Insulin like Growth Factor 1 Receptor IGF 1R - Biotech, Pharma and Life Science Channel
Although the insulin-like growth factor-1 receptor (IGF-1R) was first cloned in 1986, it was the success of targeted drugs such as trastuzumab and imatinib that tyrosine kinase inhibitors and growth factor receptor blockers became hot targets. Now companies are aggressively pursuing compounds that target IGF-1R. Other reasons for the long delay in bringing compounds against IGF-1R into the clinic may be:
- the fear that blocking IGF-1R in cancer therapy would also block the insulin receptor and signaling (70 % homology with IGF-1R) and, thus might be diabetogenic;
- the expression of IGF-1R in normal tissue throughout the body. As of July 2009, the field considerably has widened with seven specific monoclonal antibodies and three specific small molecules against IGF-1R in mid-stage clinical development and further six specific IGF-1R antagonists in preclinical stages.
Safety so far has not been the limiting step in developing IGF-1R antagonist. Combination studies with other anticancer therapies and the emergence of bispecific o rmulti-specific anti-IGF-1R antagonists indicate that efficacy of specific IGF-1R antagonists rather may limit the scope of clinical utility. In fact, the first specific anti-IGF-1R program has been discontinued and next generation molecules evaluate the efficacy spectrum of bispecific molecules, e.g. against EGF-R and IGF-1R, or of molecules with even multikinase specificity including IGF-1R.
Source; Market Research (Competitor Analysis: IGF-1R Antagonists)
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Transferrin-binding Protein A
A subtype of bacterial transferrin-binding protein found in bacteria. It forms a cell surface receptor complex with TRANSFERRIN-BINDING PROTEIN B.
Transferrin-binding Protein B
A subtype of bacterial transferrin-binding protein found in bacteria. It forms a cell surface receptor complex with TRANSFERRIN-BINDING PROTEIN A.
Bacterial Transferrin Receptor Complex
A complex of proteins that forms a receptor for TRANSFERRIN in BACTERIA. Many pathogenic bacteria utilize the transferrin-binding complex to acquire their supply of iron from serum.
Thrombopoiesis
The process of generating thrombocytes (BLOOD PLATELETS) from the pluripotent HEMATOPOIETIC STEM CELLS in the BONE MARROW via the MEGAKARYOCYTES. The humoral factor with thrombopoiesis-stimulating activity is designated THROMBOPOIETIN.
Host Factor 1 Protein
An integration host factor that was originally identified as a bacterial protein required for the integration of bacteriophage Q beta (ALLOLEVIVIRUS). Its cellular function may be to regulate mRNA stability and processing in that it binds tightly to poly(A) RNA and interferes with ribosome binding.
