30) Priority: 12.10.2006 US 851039 P Arabellastraße 30 12.04.2007 US 911459 P 81925 München (DE) (62) Document number(s) of the earlier application(s) in Remarks: accordance with Art. 76 EPC: This application was filed on 30-12-2014 as a 07875176.5 / 2 089 417 divisional application to the application mentioned under INID code 62. (71) Applicant: BHI Limited Partnership Laval, QC H7V 4A7 (CA) (54) Methods, compounds, compositions and vehicles for delivering 3- amino-1-propanesulfonic acid (57) The invention relates to methods, compounds, that will yield or generate 3APS, either in vitro or in vivo. -
Microscope Studies on the Morphogenesis of Plastids V
Bot. Mag. Tokyo 84: 123-136 (March 25, 1971) Electron Microscope Studies on the Morphogenesis of Plastids V. Concerning One-dimensional Metamorphosis of the Plastids in Cryptomeriac Leaves* by Susumu TOYAMA** and Kazuo FUNAZAKIS** Received November 25, 1970 Abstract To know about the mechanism of interconversion of plastids, electron micro- scopic observations were made on Cryptomeria leaves which aquire a reddish brown color in winter and recover their green color in coming spring to summer. In normal green leaves, two different kinds of plastids have been observed, viz, the chloroplasts having well organized grana structure in mesophyll cells and those completely lacking grana lamellae in bundle sheath cells. General feature of plastids in reddish brown leaves, may be summarized as follows : (1) The presence of red granules of rhodoxanthin (a carotenoid), and a well developed lamellar system involving grana- and intergrana-lamellae. (2) The plastoglobules, osmio- philic granules in plastids, increase in number and size as compared with the chloroplasts in normal green leaves. (3) Shrinkage which is one of the character- istic features of senescent plastids is not observed. (4) RNA content in plastid stroma is almost unchanged throughout an entire leaf stage ranging from normal green to subsequent regreening. Basic structure of the plastids in regreened leaves is quite similar to that in winter leaves, except for some increase of thylakoid membrane and decrease of osmiophilic granules. Accordingly, it is presumed that the plastids appearing in reddish brown leaves are not mere chro- moplasts but those having an incipient nature of the chloroplast, since real chromoplasts can not be converted into the chloroplasts. -
Malate- and Pyruvate-Dependent Fattyacid Synthesis In
Plant Physiol. (1992) 98, 1233-1238 Received for publication July 9, 1991 0032-0889/92/98/1 233/06/$01 .00/0 Accepted October 10, 1991 Malate- and Pyruvate-Dependent Fatty Acid Synthesis in Leucoplasts from Developing Castor Endosperm' Ronald G. Smith*2, David A. Gauthier, David T. Dennis3, and David H. Turpin Department of Botany, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4 ABSTRACT or leucoplast glycolytic enzymes are more than adequate to endosperm Leucoplasts were isolated from the endosperm of developing account for the triacylglycerol synthesis of castor castor (Ricinis communis) endosperm using a discontinuous Per- (17). However, glycolytic intermediates have not been well coil gradient. The rate of fatty acid synthesis was highest when characterized as carbon sources for fatty acid synthesis (18). malate was the precursor, at 155 nanomoles acetyl-CoA equiva- In this study, we present data regarding the kinetics and lents per milligram protein per hour. Pyruvate and acetate also exogenous cofactor requirements for fatty acid synthesis in were precursors of fatty acid synthesis, but the rates were ap- isolated leucoplast preparations using pyruvate, malate, and proximately 4.5 and 120 times less, respectively, than when acetate as carbon sources. We show that malate and pyruvate malate was the precursor. When acetate was supplied to leuco- support much higher rates of fatty acid synthesis than does plasts, exogenous ATP, NADH, and NADPH were required to acetate and the metabolism of both these substrates alleviates obtain maximal rates of fatty acid synthesis. In contrast, the any requirement for externally added reductant. Based on the incorporation of malate and pyruvate into fatty acids did not measurement of leucoplast-associated NADP+-malic enzyme require a supply of exogenous reductant. -
Program 1..154
