1
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Cytosolic Ca2+ buffers.

      1
      Cold Spring Harbor perspectives in biology
      Cold Spring Harbor Laboratory

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          "Ca(2+) buffers," a class of cytosolic Ca(2+)-binding proteins, act as modulators of short-lived intracellular Ca(2+) signals; they affect both the temporal and spatial aspects of these transient increases in [Ca(2+)](i). Examples of Ca(2+) buffers include parvalbumins (α and β isoforms), calbindin-D9k, calbindin-D28k, and calretinin. Besides their proven Ca(2+) buffer function, some might additionally have Ca(2+) sensor functions. Ca(2+) buffers have to be viewed as one of the components implicated in the precise regulation of Ca(2+) signaling and Ca(2+) homeostasis. Each cell is equipped with proteins, including Ca(2+) channels, transporters, and pumps that, together with the Ca(2+) buffers, shape the intracellular Ca(2+) signals. All of these molecules are not only functionally coupled, but their expression is likely to be regulated in a Ca(2+)-dependent manner to maintain normal Ca(2+) signaling, even in the absence or malfunctioning of one of the components.

          Related collections

          Author and article information

          Journal
          Cold Spring Harb Perspect Biol
          Cold Spring Harbor perspectives in biology
          Cold Spring Harbor Laboratory
          1943-0264
          1943-0264
          Nov 2010
          : 2
          : 11
          Affiliations
          [1 ] Unit of Anatomy, Department of Medicine, University of Fribourg, Route Albert-Gockel 1, CH-1700 Fribourg, Switzerland. beat.schwaller@unifr.ch
          Article
          cshperspect.a004051
          10.1101/cshperspect.a004051
          2964180
          20943758
          0803c447-0f79-405c-a3cf-d859f8b73e31
          History

          Comments

          Comment on this article