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Biomedical subjects

T Voit

Publications and source records attributed to T Voit.

At least 109 records · Page 6Linked to original sources
PubMed1994

Multisystem triglyceride storage disorder without ichthyosis in two siblings.

A four-year-old boy presented with hepatomegaly, vacuolized granulocytes (Jordans' anomaly) and slightly progressive myopathy as signs of multisystem triglyceride storage disease. The nine-year-old sister of the patient also showed Jordans' anomaly and early fatigability, but no overt weakness. Biochemical analysis revealed normal values for carnitines, carnitine palmityl transferase in serum and striated muscle, and beta-oxidation enzymes in striated muscles. Distribution of non-membrane-bound lipids in granulocytes, fibroblasts, smooth muscle cells and striated muscle was compatible with Chanarin-Dorfman syndrome. In contrast to Chanarin-Dorfman syndrome, our patients lacked congenital ichthyosis.

Child↗
PubMed1993

Serpentine fibula--polycystic kidney syndrome and Melnick-Needles syndrome are different disorders.

We report on the third patient with serpentine fibula-polycystic kidney syndrome. Main features in the three reported cases were growth retardation, abnormal face, hirsutism, short neck, bowed forearms and lower legs due to bowed radii and elongated serpentine fibulae, and metatarsus adductus. Two patients including our own were deaf. All were mentally normal, all were female and sporadic. In addition, we report on a girl with Melnick-Needles syndrome and illustrate the similarities and differences between these syndromes.

Child↗
PubMed1993

Demonstration of Borrelia burgdorferi infection in a child with Guillain-Barré syndrome.

A 4.5-year-old child suffered from rapidly evolving motor weakness with paresthesia and radicular pain in both legs, accompanied by an isolated elevation of protein levels in CSF. Isoelectric focusing revealed oligoclonal IgG produced in the cerebrospinal compartment only. The diagnosis of Guillain-Barré syndrome was confirmed by electrophysiological studies. High antibody titres against Borrelia burgdorferi in the serum and specific antibodies in the CSF were demonstrable by ELISA and immunoblotting. B. burgdorferi specific DNA fragments were demonstrated in urine and CSF by means of a nested polymerase chain reaction (PCR), thus providing the borrelial aetiology and indicating B. burgdorferi infection. Complete recovery was observed after treatment with high dose immunoglobulin and ceftriaxone and control urine specimens were PCR negative.

Antibodies, Bacterial↗
PubMed1993

Ultrasound measurement of quadriceps muscle in the first year of life. Normal values and application to spinal muscular atrophy.

Using real-time ultrasound imaging normal values were obtained for quadriceps muscle thickness and subcutaneous tissue depth in the first year of life from 120 normal infants. These values were corrected for weight and height by introduction of a "correcting factor". In addition, a "modified muscle index" was calculated by multiplying the ratio of muscle to subcutaneous tissue thickness with the correcting factor and showed a steady increase from birth (mean 2.1) to the end of the first year (mean 4.8). The study of 12 patients with spinal muscular atrophy type I (SMA I) revealed that 9 out of 12 SMA I patients failed to reach the 3rd percentile for the muscle to subcutaneous tissue ratio and 10 out of 12 were well below the 3rd percentile for the modified muscle index due to their muscle atrophy. Only the two youngest SMA I patients aged 4 and 6 weeks reached values on the 3rd percentile. In contrast, 10 patients with myopathy and one patient with holoprosencephaly showed values within the normal percentiles even in the presence of severe clinical muscle weakness and signs of atrophy on muscle histology. In the differential diagnosis of early onset myopathy, atrophy of the quadriceps muscle during the first months of life in the absence of markedly increased echodensity seems to be a pathognomonic finding for SMA.

Body Weight↗
PubMed1993

[High-dose immunoglobulin treatment of epilepsy in children].

High-dose, intravenously administered immunoglobulins have been successfully applied to a few cases of childhood epilepsy and led to a reduction of the seizure frequency in a number of studies. In the present study 4 patients with myoclonic-astatic petit mal or myoclonic absence were treated with intravenously administered immunoglobulins (400 mg/kg for 5 days). Deterioration occurred in 1 patient, 1 patient showed no effect, and 2 patients showed a partial and transient response. Theoretically, the rationale for immunoglobulin therapy in epilepsy is based on the assumption of autoimmune mechanisms as being the underlying pathogenesis. However, a review of the literature showed that the few studies available differ in the forms of epilepsy treated and the effects obtained. No study correlated the effects of immunoglobulin administration with a presumptive autoimmune disorder. As a result, high-dose intravenous immunoglobulin treatment of childhood epilepsy remains empirical and the group of patients who might benefit from such a treatment continues to be poorly defined.

