Mordecai P Blaustein

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Plasma membrane-cytoskeleton-endoplasmic reticulum complexes in neurons and astrocytes.

Lubomira Lencesova; Andrea O'Neill; Wendy G Resneck; Robert J Bloch; Mordecai P Blaustein (Profiled Authors: Mordecai P Blaustein; Robert J Bloch)

Department of Physiology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
The Journal of biological chemistry 2004;279(4):2885-93.

The possibility that certain integral plasma membrane (PM) proteins involved in Ca(2+) homeostasis form junctional units with adjacent endoplasmic reticulum (ER) in neurons and glia was explored using immunoprecipitation and immunocytochemistry. Rat brain membranes were solubilized with the mild, non-ionic detergent, IGEPAL CA-630. Na(+)/Ca(2+) exchanger type 1 (NCX1), a key PM Ca(2+) transporter, was immunoprecipitated from the detergent-soluble fraction. Several abundant PM proteins co-immunoprecipitated with NCX1, including the alpha2 and alpha3 isoforms of the Na(+) pump catalytic (alpha) subunit, and the alpha2 subunit of the dihydropyridine receptor. The adaptor protein, ankyrin 2 (Ank 2), and the cytoskeletal proteins, alpha-fodrin and beta-spectrin, also selectively co-immunoprecipitated with NCX1, as did the ER proteins, Ca(2+) pump type 2 (SERCA 2), and inositol-trisphosphate receptor type 1 (IP(3)R-1). In contrast, a number of other abundant PMs, adaptors, and cytoskeletal proteins did not co-immunoprecipitate with NCX1, including the Na(+) pump alpha1 isoform, PM Ca(2+) pump type 1 (PMCA1), beta-fodrin, and Ank 3. In reciprocal experiments, immunoprecipitation with antibodies to the Na(+) pump alpha2 and alpha3 isoforms, but not alpha1, co-immunoprecipitated NCX1; the antibodies to alpha1 did, however, co-immunoprecipitate PMCA1. Antibodies to Ank 2, alpha-fodrin, beta-spectrin and IP(3)R-1 all co-immunoprecipitated NCX1. Immunocytochemistry revealed partial co-localization of beta-spectrin with NCX1, Na(+) pump alpha3, and IP(3)R-1 in neurons and of alpha-fodrin with NCX1 and SERCA2 in astrocytes. The data support the idea that in neurons and glia PM microdomains containing NCX1 and Na(+) pumps with alpha2 or alpha3 subunits form Ca(2+) signaling complexes with underlying ER containing SERCA2 and IP(3)R-1. These PM and ER components appear to be linked through the cytoskeletal spectrin network, to which they are probably tethered by Ank 2.

3 Originating Grant

• 1.

  Bloch, Robert J

  Obscurin & Myofibrils in Cardiac & Skeletal Muscle

  1 June 1999 - 30 June 2009

  NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

• 2.

  BLAUSTEIN, MORDECAI P

  Calcium and Sodium Transport in Hypertension

  1 July 1990 - 31 May 2013

  NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

• 3.

  Bloch, Robert J

  Macromolecules Involved in Synapse Formation

  1 April 1981 - 31 March 2007

  NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE

Scientific Context

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