The 97th Annual Meeting of CSJ Program Chair: INOUE, Haruo(15:30~15:55) Room S1 1S1- 15 Medium and Long-Term Program Lecture Artificial Photosynthesis of Ammonia(RIES, Hokkaido Univ.)○MISAWA, Hiroaki (15:30~15:55) Fourth Building, Section B J11 Chair: INOUE, Haruo(15:55~16:20) 1S1- 16 Medium and Long-Term Program Lecture Mechanism of water-splitting by photosystem II using the energy of visible light(Grad. Sustainable and Functional Redox Chemistry Sch. Nat. Sci. Technol., Okayama Univ.)○SHEN, Jian-ren(15:55~ ) Thursday, March 16, AM 16:20 (9:30 ~9:35 ) Chair: TAMIAKI, Hitoshi(16:20~16:45) 1S1- 01 Special Program Lecture Opening Remarks(Sch. Mater. & 1S1- 17 Medium and Long-Term Program Lecture Excited State Chem. Tech., Tokyo Tech.)○INAGI, Shinsuke(09:30~09:35) Molecular Dynamics of Natural and Artificial Photosynthesis(Sch. Sci. Tech., Kwansei Gakuin Univ.)○HASHIMOTO, Hideki(16:20~16:45) Chair: ATOBE, Mahito(9:35 ~10:50) 1S1- 02 Special Program Lecture Polymer Redox Chemistry toward Chair: ISHITANI, Osamu(16:45~17:10) Functional Materials(Sch. Mater. & Chem. Tech., Tokyo Tech.)○INAGI, 1S1- 18 Medium and Long-Term Program Lecture Recent pro- Shinsuke(09:35~09:50) gress on artificial photosynthesis system based on semiconductor photocata- 1S1- 03 Special Program Lecture Organic Redox Chemistry Enables lysts(Grad. Sch. Eng., Kyoto Univ.)○ABE, Ryu(16:45~17:10) Automated Solution-Phase Synthesis of Oligosaccharides(Grad. Sch. Eng., Tottori Univ.)○NOKAMI, Toshiki(09:50~10:10) (17:10~17:20) 1S1- 04 Special Program Lecture Redox Regulation of Functional 1S1- 19 Medium and Long-Term Program Lecture Closing re- Dyes and Their Applications to Optoelectronic Devices(Fac. -
Growth, Elastin Concentration, and Collagen Concentration of Perinatal Rat Lung: Effects of Dexamethasone
003 1-3998/87/2 106-0603$02.00/0 PEDIATRIC RESEARCH Vol. 21, No. 6, 1987 Copyright O 1987 International Pediatric Research Foundation, Inc Printed in U.S. A. Growth, Elastin Concentration, and Collagen Concentration of Perinatal Rat Lung: Effects of Dexamethasone JEAN-CLAUDE SCHELLENBERG, GRAHAM C. LIGGINS, AND ALISTAIR W. STEWART Postgraduate School of Obstetrics and Gynaecology [J-C.S., G.C.L.] and Department of Community Health [A. W.S.], The University of Auckland, Auckland, New Zealand ABSTRACT. The ontogenesis of elastin and collagen ac- phological (8) or biochemical structural analysis is required. cumulation and growth of the lung were studied in Wistar Although elastin and collagen have been used as markers of rats from day 18 of gestation until day 30 postnatally. connective tissue structure of the lung in newborn and adolescent Dexamethasone phosphate 0.1 mg or normal saline solu- rats (9-12), no data are available on the fetal rat lung. The tion every 8 h for three doses was injected into pregnant present study reports the ontogenesis of collagen and elastin rats on day 17. The effects of treatment, age, and sex on accumulation in rat lung between day 18 of gestation and day lung wet weight, lung dry weight, body weight, DNA, 30 postpartum and investigates the effects of prenatal glucocor- protein and desmosine (estimated by radioimmunoassay), ticoid administration on growth and structural development of and hydroxyproline were determined in the offspring. Dex- the rat lung. A radioimmunoassay for the determination of amethasone inhibited lung growth and, to a lesser extent, desmosine, a specific cross-link amino acid of elastin (13) is body weight gain. -
Stromule Biogenesis in Maize Chloroplasts 192 6.1 Introduction 192
Plastid Tubules in Higher Plants: An Analysis of Form and Function Mark T. Waters, BA (Oxon) A thesis submitted to the University of Nottingham for the degree of Doctor of Philosophy, September 2004 ABSTRACT Besides photosynthesis, plastids are responsible for starch storage, fatty acid biosynthe- sis and nitrate metabolism. Our understanding of plastids can be improved with obser- vation by microscopy, but this has been hampered by the invisibility of many plastid types. By targeting green fluorescent protein (GFP) to the plastid in transgenic plants, the visualisation of plastids has become routinely possible. Using GFP, motile, tubular protrusions can be observed to emanate from the plastid envelope into the surrounding cytoplasm. These structures, called