Anticonvulsants↗
PubMed1992

Somatic mosaicism for a deletion of the dystrophin gene in a carrier of Becker muscular dystrophy.

Duchenne muscular dystrophy (DMD) and the allelic milder form of Becker muscular dystrophy (BMD) are caused by mutations of the dystrophin gene on the short arm of the X chromosome. One third of affected individuals are expected to result from de novo mutations. Genetic counselling of families with sporadic cases is complicated by the potential meiotic origin of the mutation in the mother resulting in germline mosaicism. Here we present direct evidence for combined somatic and germline mosaicism for a deletion of the dystrophin gene, thereby proving the mitotic origin of this deletion and pinpointing a further potential pitfall for genetic counselling. The mother of a BMD son and a BMD carrier daughter, both carrying a deletion of dystrophin cDNA 7 (0.5 kb Hind III fragment) and cDNA 8, was herself clinically healthy and had normal creatine kinase levels. A muscle specimen of the mother showed mild overall pathology as well as focal dystrophin deficiency. In contrast chromosomal in situ suppression (CISS) hybridization of metaphase chromosomes using a cosmid clone of the corresponding cDNA deleted in her son revealed no evidence of somatic mosaicism in their lymphocytes. These results emphasize the value of an approach correlating genetic and immunological data for the definition of a carrier state in BMD or DMD. The possibility of somatic mosaicism should be considered when genetic counselling of a family with a sporadic case of BMD or DMD is performed.

Blotting, Southern↗
PubMed1992

Multipoint linkage mapping of the Emery-Dreifuss muscular dystrophy gene.

The clinical features to establish the diagnosis of X-linked Emery-Dreifuss muscular dystrophy (EMD) were recently redefined at the European EMD workshop in Baarn 1991. These criteria were used to select families from the literature and two new families for linkage analysis with the DNA markers F9, DX52, DXS15, F8C and DXS115. Recombinations are observed with the DNA markers F9, DXS52 and DXS15. No recombinations were found with F8C and DXS115. Multipoint linkage analysis indicates with a maximum location score of 73.9 that the EMD locus maps very close to F8C.

Adult↗
PubMed1992

Sudden loss of hearing and vestibular function, muscular weakness, and multiple white matter lesions in preschool children.

Sudden cochlear hearing loss, occurring successively or simultaneously in both ears, was observed in four unrelated preschool children. Vestibular testing could be carried out in three patients and showed complete bilateral loss of function. All patients had a mildly retarded motor development due to nonprogressive muscular weakness. On MR imaging all patients showed multiple periventricular and subcortical white matter lesions. These lesions were not clearly progressive in one patient examined repeatedly over 6 years. Virological, bacteriological, immunological, and metabolic examinations were normal in all patients. Muscle biopsy showed morphologically abnormal mitochondria in two and lipid storage in one patient. No indications have been found for a disturbed functioning of the muscle mitochondria. The identical pattern and course of the disease in these patients suggests a new nosological entity, the aetiology of which can only speculatively be attributed to a vascular process associated with a mitochondriopathy.

Biopsy↗
PubMed1992

Direct visualization of the dystrophin network on skeletal muscle fiber membrane.

Dystrophin, the protein product of the Duchenne muscular dystrophy (DMD) gene locus, is expressed on the muscle fiber surface. One key to further understanding of the cellular function of dystrophin would be extended knowledge about its subcellular organization. We have shown that dystrophin molecules are not uniformly distributed over the humen, rat, and mouse skeletal muscle fiber surface using three independent methods. Incubation of single-teased muscle fibers with antibodies to dystrophin revealed a network of denser transversal rings (costameres) and finer longitudinal interconnections. Double staining of longitudinal semithin cryosections for dystrophin and alpha-actinin showed spatial juxtaposition of the costameres to the Z bands. Where peripheral myonuclei precluded direct contact of dystrophin to the Z bands the organization of dystrophin was altered into lacunae harboring the myonucleus. These lacunae were surrounded by a dystrophin ring and covered by a more uniform dystrophin veil. Mechanical skinning of single-teased fibers revealed tighter mechanical connection of dystrophin to the plasma membrane than to the underlying internal domain of the muscle fiber. The entire dystrophin network remained preserved in its structure on isolated muscle sarcolemma and identical in appearance to the pattern observed on teased fibers. Therefore, connection of defined areas of plasma membrane or its constituents such as ion channels to single sarcomeres might be a potential function exerted by dystrophin alone or in conjunction with other submembrane cytoskeletal proteins.

