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  1. Article

    Open Access

    Activation of Ca2+ transport in cardiac microsomes enriches functional sets of ER and SR proteins

    The importance of sarcoplasmic reticulum (SR) Ca2+-handling in heart has led to detailed understanding of Ca2+-release and re-uptake protein complexes, while less is known about other endoplasmic reticulum (ER) f...

    Steven E. Cala, Nicholas J. Carruthers… in Molecular and Cellular Biochemistry (2024)

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    Article

    Altered calsequestrin glycan processing is common to diverse models of canine heart failure

    Calsequestrin-2 (CSQ2) is a resident glycoprotein of junctional sarcoplasmic reticulum that functions in the regulation of SR Ca2+ release. CSQ2 is biosynthesized in rough ER around cardiomyocyte nuclei and then ...

    Sony Jacob, Naama H. Sleiman, Stephanie Kern… in Molecular and Cellular Biochemistry (2013)

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    Article

    The cytosolic protein kinase CK2 phosphorylates cardiac calsequestrin in intact cells

    The luminal SR protein CSQ2 contains phosphate on roughly half of the serines found in its C-terminus. The sequence around phosphorylation sites in CSQ2 suggest that the in vivo kinase is protein kinase CK2, e...

    Timothy P. McFarland, Naama H. Sleiman… in Molecular and Cellular Biochemistry (2011)

  4. No Access

    Article

    Phosphorylation and dephosphorylation of calsequestrin on CK2-sensitive sites in heart

    Calsequestrin (CSQ) concentrates in junctional sarcoplasmic reticulum (SR) where it functions in regulation of Ca2+ release. When purified from heart tissue, cardiac CSQ contains phosphate on a cluster of C-termi...

    Michal L. Ram, Arash Kiarash, James D. Marsh… in Molecular and Cellular Biochemistry (2004)

  5. No Access

    Article

    Developmental regulation of the L-type calcium channel α1C subunit expression in heart

    We used Northern analyses, RNase protection assays and immunoblot analyses to examine the relationship among developmental age of the heart, abundance of mRNA and L-type calcium channel α1Csubunit protein, and to...

    Lei Leu, Donald S. O'Hara, Steven E. Cala… in Molecular and Cellular Biochemistry (2000)

  6. No Access

    Article

    Unitary anion currents through phospholemman channel molecules

    PHOSPHOLEMMAN (PLM) is a 72-amino-acid peptide with a single transmembrane domain1–3, the expression of which induces chloride currents in Xenopus oocytes4–6. It has remained unknown whether PLM is an ion channel...

    J. Randall Moorman, Stephen J. Ackerman, Gopal C. Kowdley, M. Pamela Griffin… in Nature (1995)