CIDeRplusGeneral Information:
| Id: | 8,967 |
| Diseases: |
Diabetes mellitus, type II
- [OMIM]
Insulin resistance |
| Mammalia | |
| review | |
| Reference: | Cieslak M and Roszek K(2014) Purinergic signaling in the pancreas and the therapeutic potential of ecto-nucleotidases in diabetes Acta Biochim. Pol. 61: 655-662 [PMID: 25522227] |
Interaction Information:
| Comment | In human and animal cells of the pancreas and blood vessels activity of ecto-enzymes such as NTPDase1, NTPDase2, NTPDase3, 5’- nucleotidase and alkaline phosphatase was demonstrated. |
|
Formal Description Interaction-ID: 93688 |
|
| Comment | In human and animal cells of the pancreas and blood vessels activity of ecto-enzymes such as NTPDase1, NTPDase2, NTPDase3, 5’- nucleotidase and alkaline phosphatase was demonstrated. |
|
Formal Description Interaction-ID: 93858 |
|
| Comment | In human and animal cells of the pancreas and blood vessels activity of ecto-enzymes such as NTPDase1, NTPDase2, NTPDase3, 5’- nucleotidase and alkaline phosphatase was demonstrated. |
|
Formal Description Interaction-ID: 93859 |
|
| Comment | In human and animal cells of the pancreas and blood vessels activity of ecto-enzymes such as NTPDase1, NTPDase2, NTPDase3, 5’- nucleotidase and alkaline phosphatase was demonstrated. |
|
Formal Description Interaction-ID: 93860 |
|
| Drugbank entries | Show/Hide entries for NT5E |
| Comment | In 1963, it was reported that ATP causes an increase in the insulin secretion by the beta-cells of rabbit pancreas. Now it is known that it is effected through the activation of P2Y and P2X receptors present on pancreatic beta-cells, and that the effect triggered by ATP is dependent on blood glucose concentration. |
|
Formal Description Interaction-ID: 93861 |
|
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93862 |
complex/PPI Insulin is localized in cellular component insulin secretory granule |
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93863 |
|
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93864 |
|
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93865 |
process insulin granule exocytosis affects_quantity of drug/chemical compound |
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93866 |
|
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93867 |
|
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93868 |
|
| Comment | The granules inside the pancreatic cells contain not only insulin but also ATP and ADP - their release is regulated by the activation of P2X2 receptor present on the beta-cells. Moreover, other molecules as 5-hydroxytryptamine, gamma-aminobutyric acid, glutamate and zinc are released together with ATP and may affect the autocrine secretion of insulin. |
|
Formal Description Interaction-ID: 93869 |
|
| Comment | ATP released together with insulin from beta-cell granules in response to a rapid decrease in blood glucose levels activates P2X3 receptor, that results in the increase of intracellular Ca2+ concentration, and further amplification of insulin release. |
|
Formal Description Interaction-ID: 93870 |
|
| Comment | ATP released together with insulin from beta-cell granules in response to a rapid decrease in blood glucose levels activates P2X3 receptor, that results in the increase of intracellular Ca2+ concentration, and further amplification of insulin release. |
|
Formal Description Interaction-ID: 93871 |
|
| Comment | ATP released together with insulin from beta-cell granules in response to a rapid decrease in blood glucose levels activates P2X3 receptor, that results in the increase of intracellular Ca2+ concentration, and further amplification of insulin release. |
|
Formal Description Interaction-ID: 93872 |
|
| Comment | P2Y4 receptor activation stimulates insulin secretion independently of blood glucose level. |
|
Formal Description Interaction-ID: 93873 |
|
| Comment | P2Y1 and P2Y6 receptor activation inhibits insulin secretion despite high concentration of glucose in blood. Another study on the same receptors showed that the activation of P2Y1 and P2Y6 receptors stimulates insulin secretion when the glucose concentration raises over 8 mM. |
|
Formal Description Interaction-ID: 93874 |
|