Actinin↗
PubMed1992

Adult polyglucosan body myopathy.

This report describes a sporadic late-onset myopathy in two unrelated adults which was marked by polyglucosan inclusions surrounded by abnormally structured mitochondria, the latter finding a localized, possibly reactive phenomenon. The polyglucosan material was characterized by a battery of histochemical and enzyme histochemical techniques; revealed common antigenicity with Lafora bodies, corpora amylacea and muscle fiber inclusions in types IV and VII glycogenoses; and contained ubiquitin. Additional lectin histochemical and associated digestion preparations disclosed the presence of alpha-glycosyl residues as apparently the sole carbohydrate component in polyglucosan bodies while the above mentioned common antigenicity with Lafora bodies and other inclusions suggests an additional, so far unidentified, protein component.

Atrophy↗
PubMed1991

A homologue of dystrophin is expressed at the neuromuscular junctions of normal individuals and DMD patients, and of normal and mdx mice. Immunological evidence.

Polyclonal and monoclonal antibodies, which recognize different regions and epitopes of the dystrophin molecule, bind to a protein of Mr 400,000 which is present in extracts of mdx muscle from regions which contain neuromuscular junctions (NMJ) and is absent from those which do not. This NMJ-associated homologue of dystrophin has at least 2 epitopes which are different to usual Xp21 form of dystrophin expressed along the sarcolemma of muscle fibres in normal muscles. This protein is also expressed at the NMJ of a DMD patient who lacks the first 52 exons of the Xp21 dystrophin gene and it must therefore be translated from a different gene transcript.

Animals↗
PubMed1991

Spontaneous regression of a temporal arachnoid cyst.

Surgery is considered to be the standard therapy for arachnoid cysts (ACs). We report the case of a 13-year-old boy in whom a right temporal AC disappeared spontaneously over a period of 10 years. Bulging of the right temporal skull led to the detection of the cyst by computed tomography (CT) scan at the age of 3 years. There were no other clinical symptoms. Subsequent CT scans showed spontaneous regression of the cyst without surgical intervention. The question as to how ACs should be treated is discussed.

Adolescent↗
PubMed1991

Myopathy in Williams-Beuren syndrome.

Williams-Beuren syndrome (WBS) is a disorder of unknown aetiology. The classical features of the syndrome include a typical ('elfin') facies, mental retardation and heart defects. Myopathy has not so far been part of the spectrum of WBS. We studied six patients with WBS aged 3-25 years, five of whom showed clinical and morphological evidence of myopathy. The clinical manifestations of myopathy included hypotonia in infancy, walking delay, joint contractures, scoliosis, and increased exhaustion on exertion. These symptoms were present in variable expression but part of a typical postural pattern. Examination of muscle biopsies showed lipid storage in four patients and increased variability of fibre size in three. In one patient a muscle biopsy gave normal results. Biochemical investigation in four patients with morphological evidence of lipid storage in muscle revealed muscle carnitine deficiency in three. In addition, enzyme activities of fatty acid beta-oxidation were low in one of two specimens tested. It is concluded that a clinically relevant myopathy is part of the multi-system manifestation of WBS and a clinical trial of carnitine supplementation is justified.

Adult↗
PubMed1991

Dystrophin as a diagnostic marker in Duchenne and Becker muscular dystrophy. Correlation of immunofluorescence and western blot.

