DOCSLIB.ORG

MITOCHONDRIAL CREATINE KINASE Some Clinical, Biochemical and Morphological Aspects

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
MITOCHONDRIAL CREATINE KINASE Some Clinical, Biochemical and Morphological Aspects PDF hosted at the Radboud Repository of the Radboud University Nijmegen The following full text is a publisher's version. For additional information about this publication click this link. http://hdl.handle.net/2066/114105 Please be advised that this information was generated on 2021-10-11 and may be subject to change. MITOCHONDRIAL CREATINE KINASE some clinical, biochemical and morphological aspects Jan A.M. Smeitink MITOCHONDRIAL CREATINE KINASE some clinical, biochemical and morphological aspects Jan A.M. Smeitink MITOCHONDRIAL CREATINE KINASE SOME CLINICAL, BIOCHEMICAL AND MORPHOLOGICAL ASPECTS EEN WETENSCHAPPELIJKE PROEVE OP HET GEBIED VAN DE MEDISCHE WETENSCHAPPEN, IN HET BIJZONDER DE GENEESKUNDE PROEFSCHRIFT TER VERKRIJGING VAN DE GRAAD VAN DOCTOR AAN DE KATHOLIEKE UNIVERSITEIT NIJMEGEN VOLGENS BESLUIT VAN HET COLLEGE VAN DECANEN IN HET OPENBAAR TE VERDEDIGEN OP DINSDAG 6 OKTOBER 1992, DES NAMIDDAGS TE 1.30 UUR PRECIES DOOR JOHANNES ALBERTUS MARIA SMEITINK GEBOREN OP 21 JUNI 1956 TE ARNHEM IV Promotores : Prof. Dr. R.C.A. Sengers Prof. Dr. J.M.F. Trijbels Co-Promotores : Dr. W. Ruitenbeek Dr. R.A. Wevers Aan mijn ouders AanWillemien en Mark CONTEN CHAPTER 1 Introduction and aim of the study CHAPTER 2 Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism Biochimica et Biophysica Acta (Reviews on Bioenergetics): in press I. Introduction II. Biochemical studies of Mi-CK ΠΙ. Functional studies of Mi-CK IV. Integration of Mi-CK in cellular energy metabolism V. Perspectives CHAPTER 3 A method for quantitative measurement of mitochondrial creatine kinase in human skeletal muscle Annals of Clinical Biochemistry Ì99229:196-201 CHAPTER 4 Maturation of mitochondrial and other isoenzymes of creatine kinase in skeletal muscle of preterm bom infants Annals of Clinical Biochemistry 199229:302-306 CHAPTER 5 Mitochondrial creatine kinase activity in patients with 123 a disturbed energy generation in muscle mitochondria Journal of Inherited Metabolic Disease: accepted CHAPTER 6 Mitochondrial creatine kinase containing crystals, 133 creatine content and mitochondrial creatine kinase activity in chronic progressive external ophthalmoplegia Neuromuscular Disorders: in press CHAPTER 7 Considerations and perspectives 143 Summary 150 Samenvatting 152 Woorden van dank 155 Curriculum vitae 159 List of publications 161 This study was performed at the Department of Pediatrics of the University of Nijmegen, The Netherlands. It is part of the research program "Disorders of the neuromuscular system". Publication of this thesis was financially supported by: Ethifarma, Milupa, Fonds Bevordering Wetenschapsbeoefening Afdeling Kindergeneeskunde (Academisch Ziekenhuis, Nijmegen) en Stichting ter bevordering van Onderwijs en Speurwerk ten behoeve van de Kindergeneeskunde (Wilhelmina Kinderziekenhuis, Utrecht). CIP-DATA KONINKLIJKE BIBLIOTHEEK, DEN HAAG Smeitink, Jan A.M. Mitochondrial creatine kinase : some clinical, biochemical and morphological aspects / Jan A.M. Smeitink. - [S.l. : s.n.] (Wijk bij Duurstede : Addix). - 111. Thesis Nijmegen. - With ref. - With summary in Dutch. ISBN 90-9005239-9 Subject headings: mitochondria/myopathy No part of this book may be reproduced in any form or by any means without permission from the author. Introduction and aim of the study Chapter 1 2 CHAPTER 1 Introduction 3 Introduction and aim of the study Mitochondrial creatine kinase (Mi-CK; EC 2.7.3.2) is localized at the outer surface of the inner mitochondrial membrane. The enzyme catalyzes the transfer of they-phosphate group of adenosine triphosphate (ATP) to creatine (Cr), thereby producing phosphocreatine (PCr) plus adenosine diphosphate (ADP). Mi-CK plays an essential role