The glycosyl phosphatidylinositol anchor of human T-cadherin binds lipoproteins
| Autor: | Frances Kern, Paul Erne, Thérèse J. Resink, Thomas Niermann |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Signal peptide
Glycosylphosphatidylinositols Molecular Sequence Data Biophysics Biology Transfection Biochemistry Muscle Smooth Vascular law.invention Cell Line Phosphoinositide Phospholipase C law Cricetinae Animals Humans cardiovascular diseases Amino Acid Sequence Cell adhesion Molecular Biology Lung Aorta Cells Cultured Phospholipase C Phosphatidylinositol Diacylglycerol-Lyase HEK 293 cells Cell Biology Fibroblasts Cadherins Molecular biology Cell biology T-cadherin Blot Lipoproteins LDL Molecular Weight Solubility Type C Phospholipases Mutation Recombinant DNA lipids (amino acids peptides and proteins) Sequence Alignment Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 276(3) |
| ISSN: | 0006-291X |
| Popis: | T-cadherin (T-cad) is a Ca 2+ -dependent cell adhesion glycoprotein bound to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor. T-cad expressed on vascular smooth muscle cells (SMC) binds lipoproteins on blot. To analyze the molecular basis for the interaction of T-cad with lipoproteins we expressed recombinant human T-cad in HEK293 cells. Whereas membrane-bound T-cad from SMC and T-cad transfected HEK293 cells bind lipoproteins, T-cadherin proteins cleaved from the cell surface by phosphatidylinositol-specific phospholipase C (PI-PLC) do not. The lipoprotein-binding function is also lacking both for a recombinant human T-cad expressed in HEK293 cells without the GPI signal sequence, and for a human T-cad form expressed in Escherichia coli that contains the signal sequence for GPI attachment but is not modified with a GPI. We conclude that the GPI moiety of T-cadherin is necessary and sufficient to mediate lipoprotein binding. |
| Databáze: | OpenAIRE |
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