RGD Reference Report - Ca2+-regulatory muscle proteins in the alcohol-fed rat. - Rat Genome Database

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Ca2+-regulatory muscle proteins in the alcohol-fed rat.

Authors: Ohlendieck, K  Harmon, S  Koll, M  Paice, AG  Preedy, VR 
Citation: Ohlendieck K, etal., Metabolism. 2003 Sep;52(9):1102-12.
RGD ID: 1581765
Pubmed: PMID:14506614   (View Abstract at PubMed)

Alcoholic myopathy is characterized by muscle weakness and difficulties in gait and locomotion. It is one of the most prevalent skeletal muscle disorders in the Western hemisphere, affecting between 40% and 60% of all chronic alcohol misusers. However, the pathogenic mechanisms are unknown, although recent studies have suggested that membrane defects occur as a consequence of chronic alcohol exposure. It was our hypothesis that alcohol ingestion perturbs membrane-located proteins associated with intracellular signalling and contractility, in particular those relating to calcium homeostasis. To test this, we fed male Wistar rats nutritionally complete liquid diets containing ethanol as 35% of total dietary energy. Controls were pair-fed identical amounts of the same diet in which ethanol was replaced by isocaloric glucose. At the end of 6 weeks, rats were killed and skeletal muscles dissected. These were used to determine important ion-regulatory skeletal muscle proteins including sarcalumenin (SAR), sarcoplasmic-endoplasmic reticulum Ca(2+)-adenosine triphosphatase (ATPase) (SERCA1), the junctional face protein of 90 kd (90-JFP), alpha(1)- and alpha(2)-dihydropyridine receptor (alpha(1)-DHPR and alpha(2)-DHPR), and calsequestrin (CSQ) by immunoblotting. The relative abundance of microsomal proteins was determined by immunoblotting using the enhanced chemiluminescence (ECL) technique. The data showed that alcohol-feeding significantly reduced gastrocnemius and hind limb muscle weights (P <.05 in both instances). Concomitant changes included increases in the relative amounts of SERCA1 (P <.05) and Ca(2+)-ATPase activity (P <.025). However, there were no statistically significant changes in either SAR, 90-JFP, alpha(1)-DHPR or alpha(2)-DHPR (P >.2 in all instances). Reductions in CSQ were of marginal significance (P =.0950). We conclude that upregulation of SERCA1 protein and Ca(2+)-ATPase activity may be an adaptive mechanism and/or a contributory process in the pathology of alcohol-induced muscle disease.

RGD Manual Disease Annotations    Click to see Annotation Detail View
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
Alcohol Myopathy  ISOAtp2a1 (Rattus norvegicus)1581765; 1581765 RGD 
Alcohol Myopathy  IEP 1581765 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Atp2a1  (ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1)

Genes (Mus musculus)
Atp2a1  (ATPase, Ca++ transporting, cardiac muscle, fast twitch 1)

Genes (Homo sapiens)
ATP2A1  (ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1)

Objects referenced in this article
Gene Casq1 calsequestrin 1 Rattus norvegicus

Additional Information