Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages

被引:328
作者
Renkema, GH
Boot, RG
Au, FL
Donker-Koopman, WE
Strijland, A
Muijsers, AO
Hrebicek, M
Aerts, JMFG
机构
[1] Univ Amsterdam, Acad Med Ctr, Dept Biochem, NL-1100 DE Amsterdam, Netherlands
[2] Charles Univ, Fac Med 1, Ctr Inborn Errors Metab, Prague, Czech Republic
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1998年 / 251卷 / 1-2期
关键词
chitinase; chitotriosidase; human cartilage glycoprotein of 39 kDa; macrophages; lectin;
D O I
10.1046/j.1432-1327.1998.2510504.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In various mammals, enzymatically active and inactive members of family 18 glycosyl hydrolases, containing chitinases, have been identified. In man, chitotriosidase is the functional chitinolytic enzyme, whilst the homologous human cartilage 39-kDa glycoprotein (HC gp-39) does not exhibit chitinase activity and its function is unknown. This study establishes that HC gp-39 is a chitin-specific lectin. It is experimentally demonstrated that a single amino acid substitution in the catalytic centre of the 39-kDa isoform of chitotriosidase, which generates a similar sequence to that in HC gp-39, results in a loss of hydrolytic activity and creates the capacity to bind to chitin. The possible implication of the finding for chitinolytic and chitin-binding proteins that are produced in high quantities by activated macrophages are discussed.
引用
收藏
页码:504 / 509
页数:6
相关论文
共 46 条
  • [31] CRYSTAL-STRUCTURE OF A BACTERIAL CHITINASE AT 2.3-ANGSTROM RESOLUTION
    PERRAKIS, A
    TEWS, I
    DAUTER, Z
    OPPENHEIM, AB
    CHET, I
    WILSON, KS
    VORGIAS, CE
    [J]. STRUCTURE, 1994, 2 (12) : 1169 - 1180
  • [32] ISOLATION AND CHARACTERIZATION OF A NOVEL 39-KILODALTON WHEY-PROTEIN FROM BOVINE MAMMARY SECRETIONS COLLECTED DURING THE NONLACTATING PERIOD
    REJMAN, JJ
    HURLEY, WL
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1988, 150 (01) : 329 - 334
  • [33] PURIFICATION AND CHARACTERIZATION OF HUMAN CHITOTRIOSIDASE, A NOVEL MEMBER OF THE CHITINASE FAMILY OF PROTEINS
    RENKEMA, GH
    BOOT, RG
    MUIJSERS, AO
    DONKERKOOPMAN, WE
    AERTS, JMFG
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (05) : 2198 - 2202
  • [34] Synthesis, sorting, and processing into distinct isoforms of human macrophage chitotriosidase
    Renkema, GH
    Boot, RG
    Strijland, A
    DonkerKoopman, WE
    vandenBerg, M
    Muijsers, AO
    Aerts, JMFG
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 244 (02): : 279 - 285
  • [35] CHITINASES OF FUNGI AND PLANTS - THEIR INVOLVEMENT IN MORPHOGENESIS AND HOST-PARASITE INTERACTION
    SAHAI, AS
    MANOCHA, MS
    [J]. FEMS MICROBIOLOGY REVIEWS, 1993, 11 (04) : 317 - 338
  • [36] IDENTIFICATION OF 2 ASPARTATES AND A GLUTAMATE ESSENTIAL FOR THE ACTIVITY OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE-H FROM STREPTOMYCES-PLICATUS
    SCHMIDT, BF
    ASHIZAWA, E
    JARNAGIN, AS
    LYNN, S
    NOTO, G
    WOODHOUSE, L
    ESTELL, DA
    LAD, P
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1994, 311 (02) : 350 - 353
  • [37] IDENTIFICATION OF A 38-KDA HEPARIN-BINDING GLYCOPROTEIN (GP38K) IN DIFFERENTIATING VASCULAR SMOOTH-MUSCLE CELLS AS A MEMBER OF A GROUP OF PROTEINS ASSOCIATED WITH TISSUE REMODELING
    SHACKELTON, LM
    MANN, DM
    MILLIS, AJT
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (22) : 13076 - 13083
  • [38] DETECTION OF CHITINASE ACTIVITY AFTER POLYACRYLAMIDE-GEL ELECTROPHORESIS
    TRUDEL, J
    ASSELIN, A
    [J]. ANALYTICAL BIOCHEMISTRY, 1989, 178 (02) : 362 - 366
  • [39] Mannose-binding lectin: The pluripotent molecule of the innate immune system
    Turner, MW
    [J]. IMMUNOLOGY TODAY, 1996, 17 (11): : 532 - 540
  • [40] The 1.8 angstrom resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18
    vanScheltinga, ACT
    Hennig, M
    Dijkstra, BW
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1996, 262 (02) : 243 - 257