3′(2′)-Phosphoadenosine 5′-phosphate phosphatase is reduced in postmortem frontal cortex of bipolar patients

G. Shaltiel, N. Kozlovsky, R. H. Belmaker, G. Agam

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Objective: 3′(2′)-Phosphoadenosine 5′-phosphate (PAP) phosphatase is a novel lithium (Li) inhibitable enzyme. Thus the enzyme seemed an important candidate for studies of the molecular etiology of bipolar disorder. Methods: RT-PCR, Western-blot analysis and Pi liberation were used to measure PAP phosphatase mRNA levels, protein levels and enzyme activity (respectively) in postmortem frontal cortex specimens of bipolar patients versus normal subjects. Results: The PAP phosphatase protein levels were 24% significantly lower in bipolar patients than in normal subjects. PAP phosphatase mRNA levels and enzymatic activity did not differ between normal controls and bipolar patients. Conclusions: Abnormality of PAP phosphatase in bipolar patients offers a new direction for study of bipolar disorder etiology.

Original languageEnglish
Pages (from-to)302-306
Number of pages5
JournalBipolar Disorders
Issue number5
StatePublished - 1 Oct 2002


  • Bipolar disorder
  • Enzymatic activity
  • Frontal cortex
  • Levels
  • Lithium
  • PAP phosphatase
  • Protein levels
  • mRNA

ASJC Scopus subject areas

  • Psychiatry and Mental health
  • Biological Psychiatry


Dive into the research topics of '3′(2′)-Phosphoadenosine 5′-phosphate phosphatase is reduced in postmortem frontal cortex of bipolar patients'. Together they form a unique fingerprint.

Cite this