Mannose 6-phosphate/insulin-like growth factor II receptor: distinct binding sites for mannose 6-phosphate and insulin-like growth factor II. 1988

T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
Biochemie II, Georg-August-Universität, Göttingen, West Germany.

Pentamannosyl phosphate substituted bovine serum albumin (PMP-BSA) and insulin like growth factor II (IGF II) bind specifically to immobilized mannose 6-phosphate/insulin like growth factor II receptor. An excess of IGF II inhibited binding of PMP-BSA by less than or equal to 20%, and an excess of PMP-BSA inhibited binding of IGF II by less than or equal to 10%. Polyclonal antibodies against the receptor purified from human liver inhibited preferentially the binding of PMP-BSA, and a monocloncal antibody 2C2 inhibited only the binding of IGF II to the receptor. Similar results were obtained for binding of PMP-BSA and IGF II to human skin fibroblasts. These results suggest that the binding sites for mannose 6-phosphate and IGF II reside in different portions of the receptor.

UI MeSH Term Description Entries
D007158 Immunologic Techniques Techniques used to demonstrate or measure an immune response, and to identify or measure antigens using antibodies. Antibody Dissociation,Immunologic Technic,Immunologic Technics,Immunologic Technique,Immunological Technics,Immunological Techniques,Technic, Immunologic,Technics, Immunologic,Technique, Immunologic,Techniques, Immunologic,Antibody Dissociations,Dissociation, Antibody,Dissociations, Antibody,Immunological Technic,Immunological Technique,Technic, Immunological,Technics, Immunological,Technique, Immunological,Techniques, Immunological
D007335 Insulin-Like Growth Factor II A well-characterized neutral peptide believed to be secreted by the LIVER and to circulate in the BLOOD. It has growth-regulating, insulin-like and mitogenic activities. The growth factor has a major, but not absolute, dependence on SOMATOTROPIN. It is believed to be a major fetal growth factor in contrast to INSULIN-LIKE GROWTH FACTOR I, which is a major growth factor in adults. IGF-II,Multiplication-Stimulating Activity,Somatomedin MSA,IGF-2,Insulin Like Growth Factor II,Insulin-Like Somatomedin Peptide II,Multiplication-Stimulating Factor,Somatomedin A,Factor, Multiplication-Stimulating,Insulin Like Somatomedin Peptide II,Multiplication Stimulating Activity,Multiplication Stimulating Factor
D007457 Iodine Radioisotopes Unstable isotopes of iodine that decay or disintegrate emitting radiation. I atoms with atomic weights 117-139, except I 127, are radioactive iodine isotopes. Radioisotopes, Iodine
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008360 Mannosephosphates Phosphoric acid esters of mannose.
D011972 Receptor, Insulin A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE. Insulin Receptor,Insulin Receptor Protein-Tyrosine Kinase,Insulin Receptor alpha Subunit,Insulin Receptor beta Subunit,Insulin Receptor alpha Chain,Insulin Receptor beta Chain,Insulin-Dependent Tyrosine Protein Kinase,Receptors, Insulin,Insulin Receptor Protein Tyrosine Kinase,Insulin Receptors
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D005347 Fibroblasts Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules. Fibroblast
D006600 Hexosephosphates
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
August 1998, The Journal of biological chemistry,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
June 2000, The Journal of biological chemistry,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
May 1990, European journal of biochemistry,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
March 1993, The Journal of biological chemistry,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
June 2000, The Journal of biological chemistry,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
December 1989, Cytotechnology,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
February 2006, Bioscience reports,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
December 1987, Biochemical and biophysical research communications,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
December 1997, Proceedings of the National Academy of Sciences of the United States of America,
T Braulke, and C Causin, and A Waheed, and U Junghans, and A Hasilik, and P Maly, and R E Humbel, and K von Figura
May 1990, Biochemical and biophysical research communications,
Copied contents to your clipboard!