stromules, vary considerably in frequency and length between different plastid types, but their function is poorly understood. During tomato fruit ripening, chloroplasts in the pericarp cells differentiate into chro- moplasts. As chlorophyll degrades and carotenoids accumulate, plastid and stromule morphology change dramatically. Stromules become significantly more abundant upon chromoplast differentiation, but only in one cell type where plastids are large and sparsely distributed within the cell. Ectopic chloroplast components inhibit stromule formation, whereas preventing chloroplast development leads to increased numbers of stromules. Together, these findings imply that stromule function is closely related to the differentiation status, and thus role, of the plastid in question. In tobacco seedlings, stromules in hypocotyl epidermal cells become longer as plastids become more widely distributed within the cell, implying a plastid density-dependent regulation of stromules. Co-expression of fluorescent proteins targeted to plastids, mi- tochondria and peroxisomes revealed a close spatio-temporal relationship between stromules and other organelles. -
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WO 2010/037397 Al
(12) INTERNATIONALAPPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date 8 April 2010 (08.04.2010) WO 2010/037397 Al (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every A61K 38/17 (2006.01) C07K 14/705 (2006.01) kind of national protection available): AE, AG, AL, AM, A61K 47/48 (2006.01) GOlN 33/50 (2006.01) AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, (21) International Application Number: DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, PCT/DK2009/050257 HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, (22) International Filing Date: KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, 1 October 2009 (01 .10.2009) ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, OM, PE, PG, PH, PL, PT, RO, RS, RU, SC, SD, (25) Filing Language: English SE, SG, SK, SL, SM, ST, SV, SY, TJ, TM, TN, TR, TT, (26) Publication Language: English TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (30) Priority Data: (84) Designated States (unless otherwise indicated, for every PA 2008 0 1381 1 October 2008 (01 .10.2008) DK kind of regional protection available): ARIPO (BW, GH, 61/101,898 1 October 2008 (01 .10.2008) US GM, KE, LS, MW, MZ, NA, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, MD, RU, TJ, (71) Applicant (for all designated States except US): DAKO TM), European (AT, BE, BG, CH, CY, CZ, DE, DK, EE, DENMARK A/S [DK/DK]; Produktionsvej 42, DK-2600 ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, Glostrup (DK). -
Liberation of Desmosine and Isodesmosine As Amino Acids from Insoluble Elastin by Elastolytic Proteases
Liberation of desmosine and isodesmosine as amino acids from insoluble elastin by elastolytic proteases The Harvard community has made this article openly available. Please share how this access benefits you. Your story matters Citation Umeda, Hideyuki, Masanori Aikawa, and Peter Libby. 2011. “Liberation of Desmosine and Isodesmosine as Amino Acids from Insoluble Elastin by Elastolytic Proteases.” Biochemical and Biophysical Research Communications 411, no. 2: 281–286. Published Version doi:10.1016/j.bbrc.2011.06.124 Citable link http://nrs.harvard.edu/urn-3:HUL.InstRepos:32605695 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 NIH Public Access Author Manuscript Biochem Biophys Res Commun. Author manuscript; available in PMC 2012 July 29. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: Biochem Biophys Res Commun. 2011 July 29; 411(2): 281±286. doi:10.1016/j.bbrc.2011.06.124. Liberation of Desmosine and Isodesmosine as Amino Acids from Insoluble Elastin by Elastolytic Proteases Hideyuki Umeda, Ph.D., Masanori Aikawa, M.D., Ph.D., and Peter Libby, M.D. Division of Cardiovascular Medicine, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, USA Abstract The development of atherosclerotic lesions and abdominal aortic aneurysms involves degradation and loss of extracellular matrix components, such as collagen and elastin. Releases of the elastin cross-links desmosine (DES) and isodesmosine (IDE) may reflect elastin degradation in cardiovascular diseases.