tailieunhanh - Báo cáo khoa học: "Topology of Scavenger Receptor Class B Type I (SR-BI) on Brush Border Membrane"

Tuyển tập các báo cáo nghiên cứu khoa học quốc tế về bệnh thú y đề tài: Topology of Scavenger Receptor Class B Type I (SR-BI) on Brush Border Membrane | J. Vet. Sci. 2002 3 4 265-272 JOURNAL OF Veterinary Science Topology of Scavenger Receptor Class B Type I SR-BI on Brush Border Membrane Chang-Hoon Han1 and Mun-Han Lee2 1Brain Korea 21 School of Agricultural Biotechnology Seoul National University 441-744 Suwon Korea 2Department of Biochemistry College of Veterinary Medicine Seoul National University 441-744 Suwon Korea Received June 20 2002 Accepted November 11 2002 Abstract Both hydropathy plot and in vitro translation results predict the topology of SR-BI the receptor is an integral membrane protein of 509 amino acids consisting of a short cytoplasmic N-terminus of 9 amino acids followed by a first transmembrane dom ain of 22 amino acids the extracellular domain of 408 amino acids the second transm em brane dom ain of 22 amino acids and the cytoplasmic C-terminus of 47 amino acids. The immunoblot of rBBMV in the presence or absence of pAb589 peptide antigen the C-terminal 22 amino acid residues of SR-BI confirmed that the bands at app arent m olecular weight of 140 and 210 kDa are SR-BI related protein which might be multimeric forms of SR-BI. 125I apo A-I overlay analysis showed that SR-BI can bind to its ligand apo A-I only when it is thoroughly m atured - glycosylated and dimerized. The antibody w hich was generated against extracellular domain of SR-BI pAb230 not only prevented 125I-labeled apo A-I from binding to 140 kDa band but also inhibited the esterified cholesterol uptake of rabbit BBMV with its IC50 value of 40 K ml of IgG. In contrast the antibody generated against the C-terminal domain of SR-BI pAb589 did not show any effect either on cholesterol uptake of rabbit BBMV or 125I-labeled apo A-I binding to 140 kDa band. Overall results show that the ligand binding site of SR-BI in rabbit BBMV is located in extracellular domain and SR-BI is only functional when it is part of dim eric forms w hich ration alize the previously found cooperative nature of the binding interaction and m aybe a fundam ental .

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