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Biomedical subjects

E Jenny

Publications and source records attributed to E Jenny.

At least 19 recordsLinked to original sources
PubMed2000

Prevalence of IgA antibodies to endomysium and tissue transglutaminase in primary biliary cirrhosis.

The association between celiac disease and primary biliary cirrhosis has been described in several case reports and small screening studies, with varying prevalence rates. Stored sera from 378 patients with primary biliary cirrhosis were tested for immunoglobulin (Ig) A endomysium and tissue transglutaminase antibodies. Ten patients were positive for both antibodies (2.6%); five of these patients had had small bowel biopsies confirming celiac disease. A further 44 patients (11.6%) had raised titres of IgA tissue transglutaminase antibody but were negative for IgA endomysium antibody. The increased prevalence of celiac-related antibodies in patients with primary biliary cirrhosis suggests that the two conditions are associated, although the reason for the association remains unclear. Patients with primary biliary cirrhosis should be considered to be at high risk for celiac disease. Although liver biochemistry does not improve when these patients are fed a gluten-free diet, the complications of untreated celiac disease warrant the identification and treatment of the condition in this population.

Celiac Disease↗
PubMed1990

Plasmid analysis and restriction fragment length polymorphisms of chromosomal DNA allow a distinction between Borrelia burgdorferi strains.

We examined the relationships of the genomes of five strains of Borrelia burgdorferi isolated from ticks, two from North America, including the type strain B31, and three from Switzerland. We determined restriction fragment length polymorphisms by using eight cloned DNA fragments as hybridization probes to genomic Southern blots. Two divergent patterns were observed, represented by B31 and one Swiss strain on the one hand and the two other Swiss strains on the other. The second American strain resembled B31. One of the DNA probes allowed distinction between the closely related strains within a group. The close resemblance of one Swiss strain to the North American strains suggests the possibility of their European origin. All five strains carried a circular plasmid of about 29 kb, and three contained an additional species of about 9 kb, both of which exhibited homology between the strains. The profiles of linear plasmids revealing species of 5.1 kb to 58 kb reflected the polymorphisms of chromosomal DNAs. Linear plasmids of similar size shared DNA sequence homology. Some of the smaller plasmids tended to become lost during cultivation.

Animals↗
PubMed1989

Progressive papillomatosis of the intrahepatic and extrahepatic bile ducts. Case report.

Papillomatosis of the bile ducts is uncommon, with only 26 cases in the available literature. The salient symptom is icterus, often with right-sided abdominal pain. Endoscopic retrograde cholangiography and percutaneous transhepatic cholangiography nowadays permit preoperative diagnosis. Complete removal should be the aim, because of the tendency to continuous growth, intrahepatic spread and malignant degeneration. Four cases are presented.

Adult↗
PubMed1988

A selection cartridge for rapid detection and analysis of spontaneous mutations including insertions of transposable elements in Enterobacteriaceae.

We present a method that allows positive selection and rapid analysis of mutations in Enterobacteriaceae. Mutations are detected in a 2630 bp selection cartridge inserted in two different bacterial multicopy plasmid vectors. Spontaneous mutations in Escherichia coli, Enterobacter cloacae and Citrobacter freundii include insertions, deletions and point mutations. The small size of the target sequence facilitates rapid analysis of DNA rearrangements by cleavage with restriction enzymes and of any type of mutation by DNA sequence analysis. While in E. coli insertions of the mobile elements IS1, IS2 and IS5 were readily found, insertions of putative new transposable elements were detected in Enterobacter cloacae. The selection cartridge can thus serve as a tool for studying the spectrum of insertion mutations in Enterobacteriaceae and probably other Gram-negative bacteria, and the dependency of this spectrum on physiological and environmental factors and the host's genetic background can be investigated.

Base Sequence↗
PubMed1983

Type-specific proteins of single IIM fibres from cat muscle.

