OBJECT:Adhesion molecules are suggested to play important roles in the pathogenesis of inflammatory diseases. We examined the expression of adhesion molecules in the muscles of human inflammatory myopathies.METHODS:We immunohistochemically studied the expression and distribution of two molecules in the selectin family (E- and P-selectin) and their common ligand sialyl Lewis X in 18 inflammatory myopathies, 13 disease controls, and 16 normal controls.RESULTS:In inflammatory myopathies, E- and P-selectin were upregulated on the surface of blood vessels, especially on the endothelial cells of the venules. Sialyl Lewis X was upregulated in the blood vessels, infiltrating leukocytes, and the surface of some atrophic myofibers. Some control muscles also showed weakly positive staining with these molecules, however, expression of these molecules was most striking in the muscles of inflammatory myopathies.CONCLUSION:The results suggested that these molecules are upregulated in inflammatory myopathies and might play a role in the pathogenesis of inflammatory myopathies.

To study the relationship between dietary calcium intake and bone mineral density (BMD) among young Japanese females, we recruited 1298 females under 40 years living in Yokohama city for BMD measurement by Computed X-ray densitometer (CXD method) and dietary questionnaire. 1. The average of BMD was 2.75 mm/AI and was highest in the 35 to 39 year old group. 2. Calcium intake (Ca) and protein intake (Protein) were highest in 35 to 39 year old group. 3. BMD, Ca, and Protein were significantly higher in those who had regular dietary habits than those with irregular habits. 4. Among those who had lower Ca, (less than 600 mg per day), the amount of small fish consumed whole was negatively correlated with BMD (p = 0.035), and those with higher consumption of small fish than average had significantly (p = 0.018) lower BMD than those with lower small fish consumption adjusting for age and Ca and protein intake. These findings imply a possibility that small fish accompanied by higher salt intake may influence BMD adversely in this population by an interaction with calcium urinary excretion, which has been suggested by experimental and epidemiologic studies. Dietary composition of Ca may be important for prevention of osteoporosis.

We investigated the incidence of atopic dermatitis and related factors at infant physical examination at health centers. Subjects were 900 infants (290 four-month-old infants, 298 one-year and six month-old infants, 312 three-year-old infants) who participated in infant physical examinations in Kanazawa-ku, Yokohama City. Overall, we analyzed 696 infants whose mothers had cooperated with the survey by completing questionnaires during physical examinations, and who submitted to examination by consulting dermatologists. The incidence of atopic dermatitis was 11.6% in 4-month-old infants, 12.2% in 1.5-year-old infants, and 12.1% in 3-year-old infants. The following were found to be related to the atopic dermatitis of infants. 1. Family history of atopic dermatitis in their mothers and older siblings. 2. Mothers' limited diet during pregnancy (avoiding some food which are suspected allergens). 3. Past history of molluscum contagiosum. 4. The frequency of taking bath. While epidemiological surveys of atopic dermatitis have previously been performed, the criteria at each survey was not identical and results could not be compared precisely. In this survey, 1. Dermatologists specializing in atopic dermatitis performed examinations. 2. All diagnoses were made according to standardized criteria which are applied nationwide. 3. All subjects were from a specific region. Because of this approach, this survey provides important information that can form the basis of comparison for future epidemiological surveys of atopic dermatitis.

