The decrease in prolidase activity in myeloproliferative neoplasms

Adv Clin Exp Med. 2012 Nov-Dec;21(6):767-71.

Abstract

Background: The development of bone marrow fibrosis is a severe complication in hematological diseases. The progress of bone marrow myelofibrosis is evaluated by a trephine examination and may be characterized by the biochemical markers of collagen turnover determination.

Objectives: Investigation of serum prolidase activity and biochemical markers of collagen metabolism in order to establish its role in the development of bone marrow fibrosis.

Material and methods: The group of 37 patients with myeloproliferative neoplasms (MPN) before treatment, consisted of 16 patients with chronic myeloid leukemia (CML), 7 with primary myelofibrosis (PMF), 8 with essential thrombocythopenia (ET), and 6 with polycythemia vera (PV).

Results: It was found that the plasma activity of prolidase (Pro) was reduced to almost half together with the serum level of osteocalcin (BGL), and hydroxyproline (H-PRO) in the serum and urine of patients with MPN in comparison to the control group. In the MPN group of patients, the levels of N-terminal procollagen III peptide (PIIINP), type I procollagen (PICP) and the C-terminal telopeptide of type I collagen (ICTP) were significantly higher.

Conclusions: The alteration of collagen turnover markers in the MPN patient group (the elevation of synthesis and inhibition of collagen catabolism rate) has suggested that a diminished prolidase activity may contribute to such alteration of collagen metabolism and should be consider a biomarker of MPN progress.

MeSH terms

  • Adult
  • Aged
  • Biomarkers, Tumor / metabolism
  • Bone Marrow Neoplasms / enzymology*
  • Bone Marrow Neoplasms / physiopathology
  • Bone Remodeling
  • Case-Control Studies
  • Connective Tissue / pathology
  • Connective Tissue / physiopathology
  • Dipeptidases / metabolism*
  • Female
  • Humans
  • Male
  • Middle Aged
  • Young Adult

Substances

  • Biomarkers, Tumor
  • Dipeptidases
  • proline dipeptidase