Idioma:

Differences in local conformation in human apolipoprotein B-100 of plasma low density and very low density lipoproteins as identified by cathepsin D

CHI CHEN, G ; LAU, K ; HAMILTON, R. L ; KANE, J. P

The Journal of biological chemistry, 1991-07, Vol.266 (19), p.12581-12587 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

Texto completo disponível

Citações Citado por

Enviar para

Título:
Differences in local conformation in human apolipoprotein B-100 of plasma low density and very low density lipoproteins as identified by cathepsin D
Autor: CHI CHEN, G ; LAU, K ; HAMILTON, R. L ; KANE, J. P
Assuntos: Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Apolipoprotein B-100 ; Apolipoproteins B - chemistry ; Biological and medical sciences ; Cathepsin D - metabolism ; Cattle ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Humans ; Hydrogen-Ion Concentration ; Hydrolysis ; Lipoproteins, LDL - blood ; Lipoproteins, LDL - chemistry ; Lipoproteins, myelin ; Lipoproteins, VLDL - blood ; Lipoproteins, VLDL - chemistry ; Lipoproteins, VLDL - ultrastructure ; Microscopy, Electron ; Molecular Sequence Data ; Protein Conformation ; Proteins
É parte de: The Journal of biological chemistry, 1991-07, Vol.266 (19), p.12581-12587
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: The conformational changes of human apolipoprotein (apo) B-100 which accompany the conversion of plasma very low density lipoproteins (VLDL) to low density lipoproteins (LDL) were investigated by studying the accessibility of apoB-100 in LDL and VLDL to limited proteolysis with cathepsin D, an aspartyl proteinase involved in intracellular protein degradation. We characterized the proteolytic products of apoB-100 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by NH2-terminal sequence analysis to locate cleavage sites. The results identified at least 10 cleavage products generated from apoB-100 and showed differential accessibility of cleavage sites for cathepsin D in apoB-100 between LDL and VLDL. We identified a specific peptide region (residues 2660-2710), which is preferentially accessible to limited proteolysis by cathepsin D but inaccessible to limited proteolysis by 12 other enzymes tested. Within this peptide region, cathepsin D cleaved apoB-100 of LDL and VLDL preferentially at different sites, separated by 33-36 amino acids (2665-2666 or 2668-2669 (LDL) and 2701-2702 (VLDL]. In addition, we identified a cleavage site, located at residues 3272-3273, specific for cathepsin D, which is contained within the COOH-terminal enzyme-accessible peptide region (residues 3180-3280), which we have demonstrated using 12 endoproteases with various specificities. The previously identified NH2-terminal region (residues 1280-1320) appears to be resistant to limited cleavage by cathepsin D. However, a new site was revealed only approximately 66 kDA from the NH2 terminus. We conclude that differential accessibility and the shift of the novel scission site for cathepsin D by 33-36 amino acids indicate significant differences in local conformation at these sites in apoB-100 as VLDL are converted to LDL.
Editor: Bethesda, MD: American Society for Biochemistry and Molecular Biology
Idioma: Inglês

Links

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

Differences in local conformation in human apolipoprotein B-100 of plasma low density and very low density lipoproteins as identified by cathepsin D

CHI CHEN, G ; LAU, K ; HAMILTON, R. L ; KANE, J. P

Bethesda, MD: American Society for Biochemistry and Molecular Biology

Buscando em bases de dados remotas. Favor aguardar.