Document Detail


Human choriogonadotrophin protein core and sugar branches heterogeneity: basic and clinical insights.
MedLine Citation:
PMID:  18945715     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Human chorionic gonadotrophin (hCG) is measured in serum and urine for the early detection of ectopic pregnancy, patients with higher risk of miscarriage, embryos or fetuses with chromosome abnormalities, prediction of pre-eclampsia or fetal growth restriction and identification or follow-up of trophoblast neoplasia. This review examines basic knowledge on the heterogeneity of hCG protein core and sugar branches and its relevance to assays used in a clinical setting. METHODS: The databases Scielo and Medline/Pubmed were consulted for identification of the most relevant published papers. Search terms were gonadotrophin, glycoprotein structure, hCG structure and molecular forms of hCG. RESULTS: The synthesis of alpha (hCGalpha) and beta (hCGbeta) peptide chains and their further glycosylation involve the complex action of different enzymes. After assembly, hCG reaches the cell surface and is secreted as a bioactive heterodimer. The complex cascade of enzymes acting in hCG secretion results in heterogeneous molecular forms. The hCG molecules are differently metabolized by the liver, ovary and kidney, but the majority of hCG forms are excreted in the urine. Intact hCG, hCGalpha, hCGbeta, hyperglycosylated (hCGh), nicked (hCGn) and core fragment of hCGbeta (hCGbetacf) forms have relevant clinical use. The immunogenicity of each hCG variant, their epitopes distribution and the available antibodies are important for the development of specific assays. Depending on the prevalent form or proportion in relation to the intact hCG, the choice of assay for measurement of a specific molecule in a particular clinical setting is paramount. CONCLUSIONS: Measurement of hCG and/or its related molecules is useful in clinical practice, but greater awareness is needed worldwide regarding the use of new sensitive and specific assays tailored for different clinical applications.
Authors:
S F de Medeiros; R J Norman
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Publication Detail:
Type:  Journal Article; Review     Date:  2008-10-22
Journal Detail:
Title:  Human reproduction update     Volume:  15     ISSN:  1460-2369     ISO Abbreviation:  Hum. Reprod. Update     Publication Date:    2009 Jan-Feb
Date Detail:
Created Date:  2008-12-18     Completed Date:  2009-03-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9507614     Medline TA:  Hum Reprod Update     Country:  England    
Other Details:
Languages:  eng     Pagination:  69-95     Citation Subset:  IM    
Affiliation:
Department of Gynaecology and Obstetrics, Faculty of Medical Sciences, Federal University of Mato Grosso, Mato Grosso, Brazil. de.medeiros@terra.com.br
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Chorionic Gonadotropin / chemistry*,  immunology,  metabolism,  physiology
Female
Glycosylation
Humans
Models, Biological
Pregnancy
Protein Subunits / chemistry
Sequence Analysis, Protein
Signal Transduction
Chemical
Reg. No./Substance:
0/Chorionic Gonadotropin; 0/Protein Subunits

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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