Muscle & NerveVolume 18, Issue 8 p. 910-913 Short Report Altered distribution of β-Dystroglycan in sarcolemma of human dystrophic muscles: An immunohistochemical study Dr. Takahiro Jimi MD, Dr. Takahiro Jimi MD Division of Neurology, Departments of Medicine, Showa University Fujigaoka Hospital, Yokohama, JapanSearch for more papers by this authorDr. Yoshihiro Wakayama MD PhD, Corresponding Author Dr. Yoshihiro Wakayama MD PhD Division of Neurology, Departments of Medicine, Showa University Fujigaoka Hospital, Yokohama, JapanDivision of Neurology, Department of Medicine, Showa University Fujigaoka Hospital, 1–30, Fujigaoka, Aoba-ku, Yokohama 227, JapanSearch for more papers by this authorDr. Atsushi Takeda PhD, Dr. Atsushi Takeda PhD Clinical Pathology, Kanagawa Children's Medical Center, Showa University Fujigaoka Hospital, Yokohama, JapanSearch for more papers by this authorDr. Takuya Kobayashi MD, Dr. Takuya Kobayashi MD Department of Pediatrics, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Toshiyuki Kumagai MD, Dr. Toshiyuki Kumagai MD Division of Pediatric Neurology, Central Hospital, Aichi Prefectural Colony, Kasugai, JapanSearch for more papers by this authorDr. Yume Suzuki MD, Dr. Yume Suzuki MD Department of Neurology, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Osamu Hasegawa MD, Dr. Osamu Hasegawa MD Department of Neurology, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Sumimasa Yamashita MD, Dr. Sumimasa Yamashita MD Departments of Neurology, Kanagawa Children's Medical Center, Yokohama, JapanSearch for more papers by this authorDr. Seiji Shibuya MD, Dr. Seiji Shibuya MD Division of Neurology, Departments of Medicine, Showa University Fujigaoka Hospital, Yokohama, JapanSearch for more papers by this authorDr. Yoshiyuki Kuroiwa MD, Dr. Yoshiyuki Kuroiwa MD Department of Neurology, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Nobuko Misugi MD, Dr. Nobuko Misugi MD Orthopedics, Kanagawa Children's Medical Center, Yokohama, JapanSearch for more papers by this author Dr. Takahiro Jimi MD, Dr. Takahiro Jimi MD Division of Neurology, Departments of Medicine, Showa University Fujigaoka Hospital, Yokohama, JapanSearch for more papers by this authorDr. Yoshihiro Wakayama MD PhD, Corresponding Author Dr. Yoshihiro Wakayama MD PhD Division of Neurology, Departments of Medicine, Showa University Fujigaoka Hospital, Yokohama, JapanDivision of Neurology, Department of Medicine, Showa University Fujigaoka Hospital, 1–30, Fujigaoka, Aoba-ku, Yokohama 227, JapanSearch for more papers by this authorDr. Atsushi Takeda PhD, Dr. Atsushi Takeda PhD Clinical Pathology, Kanagawa Children's Medical Center, Showa University Fujigaoka Hospital, Yokohama, JapanSearch for more papers by this authorDr. Takuya Kobayashi MD, Dr. Takuya Kobayashi MD Department of Pediatrics, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Toshiyuki Kumagai MD, Dr. Toshiyuki Kumagai MD Division of Pediatric Neurology, Central Hospital, Aichi Prefectural Colony, Kasugai, JapanSearch for more papers by this authorDr. Yume Suzuki MD, Dr. Yume Suzuki MD Department of Neurology, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Osamu Hasegawa MD, Dr. Osamu Hasegawa MD Department of Neurology, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Sumimasa Yamashita MD, Dr. Sumimasa Yamashita MD Departments of Neurology, Kanagawa Children's Medical Center, Yokohama, JapanSearch for more papers by this authorDr. Seiji Shibuya MD, Dr. Seiji Shibuya MD Division of Neurology, Departments of Medicine, Showa University Fujigaoka Hospital, Yokohama, JapanSearch for more papers by this authorDr. Yoshiyuki Kuroiwa MD, Dr. Yoshiyuki Kuroiwa MD Department of Neurology, Yokohama City University, School of Medicine, Yokohama, JapanSearch for more papers by this authorDr. Nobuko Misugi MD, Dr. Nobuko Misugi MD Orthopedics, Kanagawa Children's Medical Center, Yokohama, JapanSearch for more papers by this author First published: August 1995 https://doi.org/10.1002/mus.880180818Citations: 4AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 Arahata K, Ishihara T, Kamakura K, Tsukahara T, Ishiura S, Baba C, Matsumoto T, Nonaka I, Sugita H: Mosaic expression of dystrophin in symptomatic carriers of Duchenne's muscular dystrophy. N Engl J Med 1989; 320: 138–142. 