| Comment | P2Y1 and P2Y6 receptor activation inhibits insulin secretion despite high concentration of glucose in blood. Another study on the same receptors showed that the activation of P2Y1 and P2Y6 receptors stimulates insulin secretion when the glucose concentration raises over 8 mM. |
|
Formal Description Interaction-ID: 93875 |
|
| Comment | Uridine diphosphate (UDP) stimulates insulin secretion through P2Y6 receptor activation. |
|
Formal Description Interaction-ID: 93876 |
|
| Drugbank entries | Show/Hide entries for UDP |
| Comment | Uridine diphosphate (UDP) stimulates insulin secretion through P2Y6 receptor activation. |
|
Formal Description Interaction-ID: 93877 |
|
| Drugbank entries | Show/Hide entries for UDP |
| Comment | ATP stimulates secretion of glucagon and insulin and this process is dependent on the blood glucose level. |
|
Formal Description Interaction-ID: 93878 |
|
| Comment | Adenosine activates four subtypes (A1, A2A, A2B and A3) of G protein-dependent receptors. The presence of adenosine receptor A1 and A2B was demonstrated on pancreatic beta-cells. |
|
Formal Description Interaction-ID: 93879 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Adenosine activates four subtypes (A1, A2A, A2B and A3) of G protein-dependent receptors. The presence of adenosine receptor A1 and A2B was demonstrated on pancreatic beta-cells. |
|
Formal Description Interaction-ID: 93880 |
|
| Drugbank entries | Show/Hide entries for ADORA2B |
| Comment | Increased expression of A1R was shown in pathological states such as oxidative stress, ischemia, inflammation and diabetes. |
|
Formal Description Interaction-ID: 93881 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Increased expression of A1R was shown in pathological states such as oxidative stress, ischemia, inflammation and diabetes. |
|
Formal Description Interaction-ID: 93882 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Increased expression of A1R was shown in pathological states such as oxidative stress, ischemia, inflammation and diabetes. |
|
Formal Description Interaction-ID: 93883 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Adenosine inhibits the release of insulin, while, together with ADP and AMP stimulates glucagon secretion. |
|
Formal Description Interaction-ID: 93884 |
|
| Drugbank entries | Show/Hide entries for Adenosine |
| Comment | Adenosine inhibits the release of insulin, while, together with ADP and AMP stimulates glucagon secretion. |
|
Formal Description Interaction-ID: 93885 |
|
| Drugbank entries | Show/Hide entries for Adenosine |
| Comment | Adenosine inhibits the release of insulin, while, together with ADP and AMP stimulates glucagon secretion. |
|
Formal Description Interaction-ID: 93886 |
|
| Comment | Adenosine inhibits the release of insulin, while, together with ADP and AMP stimulates glucagon secretion. |
|
Formal Description Interaction-ID: 93887 |
|
| Comment | Adenosine A1 receptor activation inhibits lipolysis and thus controls various pathological processes in which free fatty acids play a key role such as diabetes, insulin resistance and dyslipidemia. |
|
Formal Description Interaction-ID: 93888 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Activation of A1 receptors on adipocytes inhibits activity of adenylate cyclase, thus reduces the concentration of cAMP as well as inhibits activity of protein kinase A, and thereby impairs lipolysis. |
|
Formal Description Interaction-ID: 93889 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Activation of A1 receptors on adipocytes inhibits activity of adenylate cyclase, thus reduces the concentration of cAMP as well as inhibits activity of protein kinase A, and thereby impairs lipolysis. |
|
Formal Description Interaction-ID: 93950 |
|
| Drugbank entries | Show/Hide entries for ADORA1 or cAMP |
| Comment | Activation of A1 receptors on adipocytes inhibits activity of adenylate cyclase, thus reduces the concentration of cAMP as well as inhibits activity of protein kinase A, and thereby impairs lipolysis. |
|
Formal Description Interaction-ID: 93951 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Activation of A1 receptors on adipocytes inhibits activity of adenylate cyclase, thus reduces the concentration of cAMP as well as inhibits activity of protein kinase A, and thereby impairs lipolysis. |
