Interactions of the receptor for insulin-like growth factor II with mannose-6-phosphate and antibodies to the mannose-6-phosphate receptor
作者： Richard R. Roth , Cynthia Stover , Joji Hari , David O. Morgan , Michele C. Smith
DOI: 10.1016/0006-291X(87)90410-4
关键词: Growth factor receptor 、 Insulin-like growth factor 2 receptor 、 Tropomyosin receptor kinase C 、 Biochemistry 、 Molecular biology 、 Mannose 6-phosphate 、 Glucagon-like peptide 1 receptor 、 Protease-activated receptor 2 、 Insulin receptor 、 Biology 、 Interleukin 5 receptor alpha subunit 、 Biophysics 、 Cell biology
摘要: Abstract Recently, the sequence of human receptor for insulin-like growth factor II (IGF-II) was found to be 80% identical [Morgan et al., (1987) Nature 329 , 301–307] a partial clone bovine cation-independent mannose-6-phosphate [Lobel Proc. Natl. Acad. Sci. USA 84 2233–2237]. In present study, purified react with two different polyclonal antibodies receptor. Moreover, stimulate binding labeled IGF-II by two-fold. This effect had same specificity and affinity as reported its receptor; mannose-1-phosphate mannose no on receptor, half-maximally effective concentration 0.3 mM. Also, did not affect insulin These results support hypothesis that single protein Mr∼250,000 binds both mannose-6-phosphate. Furthermore, they indicate can modulate interaction
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