Introduction of S1PR3
Sphingosine 1-phosphate receptor 2 (S1PR3), also known as S1P3 or S1P receptor 3, is encoded by the S1PR3 gene. It belongs to the G-protein-coupled receptor (GPCR) family which has been extensively studied during the past few decades because it offers numerous possibilities for therapeutic applications. S1PR3 is expressed in all tissues, but most abundantly in heart, placenta, kidney, and liver.
|Basic Information of S1PR3|
|Protein Name||Sphingosine 1-phosphate receptor 2|
|Aliases||S1P receptor 3, S1P3, EDG3|
|Organism||Homo sapiens (Human)|
Function of S1PR3 Membrane Protein
S1PR3 is a receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Cell culture and mouse researches revealed that S1PR3 agonists may help treat wound healing. Besides, in human umbilical vein endothelial cells, compared with no treatment, the S1PR1 and S1PR3 agonist Gilenya fingolimod promoted the secretion of proregenerative cytokines. What’s more, a study has reported that phosphorylation of the S1P receptor S1PR3 is improved specifically in response to S1P. Truncation of the receptor's carboxyl-terminal domain suggested that the presence of a serine-rich stretch of residues between Leu332 and Val352 was essential to observe this effect.
Fig.1 A working model for the functions of SphK/S1P/S1PR3 in CSC regulation.
Application of S1PR3 Membrane Protein in Literature
This article indicates that Edg3 and Edg5 mediated the serum response element activation through transcriptional factors Elk-1 and serum response factor. Thus, specific G protein-coupled receptors Edg3 and Edg5 account for, at least in part, S1P-induced cell proliferation, survival, and related signaling events.
This article suggests that SPP-induced I (K.ACh) activation in human atrial myocytes is mediated by the S1PR3 subtype of SPP receptors.
This article represents the first characterization of S1P receptor activity through G proteins directly and establishes fundamental differences in coupling.
This article reveals that S1PR3 function is not subject to conventional regulation by GRK phosphorylation and that novel aspect of S1PR3 function distinct from classical G-protein coupling and receptor internalisation may be controlled its carboxyl-terminal domain.
This article shows that VEGF stimulation requires Gi-protein signaling. They show that the VEGF stimulates the expression of S1PR3 and that expression of this Gi-protein-coupled receptor is both sufficient and necessary for the expression of Akt3.
S1PR3 Preparation Options
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