|
Formal Description Interaction-ID: 93952 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Adenosine and adenosine analogues inhibit adenylate cyclase acting antagonistically to catecholamines, that raise cAMP concentration and therefore induce lipolysis in adipocytes. |
|
Formal Description Interaction-ID: 93957 |
|
| Drugbank entries | Show/Hide entries for Adenosine |
| Comment | Adenosine and adenosine analogues inhibit adenylate cyclase acting antagonistically to catecholamines, that raise cAMP concentration and therefore induce lipolysis in adipocytes. |
|
Formal Description Interaction-ID: 93959 |
|
| Comment | Adenosine and adenosine analogues inhibit adenylate cyclase acting antagonistically to catecholamines, that raise cAMP concentration and therefore induce lipolysis in adipocytes. |
|
Formal Description Interaction-ID: 93960 |
|
| Comment | Adenosine and adenosine analogues inhibit adenylate cyclase acting antagonistically to catecholamines, that raise cAMP concentration and therefore induce lipolysis in adipocytes. |
|
Formal Description Interaction-ID: 93961 |
|
| Drugbank entries | Show/Hide entries for Adenosine |
| Comment | In rats adenosine and some of its metabolites inhibit the conversion of triglycerides (TG) to free fatty acids (FFA). It was confirmed by studies of Schwabe and colleagues, in which adenosine deaminase added to the culture of fat cells stimulated lipolysis. |
|
Formal Description Interaction-ID: 93962 |
|
| Drugbank entries | Show/Hide entries for Adenosine |
| Comment | In rats adenosine and some of its metabolites inhibit the conversion of triglycerides (TG) to free fatty acids (FFA). It was confirmed by studies of Schwabe and colleagues, in which adenosine deaminase added to the culture of fat cells stimulated lipolysis. |
|
Formal Description Interaction-ID: 93966 |
|
| Comment | Adipose tissue produces proinflammatory agents such as interleukin-6 (IL-6), C-reactive protein (CRP) and plasminogen activator inhibitor 1 (PAI-1), which increase tissue resistance to insulin. Adenosine through activation of A2B receptors contributes to increased insulin resistance by stimulating production of IL-6 and other cytokines. Animal studies confirmed that the A2B receptor activation causes an increase in IL-6 concentrations in serum. |
|
Formal Description Interaction-ID: 93975 |
|
| Drugbank entries | Show/Hide entries for Adenosine or ADORA2B |
| Comment | Adipose tissue produces proinflammatory agents such as interleukin-6 (IL-6), C-reactive protein (CRP) and plasminogen activator inhibitor 1 (PAI-1), which increase tissue resistance to insulin. Adenosine through activation of A2B receptors contributes to increased insulin resistance by stimulating production of IL-6 and other cytokines. Animal studies confirmed that the A2B receptor activation causes an increase in IL-6 concentrations in serum. |
|
Formal Description Interaction-ID: 93983 |
|
| Drugbank entries | Show/Hide entries for ADORA2B or IL6 |
| Comment | Adipose tissue produces proinflammatory agents such as interleukin-6 (IL-6), C-reactive protein (CRP) and plasminogen activator inhibitor 1 (PAI-1), which increase tissue resistance to insulin. Adenosine through activation of A2B receptors contributes to increased insulin resistance by stimulating production of IL-6 and other cytokines. Animal studies confirmed that the A2B receptor activation causes an increase in IL-6 concentrations in serum. |
|
Formal Description Interaction-ID: 93984 |
|
| Drugbank entries | Show/Hide entries for IL6 |
| Comment | Adenosine in the extracellular space affects the transport of glucose into the cells of skeletal muscles, while in the cardiac muscle cells and adipocytes increases insulin-stimulated glucose transport into the cells. The conversion of adenosine to inosine by adenosine deaminase or blocking the action of adenosine with adenosine receptor antagonists (CPDPX, 8-cyclopentyl-1,3-dipropylxanthine) impairs the insulin-stimulated glucose transport in skeletal muscles. This effect could be due to either a decrease in the number of glucose transporters GLUT4 on the surface of cells or to the reduction of their efficiency. Reducing the number of glucose transporters on the cell surface is also responsible for the reduction in the effectiveness of insulin in glucose transport into skeletal muscle cells and adipocytes, which contributes to the development of insulin resistance. Results obtained by Han and colleagues indicate that adenosine influences the muscle contraction-stimulated and/or insulin-stimulated glucose transport. |
