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Acid phosphatases
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  1. H Bull1,
  2. P G Murray3,
  3. D Thomas2,
  4. A M Fraser2,4,
  5. P N Nelson
  1. 1Human and Clinical Research Group, School of Nursing, University of Nottingham, Derbyshire Royal Infirmary, Derby DE1 2QY, UK
  2. 2Biomedical Research Laboratories, School of Health Sciences, University of Wolverhampton, 62–68 Lichfield Street, Wolverhampton WV1 1DJ, UK
  3. 3Department of Pathology, Division of Cancer Studies, University of Birmingham, Birmingham B15 2TT, UK
  4. 4Orthopaedic Department, New Cross Hospital, Wednesfield Road, Wolverhampton WV10 0QP, UK
  1. Correspondence to:
 Dr P N Nelson, Biomedical Research Laboratories, School of Health Sciences, University of Wolverhampton, 62–68 Lichfield Street, Wolverhampton WV1 1DJ, UK;
 P.N.NELSON{at}wlv.ac.uk
 Dr H Bull, Hyman & Clinical Research Group, School of Nursing, University of Nottingham, Derbyshire Royal Infirmary, Derby DE1 2QY, UK

Abstract

Acid phosphatases (APs) are a family of enzymes that are widespread in nature, and can be found in many animal and plant species. Mystery surrounds the precise functional role of these molecular facilitators, despite much research. Yet, paradoxically, human APs have had considerable impact as tools of clinical investigation and intervention. One particular example is tartrate resistant acid phosphatase, which is detected in the serum in raised amounts accompanying pathological bone resorption. This article seeks to explore the identity and diversity of APs, and to demonstrate the relation between APs, human disease, and clinical diagnosis.

  • acid phosphatases
  • osteoclast
  • bone resorption
  • tartrate resistant acid phosphatase
  • AP, acid phosphatase
  • EAP, erythrocyte acid phosphatase
  • FSD, functional secretory domain
  • LAP, lysosomal acid phosphatase
  • OcAP, osteoclast acid phosphatase
  • PAP, prostate acid phosphatase
  • PSA, prostate specific antigen
  • ROS, reactive oxygen species
  • TRAP, tartrate resistant acid phosphatase

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