BACKGROUND: Recent genetic analyses have shown that Miyoshi myopathy (MM) is caused by a mutation in the DYSF, which induces the dysfunction of dysferlin. We identified the deficiency of dysferlin by immunohistochemistry and Western blot in four patients with clinically diagnosed MM, and investigated the clinical and pathological characteristics of MM. METHODS: A muscle biopsy was performed in four patients who were diagnosed with MM by clinical and electrophysiological study. Immunostaining of muscle specimens for dyferlin, dystrophin, alpha, beta, gamma, sigma-sarcoglycan, beta-dystroglycan, and caveolin-3 were performed in all four patients. We analyzed the quantitative analysis for dysferlin by Western blot in three of four patients. RESULTS: All four patients showed clinical onset during adolescence or early adulthood (15-26 year old), a slowly progressive course, and a relatively high serum creatine kinase level (2240-6400 IU/L). Routine pathological studies showed non-specific myopathic changes. On immunocytochemistry, there was negative immunoreacticity for dysferlin on muscle specimens in all patients. The immunoreactivities for dystrophin, alpha, beta, gamma, sigma-sarcoglycan, beta-dystroglycan, and caveolin-3 were normal. On Western blotting, complete loss of dysferlin was noted in all three patients with MM CONCLUSIONS: Identification of isolated deficiency of dysferlin on immunocytochemistry or Western blot is important for the confirmative diagnosis of MM.
Adolescent ; Biopsy ; Blotting, Western* ; Caveolin 3 ; Creatine Kinase ; Diagnosis ; Dystroglycans ; Dystrophin ; Humans ; Immunohistochemistry ; Muscular Diseases*

OBJECTIVETo investigate the expression of beta-dystroglycan (beta-DG) and the roles of tissue inhibitor of metalloproteinases (TIMPs) on beta-DG in salivary adenoid cystic carcinoma (SACC).

METHODSbeta-DG in highly lung metastatic cell line ACC-M and lowly lung metastatic one ACC-2 was tested by immunocytochemistry with different concentrations (10, 15, 20, 25 micromol x L(-1)) of TIMPs, and that without the regulation of TIMPs was served as controls. beta-DG was detected in seven specimens of SACC and ten cases of normal salivary gland tissues which were considered as a comparison group by immunohistochemistry.

RESULTSThere was no positive beta-DG immune-staining at the ACC-2 and ACC-M cell lines without TIMPs in the cell culture. beta-DG expressed after the regulation of TIMPs. beta-DG expression was localized predominantly in basement membrane of the acinus, while the negative results were distributed in the carcinoma cells and around the cancer cell nests.

CONCLUSIONBeta-DG is widely expressed by transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton, the fracture of this structure means that it is easy to invade and transfer, so restoration of beta-DG expression by TIMPs is considered to be critical for successful treatment of SACC.

Carcinoma, Adenoid Cystic ; Cell Line, Tumor ; Dystroglycans ; Humans ; Immunohistochemistry ; Salivary Gland Neoplasms ; Tissue Inhibitor of Metalloproteinases

It is well known that M. leprae involves peripheral nerves, but it is a few known that M. leprae involves craninal nerves. I experienced one case of relapsed leprosy accompanied by multiple cranial nerve palsies. Revealed symptoms are to involve trigeminal nerve (V). facial nerve (VII), vestibular nerve (VIII), glossopharyngeal nerve (IX), vagus nerve (X). It is not effect to treat with corticosteroid, but is good effect to treat with MDT(multiple drug therapy)
Cranial Nerve Diseases* ; Cranial Nerves* ; Dystroglycans ; Facial Nerve ; Glossopharyngeal Nerve ; Leprosy* ; Peripheral Nerves ; Trigeminal Nerve ; Vagus Nerve ; Vestibular Nerve