2 Arahata K, Hayashi YK, Mizuno Y, Yoshida M, Ozawa E: Dystrophin-associated glycoprotein and dystrophin colocalisation at sarcolemma in Fukuyama congenital muscular dystrophy. Lancet 1993; 342: 623–624. 3 Arikawa E, Ishihara T, Nonaka I, Sugita H, Arahata K: Immunocytochemical analysis of dystrophin in congenital muscular dystrophy. J Neurol Sci 1991; 105: 79–87. 4 Ervasti JM, Campbell KP: Membrane organization of the dystrophin-glycoprotein complex. Cell 1991; 66: 1121–1131. 5 Fischbeck KH, Bonilla E, Schotland DL: Freeze fracture analysis of plasma membrane cholesterol in Duchenne muscle. Ann Neurol 1983; 13: 532–535. 6 Hoffman EP, Brown RH, Kunkel LM: Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 1987; 51: 919–928. 7 Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, Slaughter CA, Sernett SW, Campbell KP: Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 1992; 355: 696–702. 8 Ibraghimov-Beskrovnaya O, Milatovich A, Ozcelik T, Yang B, Koepnick K, Francke U, Campbell KP: Human dystroglycan: skeletal muscle cDNA, genomic structure, origin of tissue specific isoforms and chromosomal localization. Hum Mol Genet 1993; 2: 1651–1657. 9 Jimi T, Wakayama Y, Takeda A, Misugi N, Kumagai T, Miyake S: Immunoreactivity of antibodies raised against synthetic peptide fragments predicted from cystein-rich and carboxy-terminal domains of dystrophin cDNA. Showa Univ J Med Sci 1992; 4: 141–150. 10 Matsumura K, Tome FMS, Collin H, Azibi K, Chaouch M, Kaplan JC, Fardeau M, Campbell KP: Deficiency of the 50K dystrophin-associated glycoprotein in severe childhood autosomal recessive muscular dystrophy. Nature 1992; 359: 320–322. 11 Matsumura K, Nonaka I, Campbell KP: Abnormal expression of dystrophin-associated protein in Fukuyama-type congenital muscular dystrophy. Lancet 1993; 341: 521–522. 12 Miranda AF, Francke U, Bonilla E, Martucci G, Schmidt B, Salviati G, Rubin M: Dystrophin immunocytochemistry in muscle culture: detection of a carrier of Duchenne muscular dystrophy. Am J Med Genet 1989; 32: 268–273. 13 Ohlendieck K, Campbell KP: Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J Cell Biol 1991; 115: 1685–1694. 14 Ohlendieck K, Matsumura K, Ionasescu VV, Towbin JA, Bosch EP, Weinstein SL, Sernett SW, Campbell KP: Duchenne dystrophy: deficiency of dystrophin-associated proteins in the sarcolemma. Neurology 1993; 43: 795–800. 15 Schotland DL, Bonilla E, Wakayama Y: Freeze fracture studies of muscle plasma membrane in human muscular dystrophy. Acta Neuropathol 1981; 54: 189–197. 16 Toda T, Segawa M, Nomura Y, Nonaka I, Masuda K, Ishihara T, Suzuki M, Tomita I, Origuchi Y, Ohno K, Misugi N, Sasaki Y, Takada K, Kawai M, Otani K, Murakami T, Saito K, Fukuyama Y, Shimizu T, Kanazawa I, Nakamura Y: Localization of gene for Fukuyama type congenital muscular dystrophy to chromosome 9q31–33. Nat Genet 1993; 5: 283–286. 17 Yoshida M, Mizuno Y, Nonaka I, Ozawa E: A dystrophin-associated glycoprotein, A3a (one of 43 DAG doublets), is retained in Duchenne muscular dystrophy muscle. J Biochem 1993; 114: 634–639. 18 Wakayama Y, Okayasu H, Shibuya S, Kumagai T: Duchenne dystrophy: reduced density of orthogonal array subunit particles in muscle plasma membrane. Neurology 1984; 34: 1313–1317. 19 Wakayama Y, Kumagai T, Shibuya S: Freeze fracture studies of muscle plasma membrane in Fukuyama type congenital muscular dystrophy. Neurology 1985; 35: 1587–1593. 20 Wakayama Y, Kumagai T, Jimi T: Small size of orthogonal array in muscle plasma membrane of Fukuyama type congenital muscular dystrophy. Acta Neuropathol 1986; 72: 130–133. 21 Wakayama Y, Kumagai T, Jimi T, Shibuya S: Freezefracture analysis of cholesterol in muscle plasma membrane of Fukuyama-type congenital muscular dystrophy. Acta Neuropathol 1987; 75: 46–50. 22 Wakayama Y, Jimi T, Misugi N, Kumagai T, Miyake S, Shibuya S, Miike T: Dystrophin immunostaining and freeze-fracture studies of muscles of patients with early stage amyotrophic lateral sclerosis and Duchenne muscular dystrophy. J Neurol Sci 1989; 91: 191–205. 23 Wakayama Y, Jimi T, Takeda A, Shibuya S, Nakamura Y, Oniki H: Immunoelectron microscopic localization of C-terminus of 43-kDa dystrophin-associated glycoprotein in normal human skeletal myofibers. J Electron Microsc 1994; 43: 327–331. Citing Literature Volume18, Issue8August 1995Pages 910-913 ReferencesRelatedInformation