Dystrophin is the gene product of the Duchenne (DMD) and Becker (BMD) muscular dystrophy gene locus on the short arm of the X chromosome. Complete lack of dystrophin is pathognomonic for DMD and variable changes of the molecule may be observed in the milder allelic form of BMD. In the present study the two methods available for dystrophin assessment, immunofluorescence detections on cryosections (IF) and Western blotting (WB) were systematically compared using polyclonal and monoclonal antibodies to various regions along the dystrophin molecule. A total of 95 patients with DMD or BMD were investigated including two female patients. Dystrophin assessment revealed abnormal abundance and/or distribution in all 95 patients with DMD or BMD. Only trace amounts of dystrophin were detected in 29% of the DMD patients and complete lack of dystrophin was found in 71%. In two females with DMD but with normal karyotype single dystrophin-positive fibres were found among more than 90% negative fibres. Out of 26 patients with BMD 19 (73%) had a dystrophin molecule of abnormal molecular weight. The results of IF were largely compatible with those from WB but differences were also observed, e.g. one barely symptomatic BMD patient with dystrophin of increased molecular weight showed normal IF. Out of four carriers of BMD three showed evidence of reduced dystrophin immunostaining in some muscle fibres. In 20 other patients limb girdle muscualar dystrophy with "Duchenne-like" or "Becker-like" phenotype was suspected because dystrophin showed normal abundance and distribution. Focal discontinuity of muscle cell-surface dystrophin staining was observed in one patient with a congenital, autosomal recessive muscular dystrophy and in one out of five patients with polymyositis/dermatomyositis. The study emphasizes the need for, and value of, dystrophin assessment in every case of suspected BMD or DMD.

Adolescent↗
PubMed1991

Xp21 dystrophin and 6q dystrophin-related protein. Comparative immunolocalization using multiple antibodies.

A protein of Mr 400 K and slightly lower Mr than Xp21 dystrophin was detected in skeletal muscle from patients with Duchenne muscular dystrophy by three antibodies raised against the midrod and C-terminal portions of chicken dystrophin, and by antibodies to dystrophin-related protein. Immunocytochemistry showed continuous sarcolemmal staining of Duchenne muscle with these antibodies. Subcellular localization to the inner face of the plasma membrane of Duchenne muscle was demonstrated by immunoelectron microscopy using the model of a Duchenne patient deleted for most of the dystrophin gene. Other antibodies were specific for Xp21 dystrophin. In conclusion, a dystrophin homologue that may be identical to the previously described dystrophin-related protein (DRP)1 is expressed in Duchenne muscle with intracellular distribution similar to Xp21 dystrophin in normal muscle.

Antibodies, Monoclonal↗
PubMed1989

Distribution of dystrophin, nebulin and Ricinus communis I (RCA-I)-binding glycoprotein in tissues of normal and mdx mice.

Dystrophin, the protein product of the Duchenne muscular dystrophy (DMD) gene locus, appeared as an immunoreactive triplet of polypeptides in striated muscle tissues from normal mice on Western blot analysis. In smooth muscle tissues, an immunoreactive doublet of corresponding molecular weight was detected. No dystrophin was found in normal mouse brain, not even after enrichment for the Triton X-100 insoluble fraction. Dystrophin was absent from all corresponding tissues from the mdx mutant mouse strain which is known to lack dystrophin. The possibility that these immunoreactive bands represent isoforms is discussed. We have also investigated two other high molecular weight proteins which show secondary abnormalities in DMD muscle, namely nebulin and the 370 kDa Ricinus communis I lectin (RCA I)-binding glycoprotein. Nebulin levels were reduced in skeletal muscle from 6-week-old mdx mice but not in oesophagus from the same animals. By contrast, the RCA I-binding 370 kDa glycoprotein which is greatly reduced in DMD skeletal muscle was present in normal amounts in mdx skeletal muscle. These findings show, for the first time, that mdx myopathy differs from DMD myopathy not only morphologically, but also in its secondary biochemical abnormalities.

Animals↗
PubMed1989

[Membrane changes in Duchenne/Becker muscular dystrophy: lectin binding and localization of dystrophin].

An RCA I-lectin binding glycoprotein of Mr = 370 kD is missing from or altered in the plasma membrane of Duchenne muscular dystrophy (DMD) skeletal muscle. In the present study the carbohydrate chain of this glycoprotein was localized to the external face of the plasma membrane in human skeletal muscle, and dystrophin, the protein product of the DMD gene, was localized to the inner (cytoplasmic) face. On double labelled Western blots the two proteins appeared as closely apposed but distinctly separate bands. Comparison of the plasma membrane binding of five lectins with overlapping sugar specificities in skeletal muscle from patients with DMD and the allelic milder disease form, Becker muscular dystrophy (BMD) showed that the RCA I-binding glycoprotein also strongly binds to phytohaemagglutinin, thereby largely characterising the carbohydrate binding site. This glycoprotein was absent or altered in DMD and markedly reduced in clinically manifest BMD but present in preclinical clinical BMD. There was no general depletion of plasma membrane glycoproteins in DMD because consistent plasma membrane binding could be demonstrated by peanut and maclura pomifera lectin. The possible implications of these findings for the pathogenesis of DMD/BMD are discussed.

Adolescent↗