PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “MUSCULAR DISEASES”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 289 records · Page 16Linked to original sources
PubMed1989

Condylar cartilage in the muscular dystrophic mouse.

The adaptability of condylar cartilage has been demonstrated previously after experimentally created functional alteration. This study was undertaken to examine the morphology of condylar cartilage in animals affected with a progressive muscular disease. Muscular dystrophic male mice (genotype: dy/dy, dy/+ x dy/+, Jackson Laboratory, Maine) and corresponding unaffected control mice were decapitated at ages 3, 6, 9, and 12 weeks, and their heads processed for histology. The cellular morphology of the condylar cartilage in the youngest age group was similar in dystrophic and control mice: the cartilage was a hypertrophic type. At ages 6 and 9 weeks, the maturational progression toward the nonhypertrophic form was observed in the dystrophic and control groups, the latter having flatter condylar heads. Differences were still evident at age 12 weeks. These observations were supported by measurements of the ratios of the mean cartilage thickness to condylar width (c/w), mean condylar height to width (h/w), and mean cartilage thickness to condylar height (c/h). This study supports the hypothesis that the adaptive nature of condylar cartilage may be regulated by the force levels to which the condyle is subjected.

Animals↗
PubMed1978

Isoenzyme distribution of creatine kinase and lactate dehydrogenase in serum and skeletal muscle in Duchenne muscular dystrophy, collagen disease, and other muscular disorders.

We determined the total activity and isoenzyme distribution of lactate dehydrogenase and creatine kinase in serum and biopsy specimens from skeletal muscle of nine normal individuals and nine patients with Duchenne muscular dystrophy (I), five with collagen disease (II), and four with non-progressive unclassified myopathy (III). Mean total serum creatine kinase in patients with Duchenne muscular dystrophy (867 U/liter, SD = 197) was 31-fold that in the control group (28 U/liter, SD = 14). There was also a small (3.3-fold) increase in the mean total serum creatine kinase of patients with III, but none in the serum from patients with II. Changes in the creatine kinase isoenzyme distribution of skeletal muscle were primarily in the MB isoenzyme. The mean percentage of creatine kinase-MB activity in muscle from patients with I (2.81, SD = 1.15) and patients with III (1.69, SD = 1.07) significantly (P less than 0.005) exceeded that of the control group (0.43, SD = 0.18). Muscle from patients with II showed little change. The most striking changes in lactate dehydrogenase were also observed in patients with I, in whom the mean total serum activity (356 U/liter, SD = 115) was 3.4-fold that of serum from the control group (105 U/liter, SD = 19). Skeletal muscle from these patients also showed a significant decrease in mean percent isoenzyme 5 activity (from 50 to 23) and an increase in that of isoenzymes 1 and 2 (from 1 to 9 and 8 to 20, respectively). These changes in the distribution of these two sets of isoenzymes in muscle were reflected in the serum.

Adolescent↗
PubMed2002

Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1.

Deletion or mutation of the SMN1 (survival of motor neurons) gene causes the common, fatal neuromuscular disease spinal muscular atrophy. The SMN protein is important in small nuclear ribonucleoprotein (snRNP) assembly and interacts with snRNP proteins via arginine/glycine-rich domains. Recently, SMN was also found to interact with core protein components of the two major families of small nucleolar RNPs, fibrillarin and GAR1, suggesting that SMN may also function in the assembly of small nucleolar RNPs. Here we present results that indicate that the interaction of SMN with GAR1 is mediated by the Tudor domain of SMN. Single point mutations within the Tudor domain, including a spinal muscular atrophy patient mutation, impair the interaction of SMN with GAR1. Furthermore, we find that either of the two arginine/glycine-rich domains of GAR1 can provide for interaction with SMN, but removal of both results in loss of the interaction. Finally, we have found that unlike the interaction of SMN with the Sm snRNP proteins, interaction with GAR1 and fibrillarin is not enhanced by arginine dimethylation. Our results argue against post-translational arginine dimethylation as a general requirement for SMN recognition of proteins bearing arginine/glycine-rich domains.

Amino Acid Substitution↗
PubMed2000

Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN).

The spinal muscular atrophy disease gene product (SMN) is crucial for small nuclear ribonuclear protein (snRNP) biogenesis in the cytoplasm and plays a role in pre-mRNA splicing in the nucleus. SMN oligomers interact avidly with the snRNP core proteins SmB, -D1, and -D3. We have delineated the specific sequences in the Sm proteins that mediate their interaction with SMN. We show that unique carboxyl-terminal arginine- and glycine-rich domains comprising the last 29 amino acids of SmD1 and the last 32 amino acids of SmD3 are necessary and sufficient for SMN binding. Interestingly, SMN also interacts with at least two of the U6-associated Sm-like (Lsm) proteins, Lsm4 and Lsm6. Furthermore, the carboxyl-terminal arginine- and glycine-rich domain of Lsm4 directly interacts with SMN. This suggests that SMN also functions in the assembly of the U6 snRNP in the nucleus and in the assembly of other Lsm-containing complexes. These findings demonstrate that arginine- and glycine-rich domains are necessary and sufficient for SMN interaction, and they expand further the range of targets of the SMN protein.

