Mannose 6-phosphate-independent endocytosis of β-glucuronidase by human fibroblasts
作者： Alfonso González-Noriega , Colette Michalak , Jose Raymundo Cruz-Perez , Felipe Masso
DOI: 10.1016/S0167-4889(00)00140-3
关键词: Peptide 、 Endocytic cycle 、 Endocytosis 、 Biology 、 Biochemistry 、 Peptide sequence 、 Receptor-mediated endocytosis 、 Pronase 、 Mannose 6-phosphate 、 Mannose
摘要: Abstract Prior work has shown that endocytosis of bovine β-glucuronidase by human fibroblasts can be mediated the existence a Man6P-independent receptor for recapture and targeting to lysosomes. In this study, we have isolated peptide (IIIb2) from pronase digested behaved as competitive inhibitor fibroblasts. This contained Ser–X–Ser sequence, where X is probably posttranslational modified Trp. Antibodies raised against impaired but not β-glucuronidase, implying new recognition marker acid hydrolases might reside in single discrete stretch amino sequence. On other hand, been bind specifically receptors fibroblast membranes. The binding was saturable, divalent cation-dependent competitively inhibited IIIb2 peptide, mannose 6-phosphate. Results presented suggested an interplay between manganese concentrations, temperature pH on dissociation β-glucuronidase-receptor complexes. All together, these data reinforce presence two endocytic systems
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