in the shuttling of high-energy phos­ phates produced by the intramitochondrially situated energy-generating system in organs with a high and fluctuating energy demand like skeletal muscle, heart and brain. A reduction in the activity of Mi-CK may cause severe problems with respect to energy-consuming processes. Saks and co-workers showed that inhibition of Mi-CK by a specific antibody resulted in a decreased total ATP production by mitoplasts [1 ]. The physiological role of the enzyme has hardly been investigated in human pathology. It may be assumed that a deficiency of Mi-CK leads to a high intra­ mitochondrial ATP/ADP ratio and a decreased amount of PCr (Figure 1). The ATP/ADP ratio has its influence on several metabolic steps. In the first place, the activity of the pyruvate dehydrogenase complex (PDHc) is inacti­ vated by a high ATP/ADP ratio mediated by a phosphorylation of the El subunit of PDHc [2]. Furthermore, in the presence of a physiological, intact coupling state of the oxidative phosphorylation, an increased ATP/ADP ratio causes inhibition of the electron flow through the respiratory chain. The resulting increase of the NADH/NAD+ ratio also produces a feedback inhibition of the PDHc, leading to accumulation of pyruvate and lactate. As a result of the increased intrami tochondrial NADH /N AD+ ratio the cy tosolic NADH/NAD+ ratio is shifted likewise through the action of the malate- aspartate shuttle. The final result is an increased lactate/pyruvate (L/P) ratio in body fluids. Both lactic acidosis and an increased L/P ratio is frequently found in body fluids of patients with mitochondrial myopathy. A mitochondrial myopathy can be defined as a muscle disease characterized by structurally or numerically abnormal mitochondria and / or abnormal functioning of mitochondria. Such a disease may be expected in patients with muscle weakness and exercise intolerance. In most of the laboratories involved in the diagnosis of mitochondrial disorders the follow­ ing biochemical measurements are performed in skeletal muscle biopsies of such patients: substrate oxidation rates, ATP production rates and activities of PDHc and respiratory chain complexes [e.g. 3]. However, despite these intensive studies, no specific enzyme deficiency could be detected in approximately 30% of the muscle samples with a disturbed pyruvate and 4 CHAPTER 1 malate oxidation rate. Therefore, extension of the diagnostic program includ­ ing determination of Mi-CK activity is warranted. The aim of this study was to develop a method to measure Mi-CK activity in human skeletal muscle and to study its applicability with respect to mitochondrial myopathies. Outline of the study In this study the results of investigations of Mi-CK activity in human skeletal muscle are described. A critical study of the literature concerning Mi-CK is presented in Chapter 2. The first objective of this study was to develop a method to determine Mi-CK activity in a small amount of human skeletal muscle and to collect reference values for Mi-CK activity. Method and reference values are presented in Chapter 3. From scarce literature data and the experience from oui group it appears that the activity of enzymes involved in the energy metabolism of muscle mitochondria inaeases with age during development and reaches adult levels approximately a few months post partum [4,5]. Knowledge about the existence of age-dependency is important to the interpretation of the biochemical studies performed in the very young age group with the suspicion of a mitochondrial disorder. Chapter 4 contains data concerning the development of Mi-CK and other CK isoenzymes in preterm born infants. Reference values for this specific age group are given. Sub­ sequently Mi-CK activity in patients with a disturbed pyruvate and malate oxidation rate, in which no specific defect of the pyruvate dehydrogenase complex and the respiratory chain could be