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Cardiac Markers pp 113–125Cite as

Creatine Kinase, Isoenzymes, and Variants

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Part of the book series: Pathology and Laboratory Medicine ((PLM))

Abstract

Creatine kinase (CK)* (EC 2.7.3.2, adenosine triphosphate: creatine N-phospho-transferase) exists as a dimer, and is an important enzyme regulator of high-energy phosphate production and utilization within contractile tissues. Recent studies suggest that CK also has a more general role in shuttling high-energy phosphate bonds via creatine phosphate (CP) from the site of ATP production in the mitochondria to the site of utilization within the cytoplasm (1). The “shuttle hypothesis” is supported by observations that CK is found in some tissues, such as the distal tubules of the nephron, that have high energy needs. Although the distal tubules have no contractile function, they nevertheless require ATP for maintenance of ionic gradients through the ATP-dependent sodium-potassium membrane pump (2).

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Authors
  1. Alan H. B. Wu
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Editors and Affiliations

  1. Hartford Hospital, Hartford, CT, USA

    Alan H. B. Wu

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© 1998 Springer Science+Business Media New York

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Wu, A.H.B. (1998). Creatine Kinase, Isoenzymes, and Variants. In: Wu, A.H.B. (eds) Cardiac Markers. Pathology and Laboratory Medicine. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4612-1806-7_7

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  • DOI: https://doi.org/10.1007/978-1-4612-1806-7_7

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-4612-7292-2

  • Online ISBN: 978-1-4612-1806-7

  • eBook Packages: Springer Book Archive

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