We reported a case of a fifteen-year-old boy with metatropic dysplasia. He showed short-limbed dwarfism at the age of 1 year and 2 months. Roentgenograms of the bone revealed generalized platyspondyly, enlargement of the epiphyseal-metaphyseal regions of long bones and halberd-shaped pelvis. Scoliosis progressed and he evolved to short-trunk dwarfism. When he was 10 years old, he developed gait disturbance gradually due to muscle weakness of lower extremities. He was examined at the age of 15 years. Motor nerve conduction velocity was reduced to 21 m/sec in left median nerve and 18.5 m/sec in left peroneus nerve. Needle EMG showed neurogenic pattern. We performed sural nerve biopsy and obtained histopathological findings. Fiber density of myelinated axons decreased. Electron microscopic examination revealed onion bulb formation surrounding a myelinated fiber and a storage in the rough-surfaced endoplasmic reticulum of Schwann cell. These inclusions were similar to those of cartilage of his long bone. We supposed that the neuropathy would have relation to this bone dysplasia.

The intramembranous particle (IMP), orthogonal array (OA) and orthogonal array subunit particle (OASP) densities in skeletal muscle plasma membranes from eight patients with Becker*s muscular dystrophy (BMD) were analysed by the freeze–fracture technique. The results showed almost normal IMP density with the significant decrease of OA and OASP densities in BMD. The group mean densities ± SE of IMPs on the protoplasmic faces with and without OASPs, and on extracellular faces/μm 2 were 2137 ± 207, 1839 ± 68 and 895 ± 108, respectively in controls; whereas those of BMD were 1989 ± 259, 1837 ± 203 and 900 ± 239, respectively ( P > 0.1 by two–tailed t –test). The group median density of OAs and their pits/nm 2 was 4.89 with mid–ranges (25˜75% values of the counts) of 2.66 ˜ 10.18 in controls; whereas that in BMD was 2.15 with mid–ranges of 1.14 ˜ 4.31 ( P < 0.01 by Wilcoxon rank–sum test). The group mean density ± SE of OASPs in controls was 15.99 ± 1.83; whereas that in BMD was 13.47 ± 1.07 ( P < 0.01 by two–tailed t –test). However, the diminution of OA and OASP densities in BMD muscle plasma membranes was not as severe as in Duchenne's muscular dystrophy. There was a relationship between OA density and clinical severity in BMD patients; the decrease of OA density in a severe BMD patient was more marked than that in mildly affected BMD patients. Therefore, it seems that marked depletion of OA density may lead to the severe disability in muscular dystrophies.

Fukuyama type congenital muscular dystrophy (FCMD) is an autosomal recessive severe muscular dystrophy associated with an anomaly of the brain. Twenty-one FCMD families, 13 of them with consanguineous marriages, were analysed by genetic linkage analyses with polymorphic microsatellite markers to map the FCMD gene. Significant lod scores were obtained with the markers D9S58 (Zmax = 5.81 at theta = 0.06), D9S59 (Zmax = 4.33 at theta = 0.02), and HXB (Zmax = 3.28 at theta = 0.09) on chromosome 9q31-33. Multipoint analysis placed FCMD between D9S58 and D9S59, with a maximum lod score of 16.93. These markers will be useful for presymptomatic, prenatal and carrier diagnosis of family members carrying FCMD, and they represent important resources for the identification of a gene responsible for FCMD.