established, was studied. Results of this investigation are presented in Chapter 5. A striking structural ab­ normality regularly observed in the intermembrane space of mitochondria of patients suffering from mitochondrial myopathies is the occurrence of crystals. Recently it was shown that these crystals contain Mi-CK protein [6,7]. We studied the relationship between Mi-CK containing crystals and the muscle aeatine content. This is presented in Chapter 6. Finally, considera­ tions about the work performed in this study and recommendations for future investigation are given in Chapter 7. Introduction 5 Glucose . LDH \ Cr^/^ PCr | Lactate f -^ *- Pyruvate · j j Cytosol Fig. 1. Hypothetical biochemical consequences of a Mi-CK deficiency. LDH = Lactate dehydrogenase; PDHc = Pyruvate dehydrogenase complex; OM = Outer mitochondrial membrane; IM = Inner mitochondrial membrane. = porm = adenine nucleotide translocator = pyruvate translocator = long chain fatty acids are, in contrast to medium and short chain fatty acids, transported via a carnitine dependent transport system = respiratory chain •• F^-ATPase 6 CHAPTER 1 References 4. Smeitink JAM, Sengers RCA, Trijbele JMF, et al. Fatal neonatal cardiomyopathy 1. Kuznetsov AV, Khuchua ZA, Saks VA. associated with cataract and mitochondrial Mitochondrial synthesis of phosphocrcatine myopathy. Eur J Pediatr 1989;148:656-659 . under physiological conditions. In: Creatine 5. Speri W, Sengers RCA, Trijbels JMF, et al. phosphate. Biochemistry.pharmacologyand Enzymeactivitiesofthemitochondrial energy clinical efficiency (Saks VA, Bobkov YG, generating system in skeletal muscle tissue Strumia E, eds) 1987:15-30, Edizioni Minerva of preterm and full term neonates. Ann Clin Medica, Torino. Biochem: in press. 2. Wieland OH. The mammalian pyruvate 6. Stadhouders A, Jap P, Wallimann T. dehydrogenase complex: structure and Biochemical nature of mitochondrial crystals. regulation.
Load more

Recommended publications
  • Lombricine Kinase Structure and Substrate Specificity: a Paradigm for Elucidation of Substrate Specificity in Phosphagen Kinases D
    Florida State University Libraries Electronic Theses, Treatises and Dissertations The Graduate School 2007 Lombricine Kinase Structure and Substrate Specificity: A Paradigm for Elucidation of Substrate Specificity in Phosphagen Kinases D. Jeffrey. Bush Follow this and additional works at the FSU Digital Library. For more information, please contact [email protected] THE FLORIDA STATE UNIVERSITY COLLEGE OF ARTS AND SCIENCES LOMBRICINE KINASE STRUCTURE AND SUBSTRATE SPECIFICITY: A PARADIGM FOR ELUCIDATION OF SUBSTRATE SPECIFICITY IN PHOSPHAGEN KINASES By D. JEFFREY BUSH A Dissertation submitted to the Department of Chemistry and Biochemistry in partial fulfillment of the requirements for the degree of Doctor of Philosophy Degree Awarded: Spring Semester, 2007 The members of the Committee approve the Dissertation of D. Jeffrey Bush defended on February 20, 2007. Michael S. Chapman Professor Co-Directing Dissertation John Dorsey Professor Co-Directing Dissertation W. Ross Ellington Outside Committee Member Michael Blaber Committee Member Approved: ____________________________________________ Joseph Schlenoff, Department Chair, Department of Chemistry & Biochemistry ____________________________________________ Joseph Travis, Dean, College of Arts & Sciences The Office of Graduate Studies has verified and approved the above named committee members. ii To the late Clifford M. Bush, who with statements such as “A heterogeneous compound of two or more substances whose ray through certain limits is confined to a specific area…” fostered a strong interest of the author in science at a very young age, if only just to know more about what he spoke. iii ACKNOWLEDGEMENTS I wish to first convey my sincere gratitude to my parents, Donald and Roberta for raising me in the nurture and admonition of the Almighty God.
