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Titolo:
Balancing N-linked glycosylation to avoid disease
Autore:
Freeze, HH; Westphal, V;
Indirizzi:
Burnham Inst, La Jolla, CA 92037 USA Burnham Inst La Jolla CA USA 92037Burnham Inst, La Jolla, CA 92037 USA
Titolo Testata:
BIOCHIMIE
fascicolo: 8, volume: 83, anno: 2001,
pagine: 791 - 799
SICI:
0300-9084(200108)83:8<791:BNGTAD>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
RABIES VIRUS GLYCOPROTEIN; HEPATITIS-B VIRUS; CARBOHYDRATE-DEFICIENT TRANSFERRIN; ALPHA-GLUCOSIDASE INHIBITORS; ROUGH ENDOPLASMIC-RETICULUM; NEONATAL MARFAN-SYNDROME; CONGENITAL DISORDER; CORE-GLYCOSYLATION; QUALITY-CONTROL; SACCHAROMYCES-CEREVISIAE;
Keywords:
congenital disorder(s) of glycosylation; single nucleotide polymorphism; mental retardation; hepatitis; viral infection;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
89
Recensione:
Indirizzi per estratti:
Indirizzo: Freeze, HH Burnham Inst, 10901 N Torrey Pines Rd, La Jolla, CA 92037 USA Burnham Inst 10901 N Torrey Pines Rd La Jolla CA USA 92037 USA
Citazione:
H.H. Freeze e V. Westphal, "Balancing N-linked glycosylation to avoid disease", BIOCHIMIE, 83(8), 2001, pp. 791-799

Abstract

Complete loss of N-glycosylation is lethal in both yeast and mammals. Substantial deficiencies in some rate-limiting biosynthetic steps cause human congenital disorders of glycosylation (CDG). Patients have a range of clinical problems including variable degrees of mental retardation, liver dysfunction, and intestinal disorders. Over 60 mutations in phosphomannomutase (encoded by PMM2) diminish activity and cause CDG-Ia. The severe mutation R141H in PMM2 is lethal when homozygous, but heterozygous in about 1/70 Northern Europeans. Another disorder, CDG-Ic, is caused by mutations in ALG6, an alpha1,3glucosyl transferase used for lipid-linked precursor synthesis, yet some function-compromising mutations occur at a high frequency in this genealso. Maintenance of seemingly deleterious mutations implies a selective advantage or positive heterosis. One possible explanation for this is that production of infective viruses such as hepatitis virus B and C, or others that rely heavily on host N-glycosylation, is substantially inhibited when only a tiny fraction of their coat proteins is misglycosylated. In contrast,this reduced glycosylation does not affect the host. Prevalent functional mutations in rate-limiting glycosylation steps could provide some resistance to viral infections, but the cost of this insurance is CDG. A balanced glycosylation level attempts to accommodate these competing agendas. By assessing the occurrence of a series of N-glycosylation-compromising alleles in multi-genic diseases, it may be possible to determine whether impaired glycosylation is a risk factor or a major determinant underlying their pathology. (C) 2001 Societe francaise de biochimie et biologic moleculaire/Editionsscientifiques et medicales Elsevier SAS. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 10:37:03