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Titolo:
TISSUE TRANSGLUTAMINASE-CATALYZED FORMATION OF HIGH-MOLECULAR-WEIGHT AGGREGATES IN-VITRO IS FAVORED WITH LONG POLYGLUTAMINE DOMAINS - A POSSIBLE MECHANISM CONTRIBUTING TO CAG-TRIPLET DISEASES
Autore:
GENTILE V; SEPE C; CALVANI M; MELONE MAB; COTRUFO R; COOPER AJL; BLASS JP; PELUSO G;
Indirizzi:
UNIV NAPLES 2,DIPARTIMENTO BIOCHIM & BIOFIS,VIA COSTANTINOPOLI 16 I-80138 NAPLES ITALY UNIV NAPLES 2,IST SCI NEUROL I-80138 NAPLES ITALY DIREZ SCI SIGMA TAU POMEZIA ROME ITALY CNR,IST BIOCHIM PROT & ENZIMOL I-80125 NAPLES ITALY CORNELL UNIV,COLL MED,DEPT BIOCHEM NEW YORK NY 10021 CORNELL UNIV,COLL MED,DEPT NEUROL & NEUROSCI NEW YORK NY 10021 CORNELL UNIV,COLL MED,DEPT MED NEW YORK NY 10021 CORNELL UNIV,COLL MED,BURKE MED RES INST WHITE PLAINS NY 10605
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 2, volume: 352, anno: 1998,
pagine: 314 - 321
Fonte:
ISI
Lingua:
ENG
Soggetto:
CROSS-LINKING ENZYMES; HUNTINGTONS-DISEASE; GLUTAMINE REPEATS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; NEURODEGENERATIVE DISEASES; SUBSTANCE-P; CELL-DEATH; IN-VIVO; PROTEIN; IDENTIFICATION;
Keywords:
TISSUE TRANSGLUTAMINASE; HUNTINGTON DISEASE; Q(N) DOMAINS; CAG EXPANSIONS; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; POLYAMINES; NEURODEGENERATIVE DISEASES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
V. Gentile et al., "TISSUE TRANSGLUTAMINASE-CATALYZED FORMATION OF HIGH-MOLECULAR-WEIGHT AGGREGATES IN-VITRO IS FAVORED WITH LONG POLYGLUTAMINE DOMAINS - A POSSIBLE MECHANISM CONTRIBUTING TO CAG-TRIPLET DISEASES", Archives of biochemistry and biophysics, 352(2), 1998, pp. 314-321

Abstract

To investigate possible biochemical mechanisms underlying the ''toxicgain of function'' associated with polyglutamine expansions, the ability of guinea pig liver tissue transglutaminase to catalyze covalent attachments of various polyamines to polyglutamine peptides was examined. Of the polyamines tested, spermine is the most active substrate, followed by spermidine and putrescine. Formation of covalent cross linksbetween polyglutamine peptides and polyamines yields high-M-r aggregates-a process that is favored with longer polyglutamines. In the presence of tissue transglutaminase, purified glyceraldehyde-3-phosphate dehydrogenase (a key glycolytic enzyme that binds tightly to the polyglutamine domains of both huntingtin and dentatorubral-pallidoluysian atrophy proteins) is covalently attached to polyglutamine peptides in vitro, resulting in the formation of high-M-r aggregates. In addition, endogenous glyceraldehyde-3-phosphate dehydrogenase of a Balb-c 3T3 fibroblast cell line overexpressing human tissue transglutaminase forms cross-links with a Q(60) polypeptide added to the cell homogenate. Possibly, expansion of polyglutamine domains (thus far known to occur in the gene products associated with at least seven neurodegenerative diseases) leads to increased/aberrant tissue transglutaminase-catalyzed cross-linking reactions with both polyamines and susceptible proteins, such as glyceraldehyde-3-phosphate dehydrogenase. Formation of cross-linked heteropolymers may lead to deposition of high-M-r protein aggregates, thereby contributing to cell death. (C) 1998 Academic Press.

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Documento generato il 30/11/20 alle ore 16:34:19