Walker-Warburg syndrome (WWS) is a rare autosomal recessive disorder characterized by congenital muscular dystrophy, brain (lissencephaly, hydrocephalus, cerebellar malformations) and retinal abnormalities, and is associated with mental retardation and seizures. In 1942, Walker was the first to report a case of WWS. As Fukuyama congenital muscular dystrophy or muscle-eye-brain disorder, it has been demonstrated that the glycosylation defects of alpha-dystroglycan which take a great role in muscle and neuron regeneration are at the root of these disorders. We report a five months old male patient who was presented with seizures as the chief complaint and was diagnosed with WWS, based on clinical criteria, MRI, muscular biopsy, ocular examination, and laboratory findings.
Biopsy ; Brain ; Dystroglycans ; Glycosylation ; Humans ; Hydrocephalus ; Intellectual Disability ; Lissencephaly ; Male ; Muscles ; Muscular Dystrophies ; Neurons ; Regeneration ; Retinaldehyde ; Seizures ; Walker-Warburg Syndrome

The muscular dystrophies are a diverse group of inherited muscle disorders characterized by progressive muscle weakness and wasting with characteristic histologic abnormalities such as degeneration, necrosis, and regeneration of muscle fibers. With progress in molecular genetics methods, new discoveries of dystrophin and related molecules have dramatically changed the understanding and diagnosis of a large group of muscular dystrophy patients. Dystrophin and its related molecular associates are tightly associated and form an essential cytoskeletal system (dystrophin-glycoprotein complex) at the muscle fiber surface membrane, which is critical for maintaining the integrity of the sarcolemma and muscle fibers. Deficiency of one of these sarcolemmal proteins, including dystrophin, dystroglycans, sarcoglycans, and laminin-2, leads to the breakdown and instability of muscle fibers and to clinically observed progressive muscle weakness. Identification of the molecular cause of muscular dystrophies would allow a genetic oriented classification and diagnosis using DNA or protein analysis. However, definition of the molecular pathogenesis of muscular dystrophies has not been completely possible until now. Future advances in this field should allow the exact diagnosis and treatment of muscular dystrophies.
Classification ; Diagnosis* ; DNA ; Dystroglycans ; Dystrophin ; Humans ; Membranes ; Molecular Biology ; Muscle Weakness ; Muscular Diseases ; Muscular Dystrophies* ; Myotonic Dystrophy ; Necrosis ; Regeneration ; Sarcoglycans ; Sarcolemma

BACKGROUND: For the differential diagnosis between the various subtypes of muscular dystrophy, the analysis of the protein expression pattern from the biopsied skeletal muscle tissue is essential. Authors performed the immunohistochemical study (IHC) using sets of antibodies for the differentiation of subtypes of muscular dystrophy. METHODS: Antibodies against dystrophin C-terminal, dystrophin rod domain, dystrophin N-terminal, alpha-, beta-, gamma-sarcoglycans, laminin alpha2 chain, dysferlin, and beta-dystroglycan were used for the IHC study in 43 patients with muscular dystrophy. The reactivity against the specific antibodies was graded and the clinical findings were assessed. RESULTS: We found 15 cases of dystrophin deficiency and 7 cases of dysferlin deficiency. Those with dystrophin deficiency were clinically classified previously as follows, 11 cases with Duchenne's muscular dystrophy (DMD), two with congenital muscular dystrophy (CMD), one with Becker's muscular dystrophy (BMD), and a female patient with limb-girdle muscular dystrophy (LGMD). Those with dysferlin deficiency consisted of 4 cases with LGMD phenotype and 3 with distal myopathy. CONCLUSIONS: The results of our study confirm the dystrophin immunostain is essential for the identification of dystrophinopathies among the various subtypes of muscular dystrophy. Also, the identification of 7 cases with dysferlin deficiency suggests dysferlinopathy is the common cause of muscular dystrophy in Korea.
Antibodies ; Diagnosis, Differential ; Distal Myopathies ; Dystroglycans ; Dystrophin ; Female ; Humans ; Immunohistochemistry ; Korea ; Laminin ; Muscle, Skeletal ; Muscular Dystrophies* ; Muscular Dystrophies, Limb-Girdle ; Muscular Dystrophy, Duchenne ; Phenotype ; Sarcoglycans