Episodes Of Rhabdomyolysis Research Articles

Lactate Transporter Defect: A New Disease of Muscle

New methods were used to identify the abnormality in a patient who showed evidence of neuromuscular dysfunction on extensive clinical examination. The methods revealed that the lactate content of the patient's skeletal muscle does not decline normally after exercise and that his red cells are defective in lactate transport. These results suggest that skeletal muscle and erythrocyte membranes share the same genetic lactate transporter (or a common subunit), which is deficient in this patient. This defect may be a common cause of elevated serum creatine kinase levels, as seen in the patient described here and of unexplained episodes of rhabdomyolysis and myoglobinuria.

Recurrent Rhabdomyolysis as a Manifestation of Alcoholic Myopathy

A 38-year-old man experienced six severe episodes of rhabdomyolysis and two episodes of pharyngeal muscle weakness superimposed on chronic alcoholic myopathy and complicated by cardiomyopathy. A muscle biopsy specimen demonstrated sharply reduced levels of electrolytes despite normal serum values; presumably, these deficiencies were related to the pathogenesis of the recurrent rhabdomyolysis.

“Carnitine deficient” myopathy and cardiomyopathy with fatal outcome

A 13-year-old boy with a mild limb girdle muscular weakness had a massive rhabdomyolysis and cardiac arrest after general anesthesia. A congestive cardiomyopathy then developed. Muscle biopsy revealed an unspecific "myopathic" degeneration of muscle fibers and a slight accumulation of lipid droplets. Carnitine content was markedly reduced in muscle and moderately in plasma. Both prednisone and carnitine therapies were unable to improve the heart insufficiency, and the patient died 1 year after the acute episode of rhabdomyolysis.

Rhabdomyolysis

HYPOPHOSPHATEMIA may result in a number of pathologic conditions. Fuller et al1have called attention to the fact that rhabdomyolysis may be precipitated by hypophosphatemia, particularly when accompanied by strenuous muscle work. In our patient, severe hypophosphatemia occurred secondary to parathyroidectomy and calcium replacement, resulting in an episode of rhabdomyolysis. Parathyroidectomy is frequently required by patients receiving longterm hemodialysis for control of renal osteodystrophy. To the best of our knowledge, rhabdomyolysis has not previously been reported as a complication of parathyroidectomy and calcium supplementation. Report of a Case A 33-year-old woman receiving long-term hemodialysis was admitted to the University of Mississippi Medical Center on March 27, 1977, for parathyroidectomy. Membranous glomerulonephritis was diagnosed in 1959, requiring long-term hemodialysis in June 1973. Her course was complicated by severe hypertension, and in October 1973 she underwent a bilateral nephrectomy for uncontrollable hypertension. During the patient's dialysis course, her serum inorganic phosphorus

Characteristics of Adult and Foetal Myoglobin in the Visible Light Spectrums

A MYOGLOBIN which differed from adult myoglobin (MbA) was found in the urine1 of a 28-year-old woman during an episode of idiopathic rhabdomyolysis with myoglobinuria. The same haem protein was later demonstrated in the patient's skeletal muscle2 where it comprised the bulk of the benzidine positive protein after haemoglobin and cytochrome c had been separated from the myoglobin by column chromatography. This distinct chromoprotein was similar in its solubility in ammonium sulphate, spectroscopic characteristics and on cellulose acetate electrophoresis to foetal skeletal myoglobin (MbF) prepared in the same manner from the psoas muscle of infants stillborn at term. It was concluded that myoglobin, like haemoglobin, can present molecular variations which express themselves as disease syndromes, for example, rhabdomyolysis, under certain conditions. Although these clinical and biochemical findings have been supported by one investigator3, other reports do not regard MbF as an entity but rather as an artefact produced by the method used in preparing the myoglobin for analysis. The evidence against MbF has recently been summarized4. The present report examines the spectroscopic characteristics of MbA and MbF, adult and foetal haemoglobin (HbA and HbF, respectively) derived from muscle and blood of the human, dog and pig. The methods were designed to study the various pigments under optimum and standard conditions to minimize the effects of changing pH, salt concentrations, temperature, state of haem oxidation, crystallizations and other manipulations.