Abstract
Amino acid sequences deduced from rat complementary DNA clones encoding the insulin-like growth factor II (IGF-II) receptor closely resemble those of the bovine cation-independent mannose-6-phosphate receptor (Man-6-P receptorCI), suggesting they are identical structures. It is also shown that IGF-II receptors are adsorbed by immobilized pentamannosyl-6-phosphate and are specifically eluted with Man-6-P. Furthermore, Man-6-P specifically increases by about two times the apparent affinity of the purified rat placental receptor for 125I-labeled IGF-II. These results indicate that the type II IGF receptor contains cooperative, high-affinity binding sites for both IGF-II and Man-6-P-containing proteins.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Cell Membrane / analysis
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Cell Membrane / metabolism
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Chromatography, Affinity
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DNA / genetics
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Female
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Hexosephosphates / metabolism*
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Insulin-Like Growth Factor II / metabolism*
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Mannosephosphates / metabolism*
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Molecular Sequence Data
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Placenta / analysis
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Pregnancy
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Rats
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Receptor, IGF Type 2
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Receptor, Insulin / genetics
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Receptor, Insulin / metabolism*
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Receptors, Somatomedin
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Sequence Homology, Nucleic Acid
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Somatomedins / metabolism*
Substances
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Carrier Proteins
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Hexosephosphates
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Mannosephosphates
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Receptor, IGF Type 2
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Receptors, Somatomedin
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Somatomedins
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mannose-6-phosphate
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Insulin-Like Growth Factor II
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DNA
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Receptor, Insulin