Handbook of Glycosyltransferases and Related Genes PDF
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SSpprriinnggeerr Japan KK Tokyo Berlin Heidelberg New York Hong Kong London Milan Paris Handbook of Glycosyltransferases and Related Genes Edited by: Naoyuki Taniguchi, Koichi Honke, Minoru Fukuda Co-editors: Henrik Clausen James W. Dennis Kiyoshi Furukawa Koichi Furukawa Gerald W. Hart Yoshio Hirabayashi Reiji Kannagi Masao Kawakita Toshisuke Kawasaki Koji Kimata Taroh Kinoshita Ulf Lindahl Takashi Muramatsu Hisashi N arimatsu Masaki Saito Harry Schachter Joel H. Shaper Pamela Stanley KazuyukiSugahara Akemi Suzuki Lawrence A. Tabak Shuichi Tsuji Dirk H. Van den Eijnden Katsuko Yamashita Masaki Yanagishita With 95 Figures, Including 5 in Color Springer NAOYUKI TANIGUCHI, M.D., Ph.D. NPrAoOfeYsUsKorI, TDAeNpIaGrUtmCeHnI,t Mof.D B.,i oPchh.Dem. istry POrsoafkeass Uorn, iDveerpsaitryt mMeendti coafl BSicohcohoelm istry 2O-s2a Ykaa mUandivaoerksai,t yS uMitead, iOcasla kSac h5o6o5l- 0871, Japan 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan KOICHI HONKE, M.D., Ph.D. KAasrsCocHiIa tHe OPNroKfEe,s sMor.D, D., ePpha.Drt.m ent of Biochemistry AOsssaokcai aUten iPvreorfseistyso Mr, eDdiecpaal rStmcheonotl o f Biochemistry O2-s2a Ykaa mUandivaeorksai,t yS uMitead, iOcasla kSac h5o6o5l- 0871, Japan 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan MINORU FUKUDA, Ph.D. MPrIoNfOesRsUo rF, UGKlyUcDoAbi, oPlho.gDy. Program PCraonfceessro Rr,e Gselayrccohb iIonlsotgityu tPer ogram CThane cBeru rRnehsaemar cIhn sItnitsutitteu te T10h9e0 1B uNronrhtahm T oInrrsetiyt uPtien es Road, La Jolla, CA 92037, USA 10901 North Torrey Pines Road, La Jolla, CA 92037, USA Cover Illustration by Koichi Honke Cover Illustration by Koichi Honke ISBN 978-4-431-67996-7 ISBN 4-431-70311-X Springer-Verlag Tokyo Berlin Heidelberg New York Library of Congress Cataloging-in-Publication Data HLiabnrdarbyo oofk Coof ngglyrecsoss yCltartaanlosfgeirnags-eisn -aPnudb lrieclaattieodn gDenaetas / N. Taniguchi, K. Honke, M. Fukuda, eds. Handbopo.k;c omf .g lycosyltransferases and related genes / N. Taniguchi, K. Honke, M. Fukuda, eds. Incpl.u;dcems .b ibliographical references. IInScBluNd e9s7 8b-ib4l-i4o3g1r-a6p7h9ic9a6l- 7re ferencIeSs.B N 978-4-431-67877-9 (eBook) IDSOBNI 1404.311070073/1917X8 -(4h-a4r3d1c-o6v7e8r7: 7a-l9k . paper) 11.. 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PPrroodduucctt lliiaabbiilliittyy:: TThhee ppuubblliisshheerr ccaann ggiivvee nnoo gguuaarraanntteeee ffoorr iinnffoorrmmaatti ioonn aabboouutt ddrruugg ddoossaaggee aanndd aappppllii ccaattiioonn tthheerreeooff ccoonnttaaiinneedd iinn tthhiiss bbooookk.. IInn eevveerryy iinnddiivviidduuaall ccaassee tthhee rreessppeeccttiivvee uusseerr mmuusstt cchheecckk iittss aaccccuu rraaccyy bbyy ccoonnssuullttiinngg ootthheerr pphhaarrmmaacceeuuttiiccaall lliitteerraattuurree.. TTyyppeesseettttiinngg:: BBeesstt --sseett TTyyppeesseetttteerr LLttdd..,, HHoonngg KKoonngg Printing and binding: Hicom, Japan SSPPIINN:: 1lO0775577445555 Preface The so-called postgenomic research era has now been launched, and the field of gly cobiology and glycotechnology has become one of the most important areas in life science because glycosylation is the most common post-translational modification reaction of proteins in vivo. On the basis of Swiss-Prot data, over 50% proteins are known to undergo glycosylation, but in fact the actual functions of most of the sugar chains in the glycoconjugates remain unknown. The complex carbohydrate chains of glycoproteins, glycolipids, and proteoglycans represent the secondary gene products formed through the reactions of glycosyl transferases. The regulation of the biosynthesis of sugar chains is under the control