G6B
Added more to the second paragraph of the function that speaks on the inhibitory function.
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The function of G6b is for it to be a cell-surface receptor that has inhibitory function that operates in a calcium-independent way. With this G6b has been seen to have a novel inhibitory receptor as well taht is found on the surface of platelets. G6b's function has a crucial connection to the identification of the extracellular ligand, as the protein ligands for the Ig superfamily members are typically, but not every time, other Ig superfamily members.{{Cite journal |last=de Vet |first=Edwin C. J. M. |last2=Newland |first2=Stephen A. B. |last3=Lyons |first3=Paul A. |last4=Aguado |first4=Begoña |last5=Campbell |first5=R. Duncan |date=2005-04-25 |title=The cell surface receptor G6b, a member of the immunoglobulin superfamily, binds heparin |url=https://www.sciencedirect.com/science/article/pii/S0014579305003728 |journal=FEBS Letters |volume=579 |issue=11 |pages=2355–2358 |doi=10.1016/j.febslet.2005.03.032 |issn=0014-5793}} Interactions between the Ig superfamily members and the ligands connected to them, typically have a low affinity, which makes the identifications of ligands in experiments challenging. At the moment the G6b Ig domain is shown to not contain any significant homology towards any other Ig domain that contain proteins with a known ligand. The extracellular domain of the G6b protein shows that there is evidence that the binding to heparin is mainly electrostatic. However, the protein ligand of the extracellular part of the G6b has not been identified yet, there is a possibility that the binding of heparin plays an essential role in the G6b biological function. |
The function of G6b is for it to be a cell-surface receptor that has inhibitory function that operates in a calcium-independent way. With this G6b has been seen to have a novel inhibitory receptor as well taht is found on the surface of platelets. G6b's function has a crucial connection to the identification of the extracellular ligand, as the protein ligands for the Ig superfamily members are typically, but not every time, other Ig superfamily members.{{Cite journal |last=de Vet |first=Edwin C. J. M. |last2=Newland |first2=Stephen A. B. |last3=Lyons |first3=Paul A. |last4=Aguado |first4=Begoña |last5=Campbell |first5=R. Duncan |date=2005-04-25 |title=The cell surface receptor G6b, a member of the immunoglobulin superfamily, binds heparin |url=https://www.sciencedirect.com/science/article/pii/S0014579305003728 |journal=FEBS Letters |volume=579 |issue=11 |pages=2355–2358 |doi=10.1016/j.febslet.2005.03.032 |issn=0014-5793}} Interactions between the Ig superfamily members and the ligands connected to them, typically have a low affinity, which makes the identifications of ligands in experiments challenging. At the moment the G6b Ig domain is shown to not contain any significant homology towards any other Ig domain that contain proteins with a known ligand. The extracellular domain of the G6b protein shows that there is evidence that the binding to heparin is mainly electrostatic. However, the protein ligand of the extracellular part of the G6b has not been identified yet, there is a possibility that the binding of heparin plays an essential role in the G6b biological function. |
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The inhibitory function that is seen is expressed on the surface of the resting platelets with cross-linking G6b which, leads to the inhibitory effect on the platelet aggregation and activation. The platelet aggregation studied with the cross-linking of G6b to determine if signaling through G6b had an effect on the platelet function. |
The inhibitory function that is seen is expressed on the surface of the resting platelets with cross-linking G6b which, leads to the inhibitory effect on the platelet aggregation and activation. The platelet aggregation studied with the cross-linking of G6b to determine if signaling through G6b had an effect on the platelet function. Cross-linking of the G6b before the activation of the platelets with the agonist ADP which led to a significant dose-dependent reduction in the platelet aggregation, leading to the end point aggregation reduced from 100% to 25%. As well the cross-linking of G6b before the activation of CRP-XL that led to a two-fold reduction in the platelet aggregation. |
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==References== |
==References== |
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