Calcitonin releases acid phosphatase from rat ventral prostate explants

Life Sci. 1994;54(8):561-5. doi: 10.1016/0024-3205(94)90007-8.

Abstract

Inclusion of salmon calcitonin in the culture medium of rat ventral prostate explants diminished l-tartarate-sensitive acid phosphatase activity in the tissues with a concomitant increment of the enzyme activity in the medium. The effect of the hormone was dose-dependent for a dose range of 10(-12)-10(-6) M. Acid phosphatase activity in prostate explants decreased from 38.6 +/- 3.5 to 20.5 +/- 2.8, whereas it increased from 0.60 +/- 0.15 to 2.80 +/- 0.40 nmol p-nitrophenol liberated/mg protein/30 min in the culture medium. Tissues exposed to 10(-6) M salmon calcitonin had higher acetylcholinesterase activity (8.8 +/- 0.7) than non-exposed ones (6.2 +/- 0.5 mumol substrate hydrolyzed/g tissue/min). These results suggest that locally produced calcitonin causes a release for prostatic acid phosphatase from prostate tissues possibly through its interaction with the cholinergic system.

MeSH terms

  • Acetylcholinesterase / metabolism
  • Acid Phosphatase / metabolism*
  • Animals
  • Calcitonin / pharmacology*
  • Culture Media
  • Culture Techniques
  • Dose-Response Relationship, Drug
  • Male
  • Prostate / drug effects*
  • Prostate / enzymology
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Culture Media
  • salmon calcitonin
  • Calcitonin
  • Acetylcholinesterase
  • Acid Phosphatase