Binding of prostacyclin by plasma glycoproteins.
The binding of prostacyclin (PGI2) to plasma proteins and the resulting increase in PGI2 stability was investigated. Using gel filtration to separate bound and free PGI2, we have found that Cohn Fraction VI can bind PGI2, and retard its hydrolysis to 6-keto-PGF1 alpha (6KPGF1 alpha). The biological activity of the bound PGI2 correlated well with the quantity of bound PGI2, measured as 6KPGF1 alpha by RIA. Fraction VI bound a greater percentage of PGI2 than the other eicosanoids tested (i.e., PGI2 greater than TXB2 greater than LTB4 greater than PGE1 greater than PGF2 alpha). The PGI2 binding activity of Fraction VI was lost after neuraminidase treatment. Our data suggest that Fraction VI glycoproteins may play an important role in the binding and stabilization of PGI2 by plasma proteins.
D011464:Epoprostenol / Q000097:blood*; D006023:Glycoproteins / Q000097:blood* / Q000302:isolation & purification; D006801:Humans; D066298:In Vitro Techniques; D011453:Prostaglandins / Q000097:blood; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism
D006023:Glycoproteins; D011453:Prostaglandins; D012709:Serum Albumin; D011464:Epoprostenol