Prostate-specific membrane antigen (PSMA): current benefits and future value

Semin Surg Oncol. 2000 Jan-Feb;18(1):10-6. doi: 10.1002/(sici)1098-2388(200001/02)18:1<10::aid-ssu3>3.0.co;2-v.

Abstract

We will review the evolution, benefits, and limitations of PSMA testing in the past, as well as its current and future value. Prostate cancer has been the most frequently diagnosed cancer and the second leading cause of cancer death in men in the United States. It has a wide spectrum of biological behavior between latent (indolent) and progressive (aggressive). Further identification of prostate-specific membrane antigen (PSMA) as a prognostic proliferation marker may enhance our understanding of the types of prostate cancer. A review of PSMA testing in the past as well as currently was conducted. Studies were reviewed that deal with detection of PSMA in serum and seminal fluid, reverse transcriptase-polymerase chain reaction (RT-PCR), immunoscintigraphy, and immunohistochemical assays. PSMA is expressed primarily in benign and cancerous prostatic epithelial cells. It is up-regulated in hormone resistant states, and in metastatic situations or other clinical situations where there is tumor recurrence or extension. Based on current results, PSMA detected in the serum by western blotting can assist in the identification, staging, and monitoring of metastatic prostate cancer. In addition, PSMA shows a promising role in directed imaging and therapy of recurrent or metastatic disease.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Antigens, Surface*
  • Blotting, Western
  • Carboxypeptidases / blood*
  • Glutamate Carboxypeptidase II
  • Humans
  • Immunohistochemistry
  • Male
  • Neoplasm Metastasis
  • Neoplasm Staging / methods
  • Prostatic Neoplasms / diagnosis
  • Prostatic Neoplasms / pathology*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sensitivity and Specificity

Substances

  • Antigens, Surface
  • Carboxypeptidases
  • FOLH1 protein, human
  • Glutamate Carboxypeptidase II