    [Show full text]
  • Acidophilic Green Algal Genome Provides Insights Into Adaptation to an Acidic Environment
    Acidophilic green algal genome provides insights into adaptation to an acidic environment Shunsuke Hirookaa,b,1, Yuu Hirosec, Yu Kanesakib,d, Sumio Higuchie, Takayuki Fujiwaraa,b,f, Ryo Onumaa, Atsuko Eraa,b, Ryudo Ohbayashia, Akihiro Uzukaa,f, Hisayoshi Nozakig, Hirofumi Yoshikawab,h, and Shin-ya Miyagishimaa,b,f,1 aDepartment of Cell Genetics, National Institute of Genetics, Shizuoka 411-8540, Japan; bCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan; cDepartment of Environmental and Life Sciences, Toyohashi University of Technology, Aichi 441-8580, Japan; dNODAI Genome Research Center, Tokyo University of Agriculture, Tokyo 156-8502, Japan; eResearch Group for Aquatic Plants Restoration in Lake Nojiri, Nojiriko Museum, Nagano 389-1303, Japan; fDepartment of Genetics, Graduate University for Advanced Studies, Shizuoka 411-8540, Japan; gDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan; and hDepartment of Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan Edited by Krishna K. Niyogi, Howard Hughes Medical Institute, University of California, Berkeley, CA, and approved August 16, 2017 (received for review April 28, 2017) Some microalgae are adapted to extremely acidic environments in pumps that biotransform arsenic and archaeal ATPases, which which toxic metals are present at high levels. However, little is known probably contribute to the algal heat tolerance (8). In addition, the about how acidophilic algae evolved from their respective neutrophilic reduction in the number of genes encoding voltage-gated ion ancestors by adapting to particular acidic environments. To gain channels and the expansion of chloride channel and chloride car- insights into this issue, we determined the draft genome sequence rier/channel families in the genome has probably contributed to the of the acidophilic green alga Chlamydomonas eustigma and per- algal acid tolerance (8).
    [Show full text]
  • Natural Products Containing 'Rare'
    molecules Review Natural Products Containing ‘Rare’ Organophosphorus Functional Groups Janusz J. Petkowski 1,* , William Bains 2 and Sara Seager 1,3,4 1 Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA; [email protected] 2 Rufus Scientific, 37 The Moor, Melbourn, Royston, Herts SG8 6ED, UK; [email protected] 3 Department of Physics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA 4 Department of Aeronautics and Astronautics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA * Correspondence: [email protected] Received: 21 January 2019; Accepted: 22 February 2019; Published: 28 February 2019 Abstract: Phosphorous-containing molecules are essential constituents of all living cells. While the phosphate functional group is very common in small molecule natural products, nucleic acids, and as chemical modification in protein and peptides, phosphorous can form P–N (phosphoramidate), P–S (phosphorothioate), and P–C (e.g., phosphonate and phosphinate) linkages. While rare, these moieties play critical roles in many processes and in all forms of life. In this review we thoroughly categorize P–N, P–S, and P–C natural organophosphorus compounds. Information on biological source, biological activity, and biosynthesis is included, if known. This review also summarizes the role of phosphorylation on unusual amino acids in proteins (N- and S-phosphorylation) and reviews the natural phosphorothioate (P–S) and phosphoramidate (P–N) modifications of DNA and nucleotides with an emphasis on their role in the metabolism of the cell. We challenge the commonly held notion that nonphosphate organophosphorus functional groups are an oddity of biochemistry, with no central role in the metabolism of the cell.
