IGF1: Difference between revisions
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<Structure load='1gzr' size='400' frame='true' align='right' caption='IGF-1 structural basis | <Structure load='1gzr' size='400' frame='true' align='right' caption='IGF-1 structural basis (PDB code [[1gzr]])' scene='75/751772/Igf-1/2'/> | ||
'''Insulin-like Growth Factor''' ('''IGF-1''') is a member of the insulin protein family. '''Insulin''' is an essential endocrine protein. Indeed, it is the only hypoglycemic hormone of the human body. This protein is secreted in the beta cells of the Langerhans’ islet in the pancreas and takes part in the glycogenesis. This molecule helps the transportation of glucose into the cells, thus reducing the blood sugar rate, contrary to glucagon. | '''Insulin-like Growth Factor''' ('''IGF-1''') is a member of the insulin protein family. '''Insulin''' is an essential endocrine protein. Indeed, it is the only hypoglycemic hormone of the human body. This protein is secreted in the beta cells of the Langerhans’ islet in the pancreas and takes part in the glycogenesis. This molecule helps the transportation of glucose into the cells, thus reducing the blood sugar rate, contrary to glucagon. | ||
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IGF-1 is a peptidic hormone of 69 amino acids which is secreted by the liver. | IGF-1 is a peptidic hormone of 69 amino acids which is secreted by the liver. | ||
This protein deals with a large scale of regulations, from growth to nutrition and it is even implied in stress response, breeding and longevity.<ref>Patrick Jouandin. Rôle de la voie de signalisation Insuline dans le couplage des informations nutritionnelles et développementales au cours de l'ovogenèse chez la drosophile. Sciences agricoles.Université Nice Sophia Antipolis, 2013. Français.<NNT : 2013NICE4102>.<tel-00932409></ref>. | This protein deals with a large scale of regulations, from growth to nutrition and it is even implied in stress response, breeding and longevity.<ref>Patrick Jouandin. Rôle de la voie de signalisation Insuline dans le couplage des informations nutritionnelles et développementales au cours de l'ovogenèse chez la drosophile. Sciences agricoles.Université Nice Sophia Antipolis, 2013. Français.<NNT : 2013NICE4102>.<tel-00932409></ref>. | ||
It is the main actor in primary growth cell control. | It is the main actor in primary growth cell control. | ||
See also: | |||
*[[Insulin-like growth factor]] | |||
*[[Insulin-like growth factor receptor]] | |||
== History == | == History == | ||
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<Structure load='4xss' size='250' frame='true' align='right' caption='IGF-1/IGF-1R Complex' /> | <Structure load='4xss' size='250' frame='true' align='right' caption='IGF-1/IGF-1R Complex' scene='75/751772/Igf1r/1'/> | ||
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=== Stimulating interaction : IGF-1 - IGF-1R === | === Stimulating interaction : IGF-1 - IGF-1R === | ||
'''Insulin-like Growth Factor 1 Receptor''' ('''IGF-1R''') is a transmembrane protein receptor. It is composed of two α subunits and two tyrosine β subunits. Both α subunits are '' | '''Insulin-like Growth Factor 1 Receptor''' ('''IGF-1R''') is a transmembrane protein receptor. It is composed of two α subunits and two tyrosine β subunits. Both α subunits are <scene name='75/751772/Igf1r/2'>cystein-rich region</scene> and therefore linked with a '''disulfide bond'''. Ligand-binding on α subunit induces activation of β subunit by autophosphorylation. It further leads to activation of the Akt and mTor pathways inside the cell. <ref>http://www.exobiologie.info/diabete/10%20recepteur.pdf, 27/01/2016</ref> | ||
[[Image:Interactions_IGF_refait.PNG | 300 px |left]] | [[Image:Interactions_IGF_refait.PNG | 300 px |left]] | ||
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Therefore, the various concentration of the insulin proteins regulates the cell activity in different context, for instance in excess of glucose or lack of Growth Hormone. | Therefore, the various concentration of the insulin proteins regulates the cell activity in different context, for instance in excess of glucose or lack of Growth Hormone. | ||
Recent research demonstrated that the homology between IGF-1R and the '''insulin receptor''' (IR) subunits allow them to bind and form a functionnal hybrid IR/IGF-1R receptor. | Recent research demonstrated that the homology between IGF-1R and the '''insulin receptor''' (IR) subunits allow them to bind and form a functionnal hybrid IR/IGF-1R receptor. The exact residues interacting with one another are not known accuraretly but the docking mechanism is the same as for IGFBP. | ||