Characterization of chicken cystatin binding to rat renal brush-border membranes
| Autor: | Maria Warwas, Jakub Gburek, Krzysztof Gołab, Bogusława Konopska |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Male
Kidney Cortex Brush border Physiology Serum albumin Receptors Cell Surface Chick Embryo urologic and male genital diseases Binding Competitive Biochemistry Kidney Tubules Proximal Animals Rats Inbred BUF Binding site Bovine serum albumin Receptor Molecular Biology Cells Cultured Binding Sites Microvilli biology Chemistry Serum Albumin Bovine Cubilin Cystatins Rats Molecular Weight Low Density Lipoprotein Receptor-Related Protein-2 Cystatin C biology.protein Calcium Cystatin Fluorescein-5-isothiocyanate |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 146:482-488 |
| ISSN: | 1096-4959 |
| DOI: | 10.1016/j.cbpb.2006.11.004 |
| Popis: | Chicken cystatin, a homologue of human cystatin C, like other low-molecular-weight proteins is metabolized by renal proximal tubule cells. However, the precise mechanism(s) of this process has not been elucidated yet. To characterize chicken cystatin binding to renal brush-border membranes, the incubation of fluorescein labelled protein with rat cortical homogenate was performed. Saturation-dependent and reversible binding with low affinity (K(d)=3.67-4.07 microM) and high capacity (B(max)=2.32-2.79 nmol/mg) was observed. Bovine albumin was the most potent competitor (K(i)=0.7 microM) among other megalin/cubilin ligands tested. The presence of Ca(+2) ions was necessary to effective cystatin binding by brush-border membranes. Obtained data strongly support the hypothesis that chicken cystatin is a novel ligand for megalin/cubilin receptors tandem on proximal tubular cells. |
| Databáze: | OpenAIRE |
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