We are analyzing https://link.springer.com/article/10.1007/s004410051315.

Title:
Sarcomeric myosin heavy chain is degraded by the proteasome | Cell and Tissue Research
Description:
Cardiac myofibrillar proteins, like all other intracellular proteins, are in a dynamic state of continual degradation and resynthesis. The balance between these opposing metabolic processes ultimately determines the number of functional contractile units within each cardiac muscle cell. Although alterations in myofibrillar protein degradation have been shown to contribute to cardiac growth and remodeling, the intracellular proteolytic systems responsible for degrading myofibrillar proteins to their constitutive amino acids are currently unknown. Lactacystin, a recently developed, highly specific proteasome inhibitor, was used in this study to examine the role of the proteasome in myosin heavy chain (MHC) degradation in cultured neonatal rat ventricular myocytes. Cells were treated with growth medium alone or with lactacystin (1–50 µM) for up to 48 h. Lactacystin significantly increased the total protein/DNA ratio and markedly prolonged MHC half-life. Other proteasome inhibitors, namely carbobenzoxy-L-leucyl-L-leucyl-L-leucinal (10 µM) and N-acetyl-L-leucyl-L-leucyl-norleucinal (100 µM), were also effective in suppressing MHC degradation. Lactacystin and other proteasome inhibitors also suppressed the markedly accelerated MHC degradation associated with Ca2+ channel blockade but did not prevent the disassembly and loss of myofibrils that accompanied contractile arrest. Thus, sarcomere disassembly precedes the degradation of MHC, which is at least in part mediated by the proteasome.
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Keywords {🔍}

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Topics {✒️}

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         headline:Sarcomeric myosin heavy chain is degraded by the proteasome
         description: Cardiac myofibrillar proteins, like all other intracellular proteins, are in a dynamic state of continual degradation and resynthesis. The balance between these opposing metabolic processes ultimately determines the number of functional contractile units within each cardiac muscle cell. Although alterations in myofibrillar protein degradation have been shown to contribute to cardiac growth and remodeling, the intracellular proteolytic systems responsible for degrading myofibrillar proteins to their constitutive amino acids are currently unknown. Lactacystin, a recently developed, highly specific proteasome inhibitor, was used in this study to examine the role of the proteasome in myosin heavy chain (MHC) degradation in cultured neonatal rat ventricular myocytes. Cells were treated with growth medium alone or with lactacystin (1–50 µM) for up to 48 h. Lactacystin significantly increased the total protein/DNA ratio and markedly prolonged MHC half-life. Other proteasome inhibitors, namely carbobenzoxy-L-leucyl-L-leucyl-L-leucinal (10 µM) and N-acetyl-L-leucyl-L-leucyl-norleucinal (100 µM), were also effective in suppressing MHC degradation. Lactacystin and other proteasome inhibitors also suppressed the markedly accelerated MHC degradation associated with Ca2+ channel blockade but did not prevent the disassembly and loss of myofibrils that accompanied contractile arrest. Thus, sarcomere disassembly precedes the degradation of MHC, which is at least in part mediated by the proteasome.
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            Cardiac hypertrophy
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            Human Genetics
            Proteomics
            Molecular Medicine
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      headline:Sarcomeric myosin heavy chain is degraded by the proteasome
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      datePublished:
      dateModified:
      pageStart:541
      pageEnd:548
      sameAs:https://doi.org/10.1007/s004410051315
      keywords:
         Key words Lactacystin
         Protein degradation
         Cardiac hypertrophy
         Atrophy
         Proteolysis
         Myocardium
         Rat (Sprague Dawley)
         Human Genetics
         Proteomics
         Molecular Medicine
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