Congenital muscular dystrophy (CMD) is a concept applied to infants showing muscular weakness and hypotonia at birth, with myopathic changes which are histopathologically similar to those of muscular dystrophy. Patients with Fukuyama-type CMD (FCMD), characterized by progressive muscular dystrophy, mental retardation and occasionally, convulsions, are more frequently seen in Japan than those with non-Fukuyama type CMD (NFCMD). FCMD has been regarded as a distinct clinical and pathological entity, although the nosologic status of CMD is still controversial. A 24-year-old man had exhibited hypotonia and weakness at birth and delay in early development. During childhood, his muscular weakness improved, and he rode a bicycle and enjoyed skiing. However, his strength began to deteriorate at the age of 19 years. Neurological examination on admission revealed prominent muscular wasting and weakness, predominantly in the proximal limbs. He had ocular involvement (corneal opacity and slow saccades), sensorineural deafness, and a high-arched palate, saddle nose and funnel chest as anomalous conditions. Serum CK was moderately elevated and EMG showed myogenic patterns. A muscle biopsy specimen of the left biceps brachii was dystrophic, showing increased variation in fiber size with fibrous tissue proliferation, an increased number of centralized nuclei, fiber splitting and degenerating/regenerating fibers. Those findings were compatible with those seen in NFCMD. In Japan, only one patient with NFCMD who was followed to adulthood has been reported. This patient's symptoms progressed very slowly. The present patient's course of illness was stable during childhood but progressive in early adulthood. It suggests heterogeneous clinical expression of the disease.(ABSTRACT TRUNCATED AT 250 WORDS)

The analysis of dystrophin in skeletal muscles was performed to identify Duchenne and Becker muscular dystrophy (DMD and BMD) by means of immunohistochemical stain and Western blotting with antisera against synthetic dystrophin peptides. The control muscle specimens derived from normal healthy persons, and patients without DMD and BMD revealed clearly continuous stains of dystrophin at surface membrane. A band with 400 kDa of molecular size by Western blotting was positively stained by anti-dystrophin antibodies. The muscle specimens from eleven DMD patients showed no observation both in the band on Western blotting and in the immunohistochemical staining of dystrophin on frozen-thin sections. BMD muscle specimens showed patchy and faint stains, but no detection of any band on Western blotting except a 380 kDa minor band with anti-peptide IX antibody in one patient muscle. The immunohistochemical procedure was found to be more sensitive than Western blotting for the detection of dystrophin. These results indicate that the dystrophin analysis by both methods is an useful tool for the differential diagnosis of patients with DMD and BMD.

The activities and contents of the lysosomal cysteine proteinases cathepsins B, H and L were examined in xenografts of biopsied muscles transplanted from age-matched normal subjects and Duchenne-muscular-dystrophy (DMD) patients into nude mice. The activity of cathepsin B increased 9-fold and that of B-plus-L increased 24-fold in the first week after transplantation in normal muscle xenografts. By the third week, the activity of cathepsin B increased a total of 20-fold and B-plus-L increased to 36-fold the original level. The activity levels of cathepsin B, B-plus-L, H and D, and acid phosphatase in normal and DMD xenografts were not significantly different when compared 2 weeks after transplantation. However, the protein content of cathepsin B in DMD muscle xenografts was more than 3-fold that of normal xenografts at 2 weeks. The profile of cathepsin H activity in normal muscle xenografts was different than those of cathepsins B and B-plus-L. In the first week, the cathepsin H diminished sharply to about one-third of the biopsied muscle level and then, by 3 weeks after transplantation, it had increased slightly to about half the original level. The amount of endogenous cysteine-proteinase inhibitor changed in parallel with the activity of cathepsins B and B-plus-L. Cathepsins B and H, but not cathepsin L, were found immunohistochemically in regenerating muscle fibres of normal and DMD xenografts 2 weeks after transplantation. Staining of cathepsin B in DMD xenografts was slightly stronger than that in normal subjects. There was no immunostaining in degenerating or necrotic muscle fibres 2 weeks after transplantation. Western-blot analysis revealed that the cathepsin B band at 29 kDa was increased in normal xenografts 2 and 3 weeks after transplantation. Also, 2 weeks after transplantation the staining intensity of this band was slightly stronger in DMD xenografts than in normal xenografts. These results suggest that cathepsin B participates in the regeneration of transplanted muscle, both normal and DMD, and in the DMD muscle fibre-wasting processes, during regeneration.

