Recent development in mammalian sialidase molecular biology

被引：139

作者：

Monti, E ^{[1
]}

Preti, A

Venerando, B

Borsani, G

机构：

[1] Univ Brescia, Dept Biomed Sci & Biotechnol, I-25123 Brescia, Italy

[2] LITA, Dept Med Chem & Biochem, I-20090 Segrate, Italy

来源：

NEUROCHEMICAL RESEARCH | 2002年 / 27卷 / 7-8期

关键词：

mammalian sialidase; molecular cloning; gene structure and expression; molecular properties; transgenic expression;

D O I：

10.1023/A:1020276000901

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：

This review summarizes the recent research development on mammalian sialidase molecular cloning. Sialic acid-containing compounds are involved in several physiological processes, and sialidases, as glycohydrolytic enzymes that remove sialic acid residues, play a pivotal role as well. Sialidases hydrolyze the nonreducing, terminal sialic acid linkage in various natural substrates, such as glycoproteins, glycolipids, gangliosides, and polysaccharides. Mammalian sialidases are present in several tissues/organs and cells with a typical subcellular distribution: they are the lysosomal, the cytosolic, and the plasma membrane-associated sialidases. Starting in 1993, 12 different mammalian sialidases have been cloned and sequenced. A comparison of their amino acid sequences revealed the presence of highly conserved regions. These conserved regions are shared with viral and microbial sialidases that have been characterized at three-dimensional structural level, allowing us to perform the molecular modeling of the mammalian proteins and suggesting a monophyletic origin of the sialidase enzymes. Overall, the availability of the cDNA species encoding mammalian sialidases is an important step leading toward a comprehensive picture of the relationships between the structure and biological function of these enzymes.

引用

页码：649 / 663

页数：15

共 92 条

[1] Comparative enzymology, biochemistry and pathophysiology of human exo-α-sialidases (neuraminidases) [J].

Achyuthan, KE ;

Achyuthan, AM .

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 2001, 129 (01) :29-64

[2] Immunohistochemical evidence for the existence of rat cytosolic sialidase in rat skeletal muscles [J].

Akita, H ;

Miyagi, T ;

Hata, K ;

Kagayama, M .

HISTOCHEMISTRY AND CELL BIOLOGY, 1997, 107 (06) :495-503

[3] ESTABLISHING A HUMAN TRANSCRIPT MAP [J].

BOGUSKI, MS ;

SCHULER, GD .

NATURE GENETICS, 1995, 10 (04) :369-371

[4] Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis [J].

Bonten, E ;

vanderSpoel, A ;

Fornerod, M ;

Grosveld, G ;

dAzzo, A .

GENES & DEVELOPMENT, 1996, 10 (24) :3156-3169

[5] Lysosomal neuraminidase - Catalytic activation in insect cells is controlled by the protective protein/cathepsin A [J].

Bonten, EJ ;

d'Azzo, A .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (48) :37657-37663

[6] Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis [J].

Bonten, EJ ;

Arts, WF ;

Beck, M ;

Covanis, A ;

Donati, MA ;

Parini, R ;

Zammarchi, E ;

d'Azzo, A .

HUMAN MOLECULAR GENETICS, 2000, 9 (18) :2715-2725

[7] Structure and function of sphingolipid- and cholesterol-rich membrane rafts [J].

Brown, DA ;

London, E .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (23) :17221-17224

[8] INFLUENZA-B VIRUS NEURAMINIDASE CAN SYNTHESIZE ITS OWN INHIBITOR [J].

BURMEISTER, WP ;

HENRISSAT, B ;

BOSSO, C ;

CUSACK, S ;

RUIGROK, RWH .

STRUCTURE, 1993, 1 (01) :19-26

[9] THE 2.2-A RESOLUTION CRYSTAL-STRUCTURE OF INFLUENZA-B NEURAMINIDASE AND ITS COMPLEX WITH SIALIC-ACID [J].

BURMEISTER, WP ;

RUIGROK, RWH ;

CUSACK, S .

EMBO JOURNAL, 1992, 11 (01) :49-56

[10] MAP OF THE HUMAN MHC [J].

CAMPBELL, RD ;

TROWSDALE, J .

IMMUNOLOGY TODAY, 1993, 14 (07) :349-352

← 1 2 3 4 5 6 7 8 9 10 →