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Protection of prostatic acid phosphatase activity in human serum samples by plasmin inhibitors
Abdul Waheed1, Robert L Van Etten
1Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, 1402 S. Grand Boulevard, St. Louis, MO 63104, USA.
Background:
The level of prostatic acid phosphatase in serum is an established marker for prostate carcinoma.
Methods:
Inactivation of homogeneous prostatic acid phosphatase from human seminal fluid by purified plasmin and human serum was studied in the presence and absence of bovine pancreatic trypsin inhibitor, a plasmin inhibitor, or phenylmethylsulfonylfluoride, a serine protease inhibitor.
Results:
Plasmin or serine protease inhibitors protect against prostatic acid phosphatase inactivation in serum samples.
Conclusion:
The immediate addition of serine protease inhibitors to serum samples taken for prostatic acid phosphatase determinations should provide more accurate results and permit extended storage of samples. The stabilization of the enzyme activity and immunological properties of prostatic acid phosphatase in blood samples by these protease inhibitors resurrects the clinical significance of prostatic acid phosphatase measurements in prostate cancer screenings.