title: Amyloid insulin interaction with erythrocytes.
abstract: Erythrocyte membrane interactions with insulin fibrils (amyloid) have been investigated using centrifugation, fluorescence spectroscopy, light scattering, and flow cytometric techniques. The results indicate that insulin fibrils are having moderate affinity to erythrocyte membrane. However, analysis of the apparent dissociation constants of human erythrocyte membranes (leaky and resealed vesicles) with amyloid insulin reveal that the insulin binding is drastically reduced on attaining the fibrillar state compared with native insulin. To understand the role of insulin receptors on erythrocytes binding to amyloid, we have studied the interaction of biotinylated forms of denatured and amyloidic insulin with erythrocytes. FITC-streptavidin was used as a counter staining in flow cytometry measurements. We found that insulin fibrils bind 10 times more with erythrocyte membranes than with amylin and denatured insulin.
authors.affiliation: Bio organic and Neurochemistry Laboratory, Central Leather Research Institute, Adyar, Chennai 600 020, India.
authors.forename: J
authors.initials: J
authors.lastname: Murali
authors.forename: D
authors.initials: D
authors.lastname: Koteeswari
authors.forename: J M
authors.initials: JM
authors.lastname: Rifkind
authors.forename: R
authors.initials: R
authors.lastname: Jayakumar
mesh_terms: D000682:Amyloid / Q000096:biosynthesis / Q000378:metabolism*; D002498:Centrifugation / Q000379:methods; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005434:Flow Cytometry / Q000379:methods; D006801:Humans; D007328:Insulin / Q000378:metabolism*; D008859:Microscopy, Polarization / Q000379:methods; D011485:Protein Binding; D013050:Spectrometry, Fluorescence / Q000379:methods
chemical_list: D000682:Amyloid; D007328:Insulin