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Titolo:
HUMAN VARIANT SEX HORMONE-BINDING GLOBULIN (SHBG) WITH AN ADDITIONAL CARBOHYDRATE CHAIN HAS A REDUCED CLEARANCE RATE IN RABBIT
Autore:
COUSIN P; DECHAUD H; GRENOT C; LEJEUNE H; PUGEAT M; BARET C; BREBANT C;
Indirizzi:
HOP ANTIQUAILLE,LAB CLIN ENDOCRINOL,1 RUE ANTIQUAILLE F-69321 LYON 05FRANCE HOP ANTIQUAILLE,LAB CLIN ENDOCRINOL F-69321 LYON 05 FRANCE HOP ANTIQUAILLE,CENT BIOCHIM LAB F-69321 LYON 05 FRANCE HOP DEBROUSSE,INSERM U329 F-69005 LYON FRANCE
Titolo Testata:
The Journal of clinical endocrinology and metabolism
fascicolo: 1, volume: 83, anno: 1998,
pagine: 235 - 240
SICI:
0021-972X(1998)83:1<235:HVSHG(>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID SEQUENCE; STEROID-BINDING; PROTEIN SBP; HALF-LIFE; MOLECULAR CHARACTERIZATION; RECOMBINANT THYROTROPIN; CELL-LINE; PLASMA; SERUM; WOMEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
P. Cousin et al., "HUMAN VARIANT SEX HORMONE-BINDING GLOBULIN (SHBG) WITH AN ADDITIONAL CARBOHYDRATE CHAIN HAS A REDUCED CLEARANCE RATE IN RABBIT", The Journal of clinical endocrinology and metabolism, 83(1), 1998, pp. 235-240

Abstract

Sex hormone-binding globulin (SHBG) is the specific plasma transport protein for sex steroid hormones in humans. Considerable variation in SHBG plasma concentration exists between individuals, irrespective of gender, body weight, or thyroid status. In the present work, the influence of carbohydrate chains on the half-life of human SHBG (hSHBG) wasinvestigated using a rabbit model. A variant hSHBG, with a point mutation in exon 8 (GAC --> AAC) encoding an amino acid substitution (Asp327Asn), which introduces an additional consensus site for N-glycosylation, has recently been identified. This mutation suppresses a recognition site for the restriction enzyme Bbs-I, allowing the development ofa simple restriction-fragments length polymorphism (RFLP) screening procedure. In a population of patients (272 female and 49 male) consulting in our Endocrinology Clinic, 48 patients (41 female and 7 male) were heterozygous for the variant hSHBG allele and 3 (2 female and 1 male) were homozygous. In this population, the total variant allele frequency was 0.083. The hSHBG genotype, as determined by RFLP, corresponded in all cases to the phenotype as determined by the migration profileof hSHBG by Western blot analysis. The influence of such an additional glycosylation site on the biological half-life of variant hSHBG was investigated. SHBG from serum of patients carrying one of the three hSHBG genotypes was purified and labeled with biotin, then injected intorabbits, as we have recently described for rabbit SHBG. Biotinylated hSHBG was captured from rabbit serum samples on tubes coated with an anti-hSHBG antibody and detected by luminometry with the streptavidine-alkaline phosphatase-dioxetane (AMPPD) system. The results showed thatthe half-life Value was significantly higher (P < 0.05) for SHBG purified from homozygous variant serum (t 1/2 beta = 51.43 +/- 1.15 and 63.63 +/- 3.92 h, for male and a female subjects SHBG respectively) thanfor SHBG purified from heterozygous variant serum (t 1/2 beta = 40.19+/- 0.12 h) or wild-type (t 1/2 beta = 38.18 +/- 7.22 h). This study demonstrated that an additional carbohydrate chain on hSHBG decreases the clearance rate of this protein. The low frequency of this variant allele means that further study will be required to determine whether it is associated with higher serum SHBG concentration.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 18:55:01