Insulin-like growth factor I (IGF I) receptor autophosphorylation and kinase activity. Effect of a human polyclonal antibody (pIgG) |
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| Authors: | R Cordera R Gherzi R De Pirro G Andraghetti G R Freidenberg F Minuto R Lauro G Giordano L Adezati |
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| Affiliation: | 1. Depts. of internal Medicine, University of Genoa, Genoa, Italy;1. Biomedical Sciences Department, Pharmacy and Pharmaceutical Technology Unit, Faculty of Pharmacy, Ctra. Madrid-Barcelona (Autovía A-II) Km. 33,600, 28805, Alcalá de Henares, Madrid, Spain;2. Faculty of Pharmacy, University of Alcalá, Alcalá de Henares, Madrid, Spain;1. Department of Ophthalmology, San Carlos Clinical Hospital, Madrid, Spain;2. Department of Pharmacy and Pharmaceutical Technology, School of Pharmacy, Complutense University of Madrid, Spain;3. Health Research Institute of the San Carlos Clinical Hospital (IdISSC), Madrid, Spain;4. Ocular Pathology National Net (OFTARED) of the Institute of Health Carlos III, Spain;5. Instituto Universitario de Farmacia Industrial (IUFI), School of Pharmacy, Complutense University of Madrid, Spain;1. Neuroscience Institute, Italian National Research Council (CNR), Area della Ricerca, Via Giuseppe Moruzzi 1, 56124 Pisa, Italy;2. Department of Pharmacy, University of Pisa, Pisa, Italy |
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| Abstract: | IGF I receptor is a tyrosine kinase capable of phosphorylating the receptor itself and other substrates. A high degree of homology does exist in tyrosine kinase domain among receptors for several polypeptide growth factor receptors and this enzymic activity has been indicated as a possible mediator of biological action. Nevertheless growth factor receptors possess peculiar specificities both in their functions and tissue distribution. A human polyclonal IgG (pIgG), previously characterized as anti insulin receptor antibody, able to inhibit insulin receptor kinase activity, was used to further investigate subunit homologies and differences in antigenicity and functional regulation between IGF I and insulin receptors, IGF I receptor tyrosine kinase was stimulated by a IGF I analog (aIGF I), produced by DNA recombinant technology, pIgG was able to inhibit IGF I receptor kinase activity, thus revealing antigenic homologies between the kinase domains of insulin and IGF I receptors. However the more pronounced inhibition of IGF I receptor-compared with insulin receptor kinase activity by pIgG suggests the existence of different regulatory mechanisms. |
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