Polyneuropathy was found in a patient with the Walker-Warburg syndrome. The most dominant features were the presence of extremely and tortuously proliferated myelin sheaths, the most of which having no neurofilaments and neurotubules. The other peculiar findings were the presence of microfilaments in Schwann cell cytoplasms, which were very similar to neurofilaments, and the presence of partial and abrupt disappearance of myelin sheaths. The severity of neuropathy was variable among nerve bundles, and a few nerve bundles looked normal on light microscopy. The above-mentioned lesions did not suggest the degeneration and/or regeneration of normally developed nerve fibers. We could not conclude the pathogenesis of this neuropathy, however, it was logical to consider that they reflected dysplastic myelination due to Schwann cell dysmaturity as well as the cerebral dysplasia.

The diaphragm muscle pathology in four patients with Fukuyama type congenital progressive muscular dystrophy (FCMD) was reported. In the diaphragm muscle fibers of three patients aged more than 14 years exhibiting chronic respiratory failure, a lot of electron dense lesions, which varied in size but did not extend over the whole length of the muscle fibers, and a marked increase in mitochondria were observed as well as the dystrophic changes. The dense lesions, consisting of electron dense fibrillary material comparable to Z-band materials in electron density, seemed to be due to Z-band disruption leading to streaming and/or large aggregations of Z-band materials. No mitochondria or other microorganelles were found in these dense lesions. These findings are thought not to be specific to FCMD, but seem to reflect diaphragm muscle fatigue, because, there were no such lesions in the diaphragm muscle of a 2-year-old infant not exhibiting chronic respiratory failure or in muscle at other sites in all patients.

We synthesized 3 peptide fragments predicted by residues 2354–2368 (peptide I), 2310–2324 (peptide II) and 2255–2269 (peptide III) on the mid-portion of the human dystrophin cDNA map where the most frequent intragenic deletions occurred in Duchenne muscular dystrophy. Rabbit antibodies against these peptides were raised and cryosections of 47 biopsied muscles were studied immunohistochemically. The 47 biopsied muscles included the quadriceps femoris muscles of 8 Duchenne muscular dystrophy patients, 8 child and 5 adult normal controls, 1 facioscapulohumeral dystrophy, 2 limb girdle dystrophy, 3 myotonic dystrophy, 3 polymyositis, 1 mitochondrial myopathy, 1 nemaline myopathy, 3 amyotrophic lateral sclerosis and the extensor digitorum longus muscles of 6 mdx mice (C57BL/10ScSn-mdx) and 6 normal control mice (C57BL/10ScSn). The peptide I antiserum continuously stained the myofiber surface membranes in 8 child and 5 adult normal control muscles, and in 14 other muscles from various neuromuscular diseases, but failed to stain the surface membranes in normal control mice. The surface membranes of 8 Duchenne muscles were not stained by the peptide I antiserum except for a few myofibers. Although the ELISA titers of peptide I, II and III antibodies were high, immunostaining by peptide II antiserum showed no reaction in the myofibers of any of the biopsied muscles, and immunostaining by peptide III antiserum revealed faint reactions on the myofiber surface membranes of all biopsied muscles, including the mdx control mouse muscles except for the Duchenne and mdx myofibers.

We used polyclonal antibodies against dystrophin for the immunohistochemical localization of this protein in human skeletal muscle. Dystrophin was localized in the sarcolemma of the myofibers in 8 infantile and 11 adult normal control muscles and in 10 early stage patient muscles with amyotrophic lateral sclerosis (ALS). The protein was absent or markedly decreased in 8 early stage patients with Duchenne muscular dystrophy (DMD). Moreover the densities of sarcolemmal plasma membrane assemblies, orthogonal arrays and their pits were estimated by freeze-fracture electron microscopy studies in the same number of muscle samples in each disease and control case. The group median densities of orthogonal arrays and their pits in the ALS group and adult control group were 4.8 with a midrange of 1.1-13.5 (25-75%) and 7.5 with a midrange of 2.3-12.9, respectively (P greater than 0.1, Wilcoxon rank-sum test), whereas those of the DMD group and child control group were 0 with a midrange of 0-1.1 and 10.8 with a midrange of 5.4-16.7 respectively (P less than 0.01). The skeletal muscles of mdx mice and their controls were also investigated by the same techniques. In mdx mice, the absence or marked deficiency of dystrophin was also noted; however, the decrease of orthogonal arrays was not as severe as in DMD, which might relate to the milder clinical features in mdx mice as compared with those in DMD.