Posttranslational heterogeneity of bone alkaline phosphatase in metabolic bone disease

Eur J Clin Chem Clin Biochem. 1994 Sep;32(9):675-80. doi: 10.1515/cclm.1994.32.9.675.

Abstract

Bone alkaline phosphatase is a marker of osteoblast activity. In order to study the posttranscriptional modification (glycosylation) of bone alkaline phosphatase in bone disease, we investigated the relationship between mass and catalytic activity of bone alkaline phosphatase in patients with osteoporosis and hyperthyroidism. Serum bone alkaline phosphatase activity was measured after lectin precipitation using the Iso-ALP test kit. Mass concentration of bone alkaline phosphatase was determined with an immunoradiometric assay (Tandem-R Ostase). In general, serum bone alkaline phosphatase mass and activity concentration correlated well. The activity : mass ratio of bone alkaline phosphatase was low in hyperthyroidism. Activation energy of the reaction catalysed by bone alkaline phosphatase was high in osteoporosis and in hyperthyroidism. Experiments with neuraminidase digestion further demonstrated that the thermodynamic heterogeneity of bone alkaline phosphatase can be explained by a different glycosylation of the enzyme.

MeSH terms

  • Adult
  • Aged
  • Aging / pathology
  • Alkaline Phosphatase / blood*
  • Alkaline Phosphatase / genetics
  • Bone and Bones / enzymology*
  • Female
  • Glycosylation
  • Humans
  • Hyperthyroidism / enzymology*
  • Immunoradiometric Assay
  • Kinetics
  • Lectins / chemistry
  • Male
  • Middle Aged
  • Neuraminidase / metabolism
  • Osteoblasts / enzymology
  • Osteoporosis / enzymology*
  • Osteoporosis, Postmenopausal / enzymology*
  • Protein Biosynthesis / genetics
  • Sex Factors
  • Thermodynamics

Substances

  • Lectins
  • Alkaline Phosphatase
  • Neuraminidase