|
Formal Description Interaction-ID: 93985 |
|
| Drugbank entries | Show/Hide entries for Adenosine |
| Comment | Numerous studies have demonstrated the activity of enzymes involved in the metabolism of ecto-nucleotides on pancreatic islet cells, alveolar and duct cells as well as blood vessels. Ecto-NTPDases (ectonucleoside triphosphate diphosphohydrolases) present on the surface of these cells play an essential role in the metabolism of ecto-nucleotides. Four ecto-NTPDases with different biological properties and localization were cloned so far: NTPDase1 (apyrase/CD39), NTPDase2, NTPDase3 and NTPDase8. In humans, the activity of NTPDase1 was found on alveolar cells (acinar cells) and blood vessels and capillaries within the pancreatic islets. Activity of NTPDase2 was found on alveolar cells, on cells surrounding the pancreatic islets and capillaries. NTPDase3 activity has been demonstrated only on Langerhans cells of the pancreas. Furthermore, high NTPDase activity has been demonstrated on platelets of patients with type 2 diabetes. There was no 5’-nucleotidase activity on the pancreatic islets cells, however the activity has been demonstrated in the capillaries of the Langerhans islets. NTPDase1 hydrolyses both ATP and ADP, NTPDase2 hydrolyses mainly ADP and NTPDase3 activity has an intermediate hydrolysis profile. The final product of ATP and ADP hydrolysis is AMP, that is converted to adenosine with the participation of 5’-nucleotidase. |
|
Formal Description Interaction-ID: 93988 |
|
| Comment | Numerous studies have demonstrated the activity of enzymes involved in the metabolism of ecto-nucleotides on pancreatic islet cells, alveolar and duct cells as well as blood vessels. Ecto-NTPDases (ectonucleoside triphosphate diphosphohydrolases) present on the surface of these cells play an essential role in the metabolism of ecto-nucleotides. Four ecto-NTPDases with different biological properties and localization were cloned so far: NTPDase1 (apyrase/CD39), NTPDase2, NTPDase3 and NTPDase8. In humans, the activity of NTPDase1 was found on alveolar cells (acinar cells) and blood vessels and capillaries within the pancreatic islets. Activity of NTPDase2 was found on alveolar cells, on cells surrounding the pancreatic islets and capillaries. NTPDase3 activity has been demonstrated only on Langerhans cells of the pancreas. Furthermore, high NTPDase activity has been demonstrated on platelets of patients with type 2 diabetes. There was no 5’-nucleotidase activity on the pancreatic islets cells, however the activity has been demonstrated in the capillaries of the Langerhans islets. NTPDase1 hydrolyses both ATP and ADP, NTPDase2 hydrolyses mainly ADP and NTPDase3 activity has an intermediate hydrolysis profile. The final product of ATP and ADP hydrolysis is AMP, that is converted to adenosine with the participation of 5’-nucleotidase. |
|
Formal Description Interaction-ID: 93996 |
|
| Comment | Numerous studies have demonstrated the activity of enzymes involved in the metabolism of ecto-nucleotides on pancreatic islet cells, alveolar and duct cells as well as blood vessels. Ecto-NTPDases (ectonucleoside triphosphate diphosphohydrolases) present on the surface of these cells play an essential role in the metabolism of ecto-nucleotides. Four ecto-NTPDases with different biological properties and localization were cloned so far: NTPDase1 (apyrase/CD39), NTPDase2, NTPDase3 and NTPDase8. In humans, the activity of NTPDase1 was found on alveolar cells (acinar cells) and blood vessels and capillaries within the pancreatic islets. Activity of NTPDase2 was found on alveolar cells, on cells surrounding the pancreatic islets and capillaries. NTPDase3 activity has been demonstrated only on Langerhans cells of the pancreas. Furthermore, high NTPDase activity has been demonstrated on platelets of patients with type 2 diabetes. There was no 5’-nucleotidase activity on the pancreatic islets cells, however the activity has been demonstrated in the capillaries of the Langerhans islets. NTPDase1 hydrolyses both ATP and ADP, NTPDase2 hydrolyses mainly ADP and NTPDase3 activity has an intermediate hydrolysis profile. The final product of ATP and ADP hydrolysis is AMP, that is converted to adenosine with the participation of 5’-nucleotidase. |
