Analysis of muscle proteins in acute quadriplegic myopathy

Matsumoto, Nobuko; Nakamura, Takeshi; Yasui, Yoshie; Torii, J

doi:10.1002/1097-4598(200008)23:8<1270::aid-mus18>3.0.co;2-e

Cited by 30 publications

(24 citation statements)

References 20 publications

(37 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1D), and by electrophoresis. 130 Immunostains are more variable depending on the myosin isoforms that are examined. 32 Myosin loss may be related to a decreased transcription rate or loss of myosin messenger RNA.…”

Section: Critical Illness Myopathysupporting

confidence: 63%

“…32 Structural proteins, aside from myosin, are mostly unaffected. 32,118,130 Myosin loss is often seen along with features of myofibrillar disorganization, including abnormal basophilic stippling with hematoxylin and eosin stains, purplish staining with Gomori trichrome, and irregular clumping of the reaction product or core-like changes with NADH-TR staining.…”

Section: Critical Illness Myopathymentioning

confidence: 99%

See 1 more Smart Citation

Neuromuscular Disorders in Critically Ill Patients: Review and Update

Lacomis

2011

Journal of Clinical Neuromuscular Disease

View full text Add to dashboard Cite

Neuromuscular disorders that are diagnosed in the intensive care unit (ICU) usually cause substantial limb weakness and contribute to ventilatory dysfunction. Although some lead to ICU admission, ICU-acquired disorders, mainly critical illness myopathy (CIM) and critical illness polyneuropathy (CIP), are more frequent and are associated with considerable morbidity. Approximately 25% to 45% of patients admitted to the ICU develop CIM, CIP, or both. Their clinical features often overlap; therefore, nerve conduction studies and electromyography are particularly helpful diagnostically, and more sophisticated electrodiagnostic studies and histopathologic evaluation are required in some circumstances. A number of prospective studies have identified risk factors for CIP and CIM, but their limitations often include the inability to separate CIM from CIP. Animal models reveal evidence of a channelopathy in both CIM and CIP, and human studies also identified axonal degeneration in CIP and myosin loss in CIM. Outcomes are variable. They tend to be better with CIM, and some patients have longstanding disabilities. Future studies of well-characterized patients with CIP and CIM should refine our understanding of risk factors, outcomes, and pathogenic mechanisms, leading to better interventions.

show abstract

Section: Critical Illness Myopathysupporting

confidence: 63%

Section: Critical Illness Myopathymentioning

confidence: 99%

Neuromuscular Disorders in Critically Ill Patients: Review and Update

Lacomis

2011

Journal of Clinical Neuromuscular Disease

View full text Add to dashboard Cite

show abstract

“…Besides muscle weakness, AQM is characterized by muscle atrophy, especially of fast twitch fibers (32), with or without selective loss of myosin filaments (33,34). The CSA of diaphragm type IIx/b fibers was significantly decreased in the MVS group and slightly more in the MVROC group.…”

Section: Overview Of the Principal Findingsmentioning

confidence: 99%

Rocuronium exacerbates mechanical ventilation–induced diaphragm dysfunction in rats

Testelmans

Maes

Wouters

et al. 2006

Critical Care Medicine

View full text Add to dashboard Cite

Infusion of rocuronium during controlled mechanical ventilation leads to further deterioration of diaphragm function, additional atrophy of type IIx/b fibers, and an increase in MURF-1 messenger RNA in the diaphragm, which suggests an activation of the ubiquitin-proteasome pathway. These findings could be important with regard to weaning failure in patients receiving this drug for prolonged periods in the intensive care unit setting.

show abstract

“…Clinical characteristics include flaccid muscle paralysis of limb muscles, muscle wasting, intact cranial nerve function, low compound muscle action potentials and intact motor and sensory nerve conduction velocities [5,7,8]. Other pathological features include a preferential loss of the thick filament protein myosin [4,5,7,9–11], muscle fiber atrophy [3–5], and an in-excitable muscle membrane [8]. …”

Section: Introductionmentioning

confidence: 99%

Myofibrillar protein and gene expression in acute quadriplegic myopathy

Norman

Zackrisson

Hedström

et al. 2009

Journal of the Neurological Sciences

View full text Add to dashboard Cite

The dramatic muscle wasting, preferential loss of myosin and impaired muscle function in intensive care unit (ICU) patients with acute quadriplegic myopathy (AQM) have traditionally been suggested to be the result of proteolysis via specific proteolytic pathways. In this study we aim to investigate the mechanisms underlying the preferential loss of thick vs. thin filament proteins and the reassembly of the sarcomere during the recovery process in muscle samples from ICU patients with AQM. Quantitative and qualitative analyses of myofibrillar protein and mRNA expression were analyzed using SDS-PAGE, confocal microscopy, histochemistry and real-time PCR. The present results demonstrate that the transcriptional regulation of myofibrillar protein synthesis plays an important role in the loss of contractile proteins, as well as the recovery of protein levels during clinical improvement, myosin in particular, presumably in concert with proteolytic pathways, but the mechanisms are specific to the different thick and thin filament proteins studied.

show abstract

Analysis of muscle proteins in acute quadriplegic myopathy

Cited by 30 publications

References 20 publications

Neuromuscular Disorders in Critically Ill Patients: Review and Update

Neuromuscular Disorders in Critically Ill Patients: Review and Update

Rocuronium exacerbates mechanical ventilation–induced diaphragm dysfunction in rats

Myofibrillar protein and gene expression in acute quadriplegic myopathy

Contact Info

Product

Resources

About