The fibre type IIM, present in the jaw-closer muscles of the cat, has a characteristic form of myosin. To analyse other proteins present in IIM fibres and the usual types I, IIA and IIB, 14C-labelled typed single fibres were analysed by 2-dimensional gel electrophoresis. Whereas types I, IIA and IIB contained both alpha- and beta-forms of tropomyosin, IIM fibres contained only a single form, shown by 1-dimensional peptide mapping to be different from the tropomyosins present in the other fibre types. This single form of tropomyosin, and two soluble proteins seen only in IIM fibres, were also found in IIM fibre-containing muscles from other species, demonstrating that IIM fibres are a distinct type.

Animals↗
PubMed1982

No classical type IIB fibres in dog skeletal muscle.

To analyse the fibre type composition of adult dog skeletal muscle, enzyme histochemistry, immunohistochemistry for type I, IIA and IIB myosins, and peptide mapping of myosin heavy chains isolated from typed single according to the activity of the m-ATPase after acidic and alkaline preincubation proved to be rather difficult and was only consistently achieved after a very careful adjustment of the systems used. One of these sub-classes of type II fibres stained more strongly for m-ATPase activity after acidic and alkaline preincubation, was oxidative-glycolytic and showed a strong reaction with an anti-type IIA myosin. The other one, however, although showed a faint reaction with an anti-type IIB myosin. Peptide mapping of the myosin heavy chains of typed single fibres revealed two populations of heavy chains among the type II fibre group. Thus, in dog muscle, we are confronted with the presence of two main classes of type II fibres, both oxidative-glycolytic, but differing in the structure of their myosin heavy chains. In contrast to some reports in the literature, no classical type IIB fibres could be detected.

Adenosine Triphosphatases↗
PubMed1982

The tensor tympani muscle of cat and dog contains IIM and slow-tonic fibres: an unusual combination of fibre types.

Using recently developed highly specific antisera to the full range of known adult mammalian skeletal muscle myosins, an immunohistochemical and histochemical examination was made of the middle ear muscle tensor tympani in the dog and cat. Approximately half the fibres were of the IIM type and there was a substantial population of apparently slow-tonic fibres, both these types being rare in mammals. In addition, some type I but no IIA nor IIB fibres were detected. Moreover, as no multiple end-plate innervation, thought to be typical of slow-tonic fibres, could be demonstrated in this muscle by acetylcholinesterase staining or by Ruffini gold impregnation, it is suggested that in tensor tympani the slow-tonic fibres are focally innervated. The very short length of the fibres, only 1-2 mm, is probably sufficient to permit adequate depolarization of a whole fibre by a single centrally situated end-plate. The functional implications of this combination of very rare fibre types in tensor tympani are unclear at present.

Animals↗
PubMed1981

Analysis of myosin light and heavy chain types in single human skeletal muscle fibers.

In this study, myosin types in human skeletal muscle fibers were investigated with electrophoretic techniques. Single fibers were dissected out of lyophilized surgical biopsies and typed by staining for myofibrillar ATPase after preincubation in acid or alkaline buffers. After 14C-labelling of the fiber proteins in vitro by reductive methylation, the myosin light chain pattern was analysed on two-dimensional gels and the myosin heavy chains were investigated by one-dimensional peptide mapping. Surprisingly, human type I fibers, which contained only the slow heavy chain, were found to contain variable amounts of fast myosin light chains in addition to the two slow light chains LC1s and LC2s. The majority of the type I fibers in normal human muscle showed the pattern LC1s, LC2s and LC1f. Further evidence for the existence in human muscle of a hybrid myosin composed of a slow heavy chain with fast and slow light chains comes from the analysis of purified human myosin in the native state by pyrophosphate gel electrophoresis. With this method, a single band corresponding to slow myosin was obtained; this slow myosin had the light chain composition LC1s, LC2s and LC1f. Type IIA and IIB fibers, on the other hand, revealed identical light chain patterns consisting of only the fast light chains LC1f, LC2f and LC3f but were found to have different myosin havy chains. On the basis of the results presented, we suggest that the histochemical ATPase normally used for fibre typing is determined by the myosin heavy chain type (and not by the light chains). Thus, in normal human muscle a number of 'hybrid' myosins were found to occur, namely two extreme forms of fast myosins which have the same light chains but different heavy chains (IIA and IIB) and a continuum of slow forms consisting of the same heavy chain and slow light chains with a variable fast light chain composition. This is consistent with the different physiological roles these fibers are thought to have in muscle contraction.

