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Titolo:
Comparative enzymology, biochemistry and pathophysiology of human exo-alpha-sialidases (neuraminidases)
Autore:
Achyuthan, KE; Achyuthan, AM;
Indirizzi:
ZymeTx Inc, Oklahoma City, OK 73104 USA ZymeTx Inc Oklahoma City OK USA 73104 Tx Inc, Oklahoma City, OK 73104 USA Univ Oklahoma, Hlth Sci Ctr, Dept Ophthalmol, Dean McGee Eye Inst, Oklahoma City, OK 73104 USA Univ Oklahoma Oklahoma City OK USA 73104 nst, Oklahoma City, OK 73104 USA
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 1, volume: 129, anno: 2001,
pagine: 29 - 64
SICI:
1096-4959(200105)129:1<29:CEBAPO>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED HUMAN-FIBROBLASTS; BETA-GALACTOSIDASE DEFICIENCY; HUMAN PLACENTAL SIALIDASE; INFLUENZA-VIRUS NEURAMINIDASE; SURFACE GANGLIOSIDE SIALIDASE; HUMAN LYSOSOMAL NEURAMINIDASE; PERIODATE-RESORCINOL METHOD; HUMAN NEUROBLASTOMA-CELLS; N-ACETYLNEURAMINIC ACID; PROTEIN CATHEPSIN-A;
Keywords:
human sialidase; human neuraminidase; sialic acid; biochemistry; pathophysiology; enzymology; molecular properties; deficiency and disease;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
202
Recensione:
Indirizzi per estratti:
Indirizzo: Achyuthan, KE ZymeTx Inc, 800 Res Pkwy 100, Oklahoma City, OK 73104 USA ZymeTx Inc 800 Res Pkwy 100 Oklahoma City OK USA 73104 4 USA
Citazione:
K.E. Achyuthan e A.M. Achyuthan, "Comparative enzymology, biochemistry and pathophysiology of human exo-alpha-sialidases (neuraminidases)", COMP BIOC B, 129(1), 2001, pp. 29-64

Abstract

This review summarizes the current research on human exo-alpha -sialidase (sialidase, neuraminidase). Where appropriate, the properties of viral, bacterial, and human sialidases have been compared. Sialic acids are implicated in diverse physiological processes. Sialidases, as enzymes acting upon sialic acids, assume importance as well. Sialidases hydrolyze the terminal. non-reducing, sialic acid linkage in glycoproteins, glycolipids: gangliosides, polysaccharides, and synthetic molecules. Therefore, a variety of assaysare available to measure sialidase activity. Human sialidase is present inseveral organs and cells. Its cellular distribution could be cytosolic, lysosomal, or in the membrane. Human sialidase occurs in a high molecular-mass complex with several other proteins, including cathepsin A and beta -galactosidase. Multi-protein complexation is important for the in vivo integrity and catalytic activity of the sialidase. However, multi-protein complexation, the occurrence of isoenzymes, diverse subcellular localization, thermal instability, and membrane association have all contributed to difficulties in purifying and characterizing human sialidases. Human sialidase isoenzymes have recently been cloned and sequenced. Even though crystal structuresfor the human sialidases are not available, the highly conserved regions of the sialidase from various organisms have facilitated molecular modeling of the human enzyme and raise interesting evolutionary questions. While themolecular mechanisms vary, genetic defects leading to human sialidase deficiency are closely associated with at least two well-known human diseases, namely sialidosis and galactosialidosis. No therapy is currently available for either disease. A thorough investigation of human sialidases is therefore crucial to human health. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 12:13:04