of the expression of glycosyltransferases, their substrate specificity, and their local ization in specific tissue sites. There is a growing body of evidence to suggest that these enzymes play pivotal roles in a variety of important cellular differentiation and developmental events, as well as in disease processes. Over 300 glycosyltransferases appear to exist in mammalian tissues. If the genes that have been purified and cloned from various species such as humans, cattle, pigs, rats and mice are counted as one, approximately 110 glycogenes that encode glycosyltransferases and related genes have been cloned at present, and this number continues to grow each day. However, most of the functions of the glycosyltransferase genes and related genes are unknown. This fact has stimulated numerous new and interesting approaches in molecular biologi cal investigations. The removal of a specific glycogene in knockout mice indicates that some of the glycosyltransferases are essential for survival, development, and oncogenesis. Exper iments using cells or animals that had been transfected with a specific glycosyltrans ferase gene show that these enzymes relate to cancer metastases, cellular invasion, and the suppression of xenoantigen expression. Although a number of excellent investi gations have been conducted, the issue of the real functions of glycoconjugates of interest remains to be elucidated. The reason for the difficulty in exploring the func tional significance of glycosyltransferase genes, or glycogenes, is that even if we are able to disrupt the gene and obtain phenotypic changes in mice, we cannot explain this as a consequence or a cause of disease. Moreover, and more importantly, we cannot identify the actual target protein(s) in vivo that may be affected by the lack of sugar chains. The phenotypic changes observed are actually not due to a disrupted glycogene but, rather, to the secondary effect of the glycogene which may affect the v VI Preface aberrant glycosylation of other glycoproteins. The same would be true for transgenic mice that overexpress specified glycogenes or for Congenital Disorders of Glycosyla tion (CGD) patients with various symptoms that cannot be explained via the mecha nism by which the symptoms appeared. In the future, therefore, the identification of target proteins in patients or in glycogene-disrupted animals is a prerequisite for understanding the real cause of the pathophysiology of diseases. The field of func tional glycomics focuses on carrying out this type of research. This handbook is useful for experimental design for this approach, which may identify the target molecules of such glycosyltransferases and related genes. The aim of this book is to provide comprehensive coverage of all glycosyltrans ferase genes and their related genes known at present. The nearly 100 chapters are designed to summarize the present knowledge of these enzymes. The presentations are brief and concise and are presented in a format that we hope will make compre hension of the data relatively easy for readers. More than fifty experts who have worked on their "pet" enzymes that were largely purified and/or cloned by their group have contributed chapters on individual glyco syltransferase genes and their related genes. We express our sincere thanks to all of them for their enormous effort and detailed work. We are particularly grateful for the assistance of the staff at Springer-Verlag Tokyo for their patience during the prepa ration of the original draft of this book and its editing. This publication was supported in part by the Naito Foundation, a Grant-in-Aid for Publication of Scientific Research Results No. 135313 from the Japan Society for the Promotion of Science, and