دورية أكاديمية
Hutchinson-Gilford progeria types defined by differential binding of lectin DSA.
| العنوان: | Hutchinson-Gilford progeria types defined by differential binding of lectin DSA. |
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| المؤلفون: | Clark MA; Department of Biochemistry, University of Sydney, NSW, Australia., Weiss AS |
| المصدر: | Biochimica et biophysica acta [Biochim Biophys Acta] 1995 Apr 24; Vol. 1270 (2-3), pp. 142-8. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam : Elsevier Pub. Co. |
| مواضيع طبية MeSH: | Plant Lectins*, Lectins/*metabolism , Progeria/*metabolism, Adolescent ; Carbohydrate Sequence ; Cells, Cultured ; Child ; Child, Preschool ; Female ; Fibroblasts/metabolism ; Glycoproteins/chemistry ; Glycoproteins/metabolism ; Humans ; Infant ; Male ; Molecular Sequence Data ; Phenotype ; Progeria/classification ; Protein Binding |
| مستخلص: | Hutchinson-Gilford Progeria Syndrome (progeria) is an extremely rare childhood disorder characterized by precocious senility which presents features similar to those seen in human aging. We have previously described a consistent increase of the glycoprotein gp200 in progeria skin fibroblasts in vitro. Here we extend these glycosylation studies and present evidence for the existence of two types of progeria skin fibroblasts. These two forms, called D- and D+, are distinguished by their response to the lectin DSA. In the D- group, DSA bound glycoproteins from progeria fibroblast strains AG03513B and AG10750 with markedly lower affinities compared with glycoproteins from three control fibroblast strains. In the D+ group, DSA binding to glycoproteins from four other progeria strains AG01972A, AG06297A, AG06917 and AG03198, was comparable to controls. Discrimination by DSA is the most distinctive feature of the D- and D+ groups, in contrast to binding of lectins Con A, GNA, PHA-L, RCA120, AAA and PNA which show no such selectivity. The data are consistent with a model of altered glycosylation in the D- type of progeria fibroblasts. |
| المشرفين على المادة: | 0 (Datura stramonium lectin) 0 (Glycoproteins) 0 (Lectins) 0 (Plant Lectins) |
| تواريخ الأحداث: | Date Created: 19950424 Date Completed: 19950531 Latest Revision: 20190610 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1016/0925-4439(94)00081-z |
| PMID: | 7727537 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0006-3002 |
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| DOI: | 10.1016/0925-4439(94)00081-z |