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Tubular aggregates (TA) are unusual intramuscular structures stained basophilic on hematoxilin and eosin (HE) staining and red on modified Gomori trichrome (GT) staining. The structures are said to be originated from sarcoplasmic reticulum and are collections of tubules with double membranes on electron microscopic studies. The TA are usually seen in biopsy muscles from patients with muscle pain and cramps but without muscle weakness, periodic paralysis or alcoholic myopathy. In addition, there are five reports on families with progressive myopathy and tubular aggregates in the literature. We presented here a 48-year-old postman without any family history, who had had progressive muscle weakness for 17 years. He had never noticed pain or cramps in his muscles, not taken any particular medicine, and not had regular alcoholic beverages. There was no ptosis, facial weakness, masticatory muscle weakness or dysphagia. Muscle wasting, started from the proximal part of four extremities had progressed to the distal part of them. He could not walk on heels or toes and walked with waddling gait. He stood up with Gowers' maneuver. Serum GOT, GPT and CK were elevated. EMG showed myogenic pattern and MCV was normal. The muscle biopsies were performed; the first one taken from quadriceps femoris muscle at 42 years old showed myopathic changes including marked variation in fiber sizes, with scattered necrotic fiber splitting and TA in type 2B fibers. The second biopsy from biceps brachii muscle at the age of 48 years, showed densely proliferated fibrous tissues, marked variation fiber sizes and scattered split fibers. The TA were rarely seen and type 2B fibers were decreased in number.(ABSTRACT TRUNCATED AT 250 WORDS)

In three adult men, serum creatine kinase activity was constantly raised for at least 4 years. They had been normal in other neuromuscular functions and did not have any established disease. Quantitative morphologic and pharmacologic studies were performed on biopsied muscle. The biceps brachii of patient 1 contained 0.3% necrotic fibers. In patient 2, only slight variation of muscle fiber diameter was noted. Muscle of patient 3 contained a few small angular fibers, and 11% of fibers exhibited internal nuclei. Sensitivity to caffeine in vitro was increased in patients 2 and 3, as seen in survivors of malignant hyperthermia; patients in hyperCKemia may be susceptible to malignant hyperthermia.

Immunoblot characterization and immunofluorescence localization of dystrophin are presented for 76 human patients with various neuromuscular diseases. Normal dystrophin (shown by immunoblotting) was invariably visualized as a continuous, peripheral membrane immunostaining of myofibers. Biochemical abnormalities of dystrophin (either lower or higher molecular weight dystrophin) resulted in patchy, discontinuous immunostaining, suggesting that the abnormal dystrophin proteins are not capable of creating a complete membrane cytoskeleton network. There was a very strong correlation of clinical diagnoses with the type of dystrophin abnormality; all Duchenne muscular dystrophy patient muscle contained no detectable dystrophin, Becker muscular dystrophy patient muscle had clearly abnormal dystrophin, and unrelated diseases showed normal dystrophin. However, a single patient of five carrying the diagnosis of Fukuyama dystrophy showed no detectable dystrophin and thus appeared to be a Duchenne dystrophy patient by the biochemical assays. We know of no other case of a patient with a disease thought to be unrelated to Duchenne/Becker dystrophy yet demonstrating dystrophin deficiency. Based on the data presented, we conclude that immunofluorescence is the best technique for the detection of female carriers of Duchenne dystrophy, whereas immunoblotting appears superior for the prognostic diagnosis of Becker muscular dystrophy.

Using the skinned fiber preparation, the response to caffeine was studied on the skeletal muscle of malignant hyperthermia or other neuromuscular diseases. The sensitivity to caffeine was increased in the muscle of malignant hyperthermia. The sensitivity also was increased in Duchenne muscular dystrophy or asymptomatic patients with raised serum creatine kinase activity. Judging from the interaction between caffeine and the contractile system, the abnormal response originated from the sarcoplasmic reticulum in malignant hyperthermia. In Duchenne muscular dystrophy, the contractile system also might be involved in the increased sensitivity. Since the disease spectrum presenting abnormal responses is broad, it is suggested that muscle fibers become sensitive to caffeine when they are degenerating or regenerating.

Three cases from 2 families had muscle weakness with predilection for distal extremities, predominantly affecting the tibialis anterior muscles, and onset in early adulthood. The disorder seemed to be inherited through an autosomal recessive trait. The EMG demonstrated a myopathic pattern and CPK was mildly elevated. The striking finding in their muscle biopsies was the presence of "rimmed" vacuoles which had acid phosphatase-positive autophagic activity and which contained numerous concentric lamellar bodies in various forms (myeloid and cabbage bodies). Despite rapid clinical progression, not only necrotic fibers with phagocytosis, as seen in Duchenne dystrophy, but also evidence of regeneration were virtually absent. Continuous destruction of myofibrils by activation of certain lysosomal proteolytic enzymes might be responsible for the production of atrophic fibers.