Effects of the long-acting insulin analog insulin glargine on cultured human skeletal muscle cells: comparisons to insulin and IGF-I
| Autor: | Sunder Mudaliar, Theodore P. Ciaraldi, Robert R. Henry, Leslie Carter, G. Seipke |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Adult
medicine.medical_specialty Endocrinology Diabetes and Metabolism medicine.medical_treatment Glucose uptake Clinical Biochemistry Insulin analog Insulin Glargine Biology Biochemistry Binding Competitive Receptor IGF Type 1 Endocrinology Reference Values Internal medicine medicine Myocyte Humans Insulin Insulin-Like Growth Factor I Muscle Skeletal Pancreatic hormone Cells Cultured Insulin glargine Biochemistry (medical) Skeletal muscle Metabolism Intracellular Membranes Middle Aged Receptor Insulin Insulin Long-Acting medicine.anatomical_structure Glucose Diabetes Mellitus Type 2 medicine.drug Signal Transduction Thymidine |
| Zdroj: | The Journal of clinical endocrinology and metabolism. 86(12) |
| ISSN: | 0021-972X |
| Popis: | The aim of this study was to determine whether the long-acting insulin analog, insulin glargine, behaves like human insulin for metabolic and mitogenic responses in differentiated cultured human skeletal muscle cells from nondiabetic and diabetic subjects. Human insulin and insulin glargine were equipotent in their ability to compete for [(125)I]insulin binding. Insulin glargine displaced [(125)I]IGF-I from the IGF-I-binding site with approximately 0.5% the potency of IGF-I. In nondiabetic muscle cells, all three ligands stimulated glucose uptake similarly, whereas the sensitivity of glucose uptake was greatest in response to IGF-I and lower and equal for human insulin and insulin glargine. In diabetic muscle cells, the final responsiveness of glucose uptake was greatest for IGF-I and equivalent for human insulin and insulin glargine; sensitivities were the same as those for nondiabetic cells. Thymidine uptake into DNA was stimulated foremost by IGF-I, whereas human insulin and insulin glargine showed equivalent, but greatly reduced, sensitivities and potencies (1% IGF-I). Stimulation of Akt phosphorylation was slightly more responsive to IGF-I compared with human insulin and insulin glargine, with sensitivities similar to glucose uptake stimulation. We conclude that in human skeletal muscle cells, insulin glargine is equivalent to human insulin for metabolic responses and does not display augmented mitogenic effects. |
| Databáze: | OpenAIRE |
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