Two-dimensional protein electrophoresis and multiple hypothesis testing to detect potential serum protein biomarkers in children with fetal alcohol syndrome
| Autor: | Henderson Lo, Orr Ga, Claire D. Coles, Powell Mk, Peter F. Lemkin, Myrick Je, Robinson Mk |
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| Rok vydání: | 1995 |
| Předmět: |
Male
medicine.medical_specialty Silver Staining Clinical Biochemistry Fetal alcohol syndrome Protein metabolism Biology Biochemistry Analytical Chemistry Silver stain chemistry.chemical_compound Internal medicine medicine Image Processing Computer-Assisted Humans Electrophoresis Gel Two-Dimensional Child Gel electrophoresis Haptoglobin Transferrin Blood Proteins Gel electrophoresis of proteins medicine.disease Molecular biology Blood proteins Retinol binding protein Endocrinology chemistry Fetal Alcohol Spectrum Disorders Case-Control Studies biology.protein Female Biomarkers |
| Zdroj: | Electrophoresis. 16(7) |
| ISSN: | 0173-0835 |
| Popis: | Fetal alcohol syndrome (FAS) surveillance and intervention efforts are hampered by the lack of a specific biochemical test for diagnosis of the syndrome. Based on the hypothesis that abnormalities in growth and development (key features of FAS) involve altered protein metabolism, we analyzed serum proteins by two-dimensional gel electrophoresis and image analysis to search for potential protein biomarkers of FAS. Serum samples from 12 participants in whom FAS had been diagnosed and 8 sex- and age-matched participants whose mothers did not consume alcohol were analyzed in duplicate to determine whether the integrated intensities of matched proteins are significantly altered in children with FAS. Multiple hypothesis testing on 34 of the gels consisting of more than 1700 spots per gel revealed 21 proteins that we classified as potential protein biomarkers of FAS on the basis of significant t-test differences at p < 0.02. We classified 8 of the proteins as candidate biomarkers on the basis of significant concentration differences between case and control subjects at p < 0.01. One of the proteins is clearly an isoform of retinol binding protein; two appear in the area of the gel where alcohol dehydrogenase is expected to appear; one appears to be an isoform of alpha-1-antitrypsin; three appear to be isoforms of the beta-chain of haptoglobin; three may be forms of immunoglobulin light chains; and several others have not been associated with known proteins. No single protein differentiated all case subjects from control subjects, but stepwise canonical discriminant analyses revealed four groups of spots that distinguished between FAS case and control subjects with no misclassifications.(ABSTRACT TRUNCATED AT 250 WORDS) |
| Databáze: | OpenAIRE |
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