a Grant-in-Aid for Scientific Research on Priority Area No. 10178105 from the Ministry of Education, Science, Sports and Culture of Japan. July 2001 Naoyuki Taniguchi Koichi Honke Minoru Fukuda EDITORS Co-editors Henrik Clausen (University of Copenhagen, Copenhagen, Denmark) James W. Dennis (Mount Sinai Hospital, Toronto, Canada) Kiyoshi Furukawa (Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan) Koichi Furukawa (Nagoya University, Nagoya, Japan) Gerald W. Hart (Johns Hopkins University, Baltimore, USA) Yoshio Hirabayashi (Riken, Wako, Japan) Reiji Kannagi (Aichi Cancer Center, Nagoya, Japan) Masao Kawakita (Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan) Toshisuke Kawasaki (Kyoto University, Kyoto, Japan) Koji Kimata (Aichi Medical University, Nagoya, Japan) Taroh Kinoshita (Osaka University, Osaka, Japan) Ulf Lindahl (Uppsala University, Uppsala, Sweden) Takashi Muramatsu (Nagoya University, Nagoya, Japan) Hisashi Narimatsu (National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan) Masaki Saito (National Cancer Center Research Institute, Tokyo, Japan) Harry Schachter (The Hospital for Sick Children, Toronto, Canada) Joel H. Shaper (Johns Hopkins University, Baltimore, USA) Pamela Stanley (Albert Einstein College of Medicine, New York, USA) Kazuyuki Sugahara (Kobe Pharmaceutical University, Kobe, Japan) Akemi Suzuki (Riken, Wako, Japan) Lawrence A. Tabak (University of Rochester, Rochester, USA) Shuichi Tsuji (Ochanomizu University, Tokyo, Japan) Dirk H. Van den Eijnden (Vrije Universiteit, Amsterdam, The Netherlands) Katsuko Yamashita (Sasaki Institute, Tokyo, Japan) Masaki Yanagishita (Tokyo Medical and Dental University, Tokyo, Japan) VII Contents Preface ......................................................... V Contributors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. XVII Glucosyltransferase 1. GlcCer Synthase (UDP-Glucose:Ceramide Glucosyltransferase, UGCG) 3 Y. HIRABAYASHI and S. ICHIKAWA Galactosyltransferases 2. ~4-Galactosyltransferase-I ...................................... 11 N.L. SHAPER and I.H. SHAPER 3. ~4-Galactosyltransferase-II, -III, -IV, -v, -VI, and -VII. . . . . . . . . . . .. . . . . 20 KIYOSHI FURUKAWA and H. CLAUSEN 4. 133-Galactosyltransferase-I, -II, and -III ............................ 27 T. HENNET and E.G. BERGER 5. ~3-Galactosyltransferase-IV (GMI Synthase) 33 KorCHI FURUKAWA 6. 133-Galactosyltransferase-V . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 37 H. NARIMATSU 7. a3-Galactosyltransferase........................................ 44 D.H. VAN DEN EIJNDEN and D.H. IOZIASSE 8. GalCer Synthase (Ceramide Galactosyltransferase, CGT) 51 w. STOFFEL N-Acetylg Iu cosa m in yltra n sferases 9. N-Acetylglucosaminyltransferase-I . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 61 P. STANLEY IX X Contents 10. N-Acetylglucosaminyltransferase-II 70 H. SCHACHTER 11. N-Acetylglucosaminyltransferase-III .............................. 80 Y. IKEDA and N. TANIGUCHI 12. N-Acetylglucosaminyltransferase-IV .............................. 87 M.T. MINOWA, S. OGURI, A. YOSHIDA, and M. TAKEUCHI 13. N-Acetylglucosaminyltransferase-V ........... . . . . . . . . . . . . . . . . . . . . 94 J.w. DENNIS 14. N-Acetylglucosaminyltransferase-VI .............................. 102 K. HONKE and N. TANIGUCHI 15. ~3-N-Acetylglucosaminyltransferase (Fringe) 107 R.S. HALTIWANGER 16. ~3-N-Acetylglucosaminyltransferase (iGnT) 114 M. FUKUDA 17. ~6-N -Acetylglucosaminyltransferase (I GnT ) 125 M. FUKUDA 18. Core 2 ~6-N-Acetylglucosaminyltransferase-I and -III ................ 133 M. FUKUDA, T. SCHWIENTEK, and H. CLAUSEN 19. Core 2 ~6-N-Acetylglucosaminyltransferase-II 143 M. FUKUDA and J.-c. YEH 20. a4-N-Acetylglucosaminyltransferase .............................. 