Elevation in plasma alkaline phosphatase level during rhG-CSF administration. Granulocytopenic patients with gynecologic cancers treated with cancer chemotherapy

Gynecol Obstet Invest. 1998;45(2):99-104. doi: 10.1159/000009934.

Abstract

Neutropenic patients suffering from gynecologic cancers treated with cancer chemotherapy were evaluated to investigate changes in levels of plasma alkaline phosphatase (ALP) during recombinant human granulocyte colony stimulating factor (rhG-CSF) administration, and to discern its causes. Plasma ALP, ALP isozymes, neutrophil alkaline phosphatase (NAP) activity, and morphological maturation of neutrophils were measured prior to, during, and after rhG-CSF administration. Plasma ALP values were significantly elevated (p < 0.05) during administration of rhG-CSF. ALP-3, the dominant alkaline phosphatase fraction of NAP, was the dominant isozyme that showed an increase in the plasma. Moreover, the elevation of plasma ALP-3 significantly correlated with the elevation of NAP activity (r = 0.939, p < 0.0001), and neutrophils in which NAP activity was induced were not limited to morphologically mature neutrophils. These results showed that rhG-CSF acts to stimulate neutrophils at all stages of maturation and causes an elevation of plasma ALP(ALP-3) concentrations in plasma.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Alkaline Phosphatase / blood*
  • Antineoplastic Agents / adverse effects*
  • Endometrial Neoplasms / drug therapy
  • Female
  • Genital Neoplasms, Female / drug therapy*
  • Granulocyte Colony-Stimulating Factor / therapeutic use*
  • Humans
  • Isoenzymes / blood*
  • Middle Aged
  • Neutropenia / chemically induced
  • Neutropenia / enzymology*
  • Neutropenia / therapy
  • Neutrophils / enzymology
  • Neutrophils / pathology
  • Ovarian Neoplasms / drug therapy
  • Recombinant Proteins

Substances

  • Antineoplastic Agents
  • Isoenzymes
  • Recombinant Proteins
  • Granulocyte Colony-Stimulating Factor
  • Alkaline Phosphatase