|
Formal Description Interaction-ID: 93999 |
|
| Comment | Numerous studies have demonstrated the activity of enzymes involved in the metabolism of ecto-nucleotides on pancreatic islet cells, alveolar and duct cells as well as blood vessels. Ecto-NTPDases (ectonucleoside triphosphate diphosphohydrolases) present on the surface of these cells play an essential role in the metabolism of ecto-nucleotides. Four ecto-NTPDases with different biological properties and localization were cloned so far: NTPDase1 (apyrase/CD39), NTPDase2, NTPDase3 and NTPDase8. In humans, the activity of NTPDase1 was found on alveolar cells (acinar cells) and blood vessels and capillaries within the pancreatic islets. Activity of NTPDase2 was found on alveolar cells, on cells surrounding the pancreatic islets and capillaries. NTPDase3 activity has been demonstrated only on Langerhans cells of the pancreas. Furthermore, high NTPDase activity has been demonstrated on platelets of patients with type 2 diabetes. There was no 5’-nucleotidase activity on the pancreatic islets cells, however the activity has been demonstrated in the capillaries of the Langerhans islets. NTPDase1 hydrolyses both ATP and ADP, NTPDase2 hydrolyses mainly ADP and NTPDase3 activity has an intermediate hydrolysis profile. The final product of ATP and ADP hydrolysis is AMP, that is converted to adenosine with the participation of 5’-nucleotidase. |
|
Formal Description Interaction-ID: 94001 |
|
| Comment | Numerous studies have demonstrated the activity of enzymes involved in the metabolism of ecto-nucleotides on pancreatic islet cells, alveolar and duct cells as well as blood vessels. Ecto-NTPDases (ectonucleoside triphosphate diphosphohydrolases) present on the surface of these cells play an essential role in the metabolism of ecto-nucleotides. Four ecto-NTPDases with different biological properties and localization were cloned so far: NTPDase1 (apyrase/CD39), NTPDase2, NTPDase3 and NTPDase8. In humans, the activity of NTPDase1 was found on alveolar cells (acinar cells) and blood vessels and capillaries within the pancreatic islets. Activity of NTPDase2 was found on alveolar cells, on cells surrounding the pancreatic islets and capillaries. NTPDase3 activity has been demonstrated only on Langerhans cells of the pancreas. Furthermore, high NTPDase activity has been demonstrated on platelets of patients with type 2 diabetes. There was no 5’-nucleotidase activity on the pancreatic islets cells, however the activity has been demonstrated in the capillaries of the Langerhans islets. NTPDase1 hydrolyses both ATP and ADP, NTPDase2 hydrolyses mainly ADP and NTPDase3 activity has an intermediate hydrolysis profile. The final product of ATP and ADP hydrolysis is AMP, that is converted to adenosine with the participation of 5’-nucleotidase. |
|
Formal Description Interaction-ID: 94002 |
|
| Comment | Numerous studies have demonstrated the activity of enzymes involved in the metabolism of ecto-nucleotides on pancreatic islet cells, alveolar and duct cells as well as blood vessels. Ecto-NTPDases (ectonucleoside triphosphate diphosphohydrolases) present on the surface of these cells play an essential role in the metabolism of ecto-nucleotides. Four ecto-NTPDases with different biological properties and localization were cloned so far: NTPDase1 (apyrase/CD39), NTPDase2, NTPDase3 and NTPDase8. In humans, the activity of NTPDase1 was found on alveolar cells (acinar cells) and blood vessels and capillaries within the pancreatic islets. Activity of NTPDase2 was found on alveolar cells, on cells surrounding the pancreatic islets and capillaries. NTPDase3 activity has been demonstrated only on Langerhans cells of the pancreas. Furthermore, high NTPDase activity has been demonstrated on platelets of patients with type 2 diabetes. There was no 5’-nucleotidase activity on the pancreatic islets cells, however the activity has been demonstrated in the capillaries of the Langerhans islets. NTPDase1 hydrolyses both ATP and ADP, NTPDase2 hydrolyses mainly ADP and NTPDase3 activity has an intermediate hydrolysis profile. The final product of ATP and ADP hydrolysis is AMP, that is converted to adenosine with the participation of 5’-nucleotidase. |