    [Show full text]
  • Natural Products Containing 'Rare'
    Natural Products Containing ‘Rare’ Organophosphorus Functional Groups The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Petkowski, Janusz, et al. “Natural Products Containing ‘Rare’ Organophosphorus Functional Groups.” Molecules, vol. 24, no. 5, Feb. 2019, p. 866. As Published http://dx.doi.org/10.3390/molecules24050866 Publisher Multidisciplinary Digital Publishing Institute Version Final published version Citable link http://hdl.handle.net/1721.1/120918 Terms of Use Creative Commons Attribution Detailed Terms https://creativecommons.org/licenses/by/4.0/ molecules Review Natural Products Containing ‘Rare’ Organophosphorus Functional Groups Janusz J. Petkowski 1,* , William Bains 2 and Sara Seager 1,3,4 1 Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA; [email protected] 2 Rufus Scientific, 37 The Moor, Melbourn, Royston, Herts SG8 6ED, UK; [email protected] 3 Department of Physics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA 4 Department of Aeronautics and Astronautics, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA * Correspondence: [email protected] Received: 21 January 2019; Accepted: 22 February 2019; Published: 28 February 2019 Abstract: Phosphorous-containing molecules are essential constituents of all living cells. While the phosphate functional group is very common in small molecule natural products, nucleic acids, and as chemical modification in protein and peptides, phosphorous can form P–N (phosphoramidate), P–S (phosphorothioate), and P–C (e.g., phosphonate and phosphinate) linkages. While rare, these moieties play critical roles in many processes and in all forms of life.
    [Show full text]
  • Acidophilic Green Algal Genome Provides Insights Into Adaptation To
    Acidophilic green algal genome provides insights into PNAS PLUS adaptation to an acidic environment Shunsuke Hirookaa,b,1, Yuu Hirosec, Yu Kanesakib,d, Sumio Higuchie, Takayuki Fujiwaraa,b,f, Ryo Onumaa, Atsuko Eraa,b, Ryudo Ohbayashia, Akihiro Uzukaa,f, Hisayoshi Nozakig, Hirofumi Yoshikawab,h, and Shin-ya Miyagishimaa,b,f,1 aDepartment of Cell Genetics, National Institute of Genetics, Shizuoka 411-8540, Japan; bCore Research for Evolutional Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan; cDepartment of Environmental and Life Sciences, Toyohashi University of Technology, Aichi 441-8580, Japan; dNODAI Genome Research Center, Tokyo University of Agriculture, Tokyo 156-8502, Japan; eResearch Group for Aquatic Plants Restoration in Lake Nojiri, Nojiriko Museum, Nagano 389-1303, Japan; fDepartment of Genetics, Graduate University for Advanced Studies, Shizuoka 411-8540, Japan; gDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan; and hDepartment of Bioscience, Tokyo University of Agriculture, Tokyo 156-8502, Japan Edited by Krishna K. Niyogi, Howard Hughes Medical Institute, University of California, Berkeley, CA, and approved August 16, 2017 (received for review April 28, 2017) Some microalgae are adapted to extremely acidic environments in pumps that biotransform arsenic and archaeal ATPases, which which toxic metals are present at high levels. However, little is known probably contribute to the algal heat tolerance (8). In addition, the about how acidophilic algae evolved from their respective neutrophilic reduction in the number of genes encoding voltage-gated ion ancestors by adapting to particular acidic environments. To gain channels and the expansion of chloride channel and chloride car- insights into this issue, we determined the draft genome sequence rier/channel families in the genome has probably contributed to the of the acidophilic green alga Chlamydomonas eustigma and per- algal acid tolerance (8).
    [Show full text]
  • Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles
    Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur Quetglas, Sarah Zorman, Martin Pelosse, Pierre dos Santos, Francois Boucher, Tuuli Käämbre, et al. To cite this version: Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur Quet- glas, et al.. Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling. Systems Biology of Metabolic and Sig- naling Networks, Springer, pp.261-320, 2014, 9783642385056. 10.1007/978-3-642-38505-6_11. hal- 01949810 HAL Id: hal-01949810 https://hal.univ-grenoble-alpes.fr/hal-01949810 Submitted on 26 Jun 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Chapter 11 Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur, Sarah Zorman, Martin Pelosse, Pierre Dos Santos, Franc¸ois Boucher, Tuuli Kaambre, and Rita Guzun V. Saks (*) Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia e-mail: [email protected] U.
