darrenG10
Well-known member
Tresiba degludec
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Finally, it is important to note that IDeg is a full agonist of the insulin receptor and maintains the metabolic responses of human insulin. IDeg has a low affinity for the human insulin-like growth factor-1 receptor (IGF-1 receptor), comparable with that of human insulin.4 In order to investigate metabolic responses and molecular safety Nishimura et al. performed binding studies using recombinant human insulin receptors and human IGF-1 receptors. The affinity of IDeg for human insulin receptor isoforms was found to be similar while the affinity for the human IGF-1 receptor was lower. In particular, IGF-1 receptor binding relative to insulin receptor binding was low (<1 % relative to human insulin) as well as was the mitogenic/metabolic potency ratio (<1 % relative to human insulin).
lantus gargine
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To investigate whether human insulin (HI) and insulin analogues differ in their ability to activate the human IGF-I receptor (IGF-IR), the human insulin receptor A (IR-A) and the human insulin receptor B (IR-B) in vitro. HI, short-acting insulin analogues (insulin aspart; insulin lispro) and long-acting insulin analogues (insulin glargine; insulin detemir) were compared by using kinase receptor activation (KIRA) bioassays specific for IGF-IR, IR-A or IR-B, respectively. These assays quantify ligand activity by measuring receptor auto-phosphorylation upon ligand binding. HI and insulin analogues were tested in a range from 0.1 to 100 nM. Short-acting analogues: Overall, short-acting insulin analogues did not differ substantially from HI, nor from each other. Insulin lispro was slightly more potent than HI and insulin aspart in activating the IGF-IR, only reaching statistical significance at 100 nM (p<0.01). Long-acting analogues: At <10 nM insulin glargine was as potent as HI in activating the IRs and IGF-IR. At 10-100 nM insulin glargine was significantly more potent than HI in activating the IR-B (p<0.05) and IGF-IR (p<0.001). Insulin glargine was more potent than insulin detemir in activating all three receptors (p<0.001). Insulin detemir was less potent than HI in activating the IRs at 1-10 nM (p<0.01) and IGF-IR at >1 nM (p<0.05). Insulin glargine was more potent in activating the IGF-IR than HI and insulin detemir. Since KIRA bioassays do not mimic the exact in vivo situation, further research is needed to find out whether our data have implications for clinical use of insulin glargine.
from this we can see lantus is the clear winner insulin is powerful because it raises igf-1 10xmore than normal and the second benefit blood sugar control thirdly glycogen synthesis
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Finally, it is important to note that IDeg is a full agonist of the insulin receptor and maintains the metabolic responses of human insulin. IDeg has a low affinity for the human insulin-like growth factor-1 receptor (IGF-1 receptor), comparable with that of human insulin.4 In order to investigate metabolic responses and molecular safety Nishimura et al. performed binding studies using recombinant human insulin receptors and human IGF-1 receptors. The affinity of IDeg for human insulin receptor isoforms was found to be similar while the affinity for the human IGF-1 receptor was lower. In particular, IGF-1 receptor binding relative to insulin receptor binding was low (<1 % relative to human insulin) as well as was the mitogenic/metabolic potency ratio (<1 % relative to human insulin).
lantus gargine
^
To investigate whether human insulin (HI) and insulin analogues differ in their ability to activate the human IGF-I receptor (IGF-IR), the human insulin receptor A (IR-A) and the human insulin receptor B (IR-B) in vitro. HI, short-acting insulin analogues (insulin aspart; insulin lispro) and long-acting insulin analogues (insulin glargine; insulin detemir) were compared by using kinase receptor activation (KIRA) bioassays specific for IGF-IR, IR-A or IR-B, respectively. These assays quantify ligand activity by measuring receptor auto-phosphorylation upon ligand binding. HI and insulin analogues were tested in a range from 0.1 to 100 nM. Short-acting analogues: Overall, short-acting insulin analogues did not differ substantially from HI, nor from each other. Insulin lispro was slightly more potent than HI and insulin aspart in activating the IGF-IR, only reaching statistical significance at 100 nM (p<0.01). Long-acting analogues: At <10 nM insulin glargine was as potent as HI in activating the IRs and IGF-IR. At 10-100 nM insulin glargine was significantly more potent than HI in activating the IR-B (p<0.05) and IGF-IR (p<0.001). Insulin glargine was more potent than insulin detemir in activating all three receptors (p<0.001). Insulin detemir was less potent than HI in activating the IRs at 1-10 nM (p<0.01) and IGF-IR at >1 nM (p<0.05). Insulin glargine was more potent in activating the IGF-IR than HI and insulin detemir. Since KIRA bioassays do not mimic the exact in vivo situation, further research is needed to find out whether our data have implications for clinical use of insulin glargine.
from this we can see lantus is the clear winner insulin is powerful because it raises igf-1 10xmore than normal and the second benefit blood sugar control thirdly glycogen synthesis