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Titolo:
Biochemical characterization of a neuroserpin variant associated with hereditary dementia
Autore:
Yazaki, M; Liepnieks, JJ; Murrell, JR; Takao, M; Guenther, B; Piccardo, P; Farlow, MR; Ghetti, B; Benson, MD;
Indirizzi:
Indiana Univ, Sch Med, Dept Pathol & Lab Med, Indianapolis, IN 46202 USA Indiana Univ Indianapolis IN USA 46202 ab Med, Indianapolis, IN 46202 USA
Titolo Testata:
AMERICAN JOURNAL OF PATHOLOGY
fascicolo: 1, volume: 158, anno: 2001,
pagine: 227 - 233
SICI:
0002-9440(200101)158:1<227:BCOANV>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
TISSUE-PLASMINOGEN ACTIVATOR; SERINE-PROTEASE INHIBITOR; INCLUSION-BODIES; ALPHA1-ANTITRYPSIN DEFICIENCY; CORPORA-AMYLACEA; MOLECULAR-BASIS; LUNG-DISEASE; LIVER; ALPHA-1-ANTITRYPSIN; MUTATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Benson, MD Indiana Univ, Sch Med, Dept Pathol & Lab Med, 975 W Walnut St,IB-503, Indianapolis, IN 46202 USA Indiana Univ 975 W Walnut St,IB-503 Indianapolis IN USA 46202 A
Citazione:
M. Yazaki et al., "Biochemical characterization of a neuroserpin variant associated with hereditary dementia", AM J PATH, 158(1), 2001, pp. 227-233

Abstract

Neuroserpin isolated from inclusion bodies in the brain. of a patient witha neurodegenerative disease was characterized biochemically, The protein consisted of residues 20 to 410 of the neuroserpin precursor deduced from its cDNA sequence indicating the entire molecule was deposited. A minor amount started with residue 19 of the precursor, and the carboxyl terminus was heterogeneous ending at residues 405, 407, 409, and 410. Arg was present at position 52, No normal Ser52 was found indicating that only mutant neuroserpin was present in the inclusion bodies. The three potential Asn glycosylation sites all contained carbohydrate, DNA sequence analysis of exons 2 to 19 of the neuroserpin gene in the proband showed the published normal neuroserpin sequence except for the presence of both adenine and cytosine at the first position of codon 52, that indicates heterozygosity for both the normal Ser(AGT) and variant Arg(CGT) at this position in the expressed protein,Restriction fragment length polymorphism analysis of a polymerase chain reaction product from exon 2 revealed the propositus and his affected siblingboth were heterozygous for the mutation whereas 100 unaffected controls were negative, Chemical characterization of the variant neuroserpin will significantly enhance the understanding of this protein in both normal physiology and neurodegenerative diseases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 05:48:24