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After plateplate activation, the release of plateboard reaction protein (TSP-1) increases, which in turn promotes plate plate plate activation, but its role in hemostation in the body is not clear.
Aburima et al. have found that TSP-1 is an important mediated factor for hemostation and can promote plate plate plate activation by inhibiting camp.
Outside the body, knocking out the TSP-1 gene does not affect platelet activation, but in models of hemostating and thrombosis, TSP-1 defects can prolong bleeding time in mice, leading to thrombosis defects and increased sensitivity to prostaline analogue Ilo prostin.
plateplates in wild type (WT) mice can improve thrombosis thrombosis esoterypes, but TSP-1-type plateplates can't be transplanted, indicating that plate plateboard sourceSP-1 has important functions.
in functional analysis experiments, TSP-1 defective plateplates were more sensitive to cAMP signals and PGI2 to plateplate aggregation and block suppression in blood flow.
plasma replacement experiment showed that plasma TSP-1 could not correct the high sensitivity of PGI2 of TSP-1-/-type plateplates.
Contrary, incubation of TSP-1-/- plate plate plates with the release of WT plate plateboards or purified TSP-1 reduces the inhibition of PGI2, but does not have this effect incubating with releases of TSP-1-/- plate plate plates.
WT plate plate plate activation reduces camp accumulation and downstream signals, which is associated with an increase in the activity of camp hydrolyzed enzyme phosphate 3A (PDE3A).
PDE3A activity and camp accumulation of plateplates in mice with TSP-1-/- were not affected.
plateplates with TSP-1 subject CD36 defects are more sensitive to PGI2/cAMP signals, PDE3A activity is reduced, and is not affected by plateboard sources or purified TSP-1.
results of this study show that the release of TSP-1 regulates hemostage in the body by regulating plateplate cAMP signals at the site of vascular damage.
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