    [Show full text]
  • 12) United States Patent (10
    US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.
    [Show full text]
  • POLSKIE TOWARZYSTWO BIOCHEMICZNE Postępy Biochemii
    POLSKIE TOWARZYSTWO BIOCHEMICZNE Postępy Biochemii http://rcin.org.pl WSKAZÓWKI DLA AUTORÓW Kwartalnik „Postępy Biochemii” publikuje artykuły monograficzne omawiające wąskie tematy, oraz artykuły przeglądowe referujące szersze zagadnienia z biochemii i nauk pokrewnych. Artykuły pierwszego typu winny w sposób syntetyczny omawiać wybrany temat na podstawie możliwie pełnego piśmiennictwa z kilku ostatnich lat, a artykuły drugiego typu na podstawie piśmiennictwa z ostatnich dwu lat. Objętość takich artykułów nie powinna przekraczać 25 stron maszynopisu (nie licząc ilustracji i piśmiennictwa). Kwartalnik publikuje także artykuły typu minireviews, do 10 stron maszynopisu, z dziedziny zainteresowań autora, opracowane na podstawie najnow­ szego piśmiennictwa, wystarczającego dla zilustrowania problemu. Ponadto kwartalnik publikuje krótkie noty, do 5 stron maszynopisu, informujące o nowych, interesujących osiągnięciach biochemii i nauk pokrewnych, oraz noty przybliżające historię badań w zakresie różnych dziedzin biochemii. Przekazanie artykułu do Redakcji jest równoznaczne z oświadczeniem, że nadesłana praca nie była i nie będzie publikowana w innym czasopiśmie, jeżeli zostanie ogłoszona w „Postępach Biochemii”. Autorzy artykułu odpowiadają za prawidłowość i ścisłość podanych informacji. Autorów obowiązuje korekta autorska. Koszty zmian tekstu w korekcie (poza poprawieniem błędów drukarskich) ponoszą autorzy. Artykuły honoruje się według obowiązujących stawek. Autorzy otrzymują bezpłatnie 25 odbitek swego artykułu; zamówienia na dodatkowe odbitki (płatne) należy zgłosić pisemnie odsyłając pracę po korekcie autorskiej. Redakcja prosi autorów o przestrzeganie następujących wskazówek: Forma maszynopisu: maszynopis pracy i wszelkie załączniki należy nadsyłać w dwu egzem­ plarzach. Maszynopis powinien być napisany jednostronnie, z podwójną interlinią, z marginesem ok. 4 cm po lewej i ok. 1 cm po prawej stronie; nie może zawierać więcej niż 60 znaków w jednym wierszu nie więcej niż 30 wierszy na stronie zgodnie z Normą Polską.
    [Show full text]
  • The Relevance of Transhydrogenases and Heterologous Phosphagen Kinases for Microbial Cofactor Metabolism
    Research Collection Doctoral Thesis The relevance of transhydrogenases and heterologous phosphagen kinases for microbial cofactor metabolism Author(s): Canonaco, Fabrizio Publication Date: 2003 Permanent Link: https://doi.org/10.3929/ethz-a-004525971 Rights / License: In Copyright - Non-Commercial Use Permitted This page was generated automatically upon download from the ETH Zurich Research Collection. For more information please consult the Terms of use. ETH Library DISS. ETH.Nr. 15040 The relevance of transhydrogenases and heterologous phosphagen kinases for microbial cofactor metabolism A dissertation submitted to the SWISS FEDERAL INSTITUTE OF TECHNOLOGY ZURICH for the degree of Doctor of Natural Science Presented by Fabrizio Canonaco Dipl. Natw. ETH born April 22nd, 1975 in Locarno, Switzerland Accepted on the recommendation of PD Dr. U. Sauer Prof. T. Wallimann PD Dr. U. Schlattner Prof. H. Hennecke 2003 Seite Leer Blank 2 ACKNOWLEDGEMENTS and further back to the When I think back to the time point where I began my PhD, in a how one recalls as have being important years of the study, it is surprising many people I owe a it is not to name them all, but to some people way or another. In this section, possible PhD. tribute, because without them I would not have succeeded in finishing my and it could not have been else. They The first big 'thank you' goes to my family, to without me in I did not want do, always played a central role in my life, pushing anything their sacrifices and their encouragements I but supporting me in everything I chose. Without would not have been writing these pages.
