Phosphorylation of the 24p3 protein secreted from mouse uterus in vitro and in vivo |
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Authors: | Lee Y C Lin S D Yu H M Chen S T Chu S T |
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Affiliation: | (1) Academia Sinica, Institute of Biological Chemistry, Taiwan;(2) Institute of Biochemical Science, College of Science, National Taiwan University, Taipei, 10617, Taiwan |
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Abstract: | The 24p3 protein is a 25 KDa glycoprotein, having been purified from mouse uterine fluid. Thr54, Ser88, and Thr128/Ser129 on the protein molecule were predicted to be the phosphorylation site of casein kinase II, protein kinase C, and cAMP-dependent protein kinase, respectively. Incorporation of phosphate to this protein from [-32P]-ATP was tested in the solution suitable for the three kinases. Neither casein kinase II nor cAMP-dependent protein kinase reacted to the 24p3 protein; however, protein kinase C demonstrated phosphorylation to this protein. This phosphorylation may be competing with a polypeptide segment: Arg79-Tyr-Trp-Ilu-Arg-Thr-Phe-Val-Pro-Ser88-Ser-Arg-Ala-Gly-Gln-Phe-Thr-Leu-Gly97 in the 24p3 protein molecule. To support this theory, Ser88 is a phosphorylation site of protein kinase C on 24p3 protein. The enzyme kinetic parameter, based on the Michaelis-Menten equation, determined Km to be 2.96 M in the phosphorylation of 24p3 protein by the kinase. Both of the phosphorylated and dephosphorylated form of 24p3 protein can enhance the cAMP-dependent protein kinase activity in vitro. In addition, this experiment will show for the first time that serine-phosphorylated 24p3 protein exists in mouse uterine tissue. |
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Keywords: | Phosphorylation protein kinase serinephosphate uterine protein |
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