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Unique Ca2+-Binding Proteins in Metazoan Invertebrates

  • Jos A. Cox
  • Ying Luan-Rilliet
  • Takashi Takagi

Abstract

Many external signals, like hormones, growth factors, sensory stimuli, neurotransmitters, or nerve impulses, are translated into intracellular information via the so-called Ca2+ signal, i.e., a transient increase (often oscillatory) in the free Ca2+ concentration from the resting 0.1 μM to peak values ranging from 0.2 to 2 μM. The Ca2+ signal is regulated by many devices at the level of the plasma membrane, of IP3-sensitive vesicular organelles, of cytosolic Ca2+ sequestering agents and, exceptionally, of the mitochondria. Also, the Ca2+ signal, first confined to the cytosol, is transduced into the mitochondria, where it regulates the production of ATP. The Ca2+ signal is useless unless it can be coupled to the cellular response systems, which range from muscle contraction, cell division, secretion, metabolic changes, and perception, to memory storage. Kretsinger proposed that proteins only can be mediators of the Ca2+ signal and that most of these Ca2+-binding proteins (CaBP1) possess a recurrent structural motif, i.e., the EF-hand Ca2+-binding domain (for recent review, see Kretsinger 1987). A functionally important discrimination must be made between two types of CaBPs: (1) those that convey the Ca2+-signal to a specific response system through conformational changes and activation of the target, and (2) those that buffer the Ca2+ and Mg2+ concentrations inside the cell. The former type possesses so-called Ca2+-specific sites, the latter Ca2++Mg2+ mixed sites.

Keywords

Fast Skeletal Muscle Mixed Site Muscle Myosin Light Chain Kinase Smooth Muscle Myosin Light Chain Sarcoplasmic Calcium Binding Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • Jos A. Cox
  • Ying Luan-Rilliet
  • Takashi Takagi

There are no affiliations available

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