    [Show full text]
  • 1787 Genome-Wide Identification and Characterization of Eukaryotic Protein Kinases Kanhu Charan Das1, Parismita Kalita1, Timir
    [Frontiers in Bioscience, Landmark, 25, 1787-1827, June 1, 2020] Genome-wide identification and characterization of eukaryotic protein kinases Kanhu Charan Das1, Parismita Kalita1, Timir Tripathi1 1Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India TABLE OF CONTENTS 1. Abstract 2. Introduction 3. Methods 3.1. F. gigantica gene sequence retrieval 3.2. Generation of hidden markov models (HMMs) 3.3. Classification and domain analysis of FgePKs 4. Results 4.1. Identification of kinase-like proteins in F. gigantica genome 4.2. Classification and domain analysis of FgePKs 4.2.1. Ser/Thr kinase group 4.2.1.1. cAMP-dependent protein kinase (AGC) group 4.2.1.1.1. Protein kinase C (PKC) 4.2.1.1.2. Protein kinase A (PKA) 4.2.1.2. Calmodulin kinase (CaMK) group 4.2.1.3. Cyclin-dependent kinase and other close relatives (CMGC) group 4.2.1.3.1. Cyclin dependent kinases (CDK) 4.2.1.3.2. Mitogen activated protein kinases (MAPK) 4.2.1.3.3. Glycogen synthase 3 kinases (GSK3) 4.2.1.3.4. Dual-specificity Tyr regulated kinases (DYRK) 4.2.1.4. Sterile Ser/Thr kinase (STE) group 4.2.1.5. Casein kinase 1 (CK1) group 4.2.2. Tyr kinase group 4.3.3. Hybrid group 4.3.3.1. Tyr kinase-like (TKL) group 4.3.3.2. Others 5. Discussion 6. Acknowledgments 7. References 1. ABSTRACT The tropical liver fluke, Fasciola gigantica is kinases (ePKs) are regulators of cellular a food-borne parasite responsible for the phosphorylation.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling
    Chapter 11 Systems Level Regulation of Cardiac Energy Fluxes Via Metabolic Cycles: Role of Creatine, Phosphotransfer Pathways, and AMPK Signaling Valdur Saks, Uwe Schlattner, Malgorzata Tokarska-Schlattner, Theo Wallimann, Rafaela Bagur, Sarah Zorman, Martin Pelosse, Pierre Dos Santos, Franc¸ois Boucher, Tuuli Kaambre, and Rita Guzun V. Saks (*) Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France Laboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Tallinn, Estonia e-mail: [email protected] U. Schlattner (*) • M. Tokarska-Schlattner • S. Zorman • M. Pelosse Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France e-mail: [email protected] T. Wallimann ETH Zu¨rich, Zu¨rich, Switzerland R. Bagur Laboratory of Fundamental and Applied Bioenergetics, Univ. Grenoble Alpes, Grenoble, France INSERM, U1055 Grenoble, France TIMC-IMAG, Univ. Grenoble Alpes, Grenoble, France CNRS, UMR5525, Grenoble, France P.D. Santos Univ. Bordeaux, Bordeaux, France Centre de Recherche Cardiothoracique de Bordeaux, Inserm, U1045, Bordeaux, France LIRYC, L’Institut de rythmologie et mode´lisation cardiaque, Universite´ de Bordeaux, Bordeaux, France F. Boucher TIMC-IMAG, Univ. Grenoble Alpes, Grenoble, France CNRS, UMR5525, Grenoble, France M.A. Aon et al. (eds.), Systems Biology of Metabolic and Signaling Networks, 261 Springer Series in Biophysics 16, DOI 10.1007/978-3-642-38505-6_11,
    [Show full text]