151 J. NAKAYAMA 21. O-GlcNAc Transferase. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 158 S.P.N. IYER and G.W. HART N-Acetylgalactosaminyltransferases 22. Polypeptide N-Acetylgalactosaminyltransferases . . . . . . . . . . . . . . . . . . . .. 167 F.K. HAGEN, K.G. TEN HAGEN, and L.A. TABAK 23. ~4-N-Acetylgalactosaminyltransferase . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 174 KorCHI FURUKAWA 24. Histoblood Group A and B Transferases, Their Gene Structures, and Common 0 Group Gene Structures ........................... 180 S. HAKOMORI 25. Histoblood Group A Variants, 0 Variants, and Their Alleles 189 S. HAKOMORI 26. Forssman Glycolipid Synthase 197 K. HONKE Contents XI Fucosyltra nsferases 27. a2-Fucosyltransferases (FUn, FUT2, and Secl) 205 R. ORIOL and R. MOLLICONE 28. a3/4-Fucosyltransferase (FUT3, Lewis enzyme) 218 H. NARIMATSU 29. a3-Fucosyltransferase-IV (FUT4) . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 226 H. NARIMATSU 30. a3-Fucosyltransferase-V (FUT5) 232 R. KANNAGI 31. a3-Fucosyltransferase-VI (FUT6) . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 237 R. KANNAGI 32. a3-Fucosyltransferase-VII (FUT7) 246 H. NARIMATSU 33. a3-Fucosyltransferase-IX (FUT9) . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 252 H. NARIMATSU 34. a6-Fucosyltransferase (FUT8) ................................... 259 E. MIYOSHI and N. TANIGUCHI Sialyltransferases 35. ST3Gal-I 267 M. FUKUDA and J.D. MARTH 36. ST3Gal-II (SAT-IV) ............................................ 274 T. HAMAMOTO and S. TsuJI 37. ST3Gal-III 279 S. KITAZUME-KAWAGUCHI and S. TsuJI 38. ST3Gal-IV 284 S. KITAZUME-KAWAGUCHI and S. TSUJI 39. ST3Gal-V (GM3 Synthase, SAT-I) ................................. 289 M. SAITO and A. ISHII 40. ST6Gal-I 295 T. HAMAMOTO and S. TsuJI 41. ST6GalNAc-I ................................................. 301 N. KUROSAWA and S. TSUJI 42. ST6GalNAc-II ................................................ 306 N. KUROSAWA and S. TSUJI 43. ST6GalNAc-III (STY) .......................................... 311 S. TAKASHIMA and S. TsuJI XII Contents 44. ST6GalNAc-IV . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 317 S. TAKASHIMA and S. TSUJI 45. ST8Sia-I (GD3 Synthase, SAT-II) . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 323 Y. SANAI 46. ST8Sia-II (STX) . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 329 N. KOJIMA and S. TsuJI 47. ST8Sia-III 335 Y. YOSHIDA and S. TSUJI 48. ST8Sia-IV (PST-I) . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 340 J. NAKAYAMA, K. ANGATA, M. SUZUKI, and M. FUKUDA 49. ST8Sia-V (SAT-V/SAT-III) . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 347 M. KaNa and S. TsuJI 50. CMP-NeuAc Hydroxylase 352 A. SUZUKI Glucuronyltransferases 51. HNK-l Glucuronyltransferase ................................... 359 S. OKA and T. KAWASAKI 52. GAG Glucuronyltransferase-I .................................... 368 H. KITAGAWA and K. SUGAHARA 53. UDP-Glucose Dehydrogenase 375 A.P. SPICER GAG Synthesis 54. a4-N-Acetylhexosaminyltransferase (EXTL2) ....................... 385 H. KITAGAWA and K. SUGAHARA 55. Hyaluronan Synthase-I, -2, and -3 ................................ 392 K. KIMATA 56. Heparan Sulfate GlcA/GlcNAc Transferase . . . . . . . . . . . . . . . . . . . . . . . . .. 397 M. KUSCHE-GULLBERG and U. LINDAHL 57. D-Glucuronyl C5-Epimerase in HeparinlHeparan Sulfate Biosynthesis 403 J.-P. LI and U. LINDAHL Sulfotransferases 58. Chondroitin 6-Sulfotransferase . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 413 O. HABUCHI 59. Keratan Sulfate Gal-6-Sulfotransferase . . . . . . . . . . . . . . . . . . . . . . . . . . . .. 418 M. FUKUTA and O. HABUCHI
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