|
Formal Description Interaction-ID: 94003 |
|
| Comment | Participation of NTPDase1 (apyrase) in insulin secretion was experimentally confirmed by the results of studies, in which administration of the apyrase inhibitor ARL67156 caused an increase in insulin secretion. NTPDase1 impairs insulin secretion both by hydrolysis of extracellular ATP and ADP as by providing AMP as a substrate for 5'-nucleotidase. Thus, NTPDase1 participates in the formation of adenosine. Adenosine-mediated activation of P1 receptors probably slightly inhibits the secretion of insulin. It can be assumed that a significant reduction in the activity of ecto-5’-nucleotidase should result in decreasing the concentration of adenosine outside the cell, which can affect the secretion of insulin. |
|
Formal Description Interaction-ID: 94004 |
|
| Comment | Basic micromolar concentrations of adenosine in isolated pancreatic islets are sufficient to stimulate the secretion of glucagon and to inhibit insulin secretion by the activation of A1 receptor. |
|
Formal Description Interaction-ID: 94005 |
|
| Drugbank entries | Show/Hide entries for Adenosine or ADORA1 |
| Comment | Basic micromolar concentrations of adenosine in isolated pancreatic islets are sufficient to stimulate the secretion of glucagon and to inhibit insulin secretion by the activation of A1 receptor. |
|
Formal Description Interaction-ID: 94006 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Basic micromolar concentrations of adenosine in isolated pancreatic islets are sufficient to stimulate the secretion of glucagon and to inhibit insulin secretion by the activation of A1 receptor. |
|
Formal Description Interaction-ID: 94007 |
|
| Drugbank entries | Show/Hide entries for ADORA1 |
| Comment | Diabetes includes the metabolic disorders not only of the pancreas, but also other organs and tissues such as liver, skeletal muscles and adipose tissue. The key pathophysiological disorder is abnormal metabolism and glucose transport ssociated with inadequate secretion of insulin. This leads to an increase in blood glucose level, the formation of free fatty acids and the release of pro-inflammatory cytokines. In type 2 diabetes these processes lead to the phenomenon of insulin resistance, which is mainly responsible for the progression of the disease. Purinergic signaling plays a key role in the above processes. Purinergic receptors P1 and P2 are present on the pancreatic islet cells as well as on hepatocytes, adipocytes, in the circulatory system and pancreatic nerves. |
|
Formal Description Interaction-ID: 94009 |
affects_activity of disease |
| Comment | P2X3 receptor is of particular importance in human beta-cells. The P2X3R activation results in a positive autocrine signal and its subsequent amplification. Insulin secretion increases as a consequence of the process. ATP participates in this autocrine feedback loop associated with the secretion of insulin. ATP is released together with insulin from beta-cell granules in response to the rapid increase in blood glucose concentration. ATP in the extracellular environment, through the P2X3 receptor activation initiates the increase in intracellular calcium ions concentration, and thus amplifies the release of insulin. |
|
Formal Description Interaction-ID: 94012 |
|
| Comment | P2X3 receptor is of particular importance in human beta-cells. The P2X3R activation results in a positive autocrine signal and its subsequent amplification. Insulin secretion increases as a consequence of the process. ATP participates in this autocrine feedback loop associated with the secretion of insulin. ATP is released together with insulin from beta-cell granules in response to the rapid increase in blood glucose concentration. ATP in the extracellular environment, through the P2X3 receptor activation initiates the increase in intracellular calcium ions concentration, and thus amplifies the release of insulin. |
|
Formal Description Interaction-ID: 94013 |
|