Amino Acid Sequence↗
PubMed1983

[A forgotten muscular dystrophy: Ullrich's disease].

The muscular disease described by Ullrich (1930) is no longer included in classifications of neuromuscular disorders. A typical case is reported and 15 documented cases have been found in the German and Japanese literature. The clinical picture associates, paradoxically, retraction of proximal muscles and hyperlaxity of distal muscles and joints. The dystrophic nature of the disease is uncertain.

Adolescent↗
PubMed1981

[Hodgkin's disease with muscular involvement. 2 cases (author's transl)].

The authors report on two cases of Hodgkin's disease with muscular involvement. This exceptional complication occurred during the terminal phase of a stage IV disease in one case and during remission of a stage III disease in the other case, where it responded to combined chemotherapy. Muscular lesions in Hodgkin's disease may be due to extension from adjacent tissues or from dissemination through the blood stream. They do not necessarily indicate a more severe prognosis.

Adolescent↗
PubMed1993

The gastroenterologist's approach to dysphagia.

In the gastroenterological diagnostic armamentarium, dysphagia is considered as an important symptom for diseases of the esophagus. Concerning the history of illness, symptoms such as retrosternal pain and heartburn are often associated with gastroesophageal reflux disease. Morphological changes of the mucosa can be diagnosed by flexible endoscopy and radiographic examinations. Investigation with 24-h pH monitoring, manometry, and pharmacological tests is necessary for the diagnosis of functional disorders. Additionally, dysphagia can be associated with multiple internal diseases, including muscular diseases such as dermatomyositis, progressive systemic sclerosis, as well as lupus erythematosus. Difficulties in swallowing associated with hypo- and hyperthyroidism can also be interpreted as muscular lesions. Metabolic disorders such as alcoholism, and diabetes mellitus can be the cause of dysphagia. Increasing importance in the differential diagnosis of dysphagia is attached to infections of the upper GI tract. Especially in immunocompromised patients, infections of Candida albicans, mycobacterias, herpes, varicella zoster, and cytomegaloviruses can produce dysphagia and odynophagia. The differential diagnosis of the "angina-like chest pain" has to differentiate between cardiac disease and a noncardiac genesis. Therefore, besides the cardiac diagnostic investigation, endoscopy, radiography, and manometry are often indicated.

Deglutition Disorders↗
PubMed2001

[Aldolase].

Aldolase (EC 4.1.2.13) plays an important role in glucose metabolism. Aldolase has a molecular weight of 160 kDa and has three isozymes, namely aldolase A, B and C. The enzyme is probably present in all cells; it occurs in particularly large quantities in the muscles, liver and brain. An increase in serum aldolase is found in myotonic muscular disease, such as progressive muscular dystrophy and polymyositis. The enzyme rises in myocardial infarction, reaches a maximum within 24-48 hours and returns to normal in the course of five days. In these muscular diseases, aldolase A isozyme is elevated. Aldolase activity, especially B isozyme, in serum rises to very high levels in acute hepatitis, but is slightly elevated in cirrhosis, chronic hepatitis and obstructive jaundice. Aldolase becomes elevated in serum with malignant tumors, and isozyme A is predominant in serum. Erythrocytes are also rich in aldolase, and the enzyme rises in hemolytic anemia.

Acute Disease↗
PubMed2003

Riluzole attenuates spinal muscular atrophy disease progression in a mouse model.

Spinal muscular atrophy (SMA) is a motor neuron disease caused by mutations of the survival motor neuron 1 gene (SMN1). No curative treatment is available. Mutant mice carrying homozygous deletion of Smn exon 7 directed to neurons display a degenerative process of motor neurons similar to that found in human SMA. To test whether riluzole, which exhibits neurotrophic properties, might have a protective role in SMA, mutant mice were treated with it after the onset of the degenerative process. Riluzole improved median survival and exerted a protective effect against aberrant cytoskeletal organization of motor synaptic terminals but not against loss of proximal axons. These results demonstrate that the disease course of SMA can be attenuated after the onset of neuromuscular defects and may warrant further investigation in a therapeutic trial in SMA.

Animals↗
PubMed2001

Statin induced myopathy does not show up in MIBI scintigraphy.

Statin induced myopathy is the most commonly seen side effect in users of this family of drugs. Their different forms present with either creatine phosphokinase (CK) elevation or not, signs of in vivo oxidation injury or not or a combination of both. The pathogenetic background, however, still remains obscure. As MIBI, beside myocardial and tumour scintigraphy, is useful in detecting muscle metabolic abnormalities, an increased uptake of MIBI in the diseased muscular segments could be expected. We investigated seven patients (five males, two females; aged 36-56 years) with statin induced myopathy with either elevated CK, isoprostanes or muscle pains at varying combinations. MIBI whole-body imaging was done immediately, the patients still being on the respective statin. Sixteen patients (six males, 10 females) suffering from lung or breast cancer and being on statins served as controls. No uptake abnormalities in any muscular segment either in the patients or the control group were seen. Thus, MIBI scintigraphy is not useful, apparently, in diagnosing and eventually localizing statin induced myopathy. These findings indicate that MIBI scintigraphy is of no help for diagnosis and gaining further insight into statin induced myopathy.

Adult↗