Adenosine Triphosphatases↗
PubMed1981

Muscle beta-actinin and serum albumin of the chicken are indistinguishable by physicochemical and immunological criteria.

Chicken muscle beta-actinin is considered to be one of the "true" myofibrillar components due to its specific binding to isolated myofibrils. Surprisingly, the direct comparison of this muscle protein with serum albumin, both isolated from chicken, showed that they behaved identically under several electrophoretic conditions. Furthermore, immunoreplica gels and double-immunodiffusion tests with antibodies prepared against beta-actinin established the serological identity of both proteins. No significant differences were found by circular dichroic spectroscopy or in amino acid composition. In addition, the amino-terminal sequences of both proteins were identical (H2N-Asp-Ala-Glu-His-Lys-Ser-Glu-Ile-Ala-His-Arg-Tyr-Asn-Asp-Leu-). Combined, these results strongly indicate that muscle beta-actinin and serum albumin are similar, if not identical.

Actinin↗
PubMed1980

Myosin types in human skeletal muscle fibers.

By combining enzyme histochemistry for fiber typing with immunohistochemistry for slow and fast myosin a correlation between fiber type and myosin type was sought in human skeletal muscle. Fiber typing was done by staining for myofibrillar ATPases after preincubation at discriminating pH values. Myosin types were discriminated using type specific anti-rabbit myosin antibodies shown to cross-react with human myosin and were visualized by a protein A-peroxidase method. Type I fibers were shown to contain slow myosin only, type IIA and IIB fibers fast myosin only, and type IIC fibers both myosins in various proportions. When muscle biopsies from well-trained athletes were investigated essentially the same staining pattern was observed. However, rarely occurring type I fibers with high glycolytic activity were detected containing additional small amounts of fast myosin and occasional type IIA fibers had small amounts of slow myosin. Based on the observation of various fiber types in which slow and fast myosin coexist we propose a dynamic continuum of fibers encompassing all fiber types.

Adenosine Triphosphatases↗
PubMed1979

Fast and slow myosin within single skeletal muscle fibres of adult rabbits.

There is good evidence for the coexistence of different myosin types both in developing muscles and in Purkinje cells from adult chicken hearts. In skeletal muscle fibres of adult animals, however, coexistence of fast (FM) and slow (SM) myosin has only been demonstrated after long-term electrical stimulation. The term 'promiscuity' has recently been coined to describe the coexistence of different myosin isoenzymes within a single fibre. Using novel, refined immunological methods we demonstrate here the presence of both FM and SM within single fibres of the musculus tibialis anterior of adult rabbits. Essentially identical results were also obtained with other muscles. Our findings imply that the genes coding for FM and SM can be expressed simultaneously within the same cell throughout an animal's entire life, and not only during development or after artificial electrical stimulation.

Animals↗
PubMed1978

The size of the fibre populations in rabbit skeletal muscles as revealed by indirect immunofluorescence with anti-myosin sera.

Antibodies against myosin of the fast long. Dorsi and the slow soleus muscle of rabbits were induced in guinea pigs. With the aid of a new technique, the gel-electrophoresis-derived-enzyme-linked-immunosorbent assay (GEDELISA) it could be shown that they are directed against the heavy and the light chains of fast (M. long. dorsi) and slow (M. soleus) myosin. In the indirect immunofluorescence test each antiserum only stained one population of fibres in five different muscles tested. The single fibres were observed to react only with one of the two types of antisera. The following percentage of fibres showed a positive reaction with the anti-fast myosin serum: M. long. dorsi, 95%; M. psoa maior, 95%, M. psoa minor, 92%; M. tibialis ant., 90%; M. soleus, 15%.

Animals↗
PubMed1978

The influence of aging on the myosin type of the rabbit soleus and longissimus dorsi muscles.

The influence of aging on the myosin type, and on the fibre composition of both the slowly contracting ("red") M. soleus and the fast ("white") M. longissimus dorsi was examined in the rabbit. For myosin characterization isolated myofibrils were electrophoresed on SDS-polyacrylamide gels, and the fibre pattern within the respective muscles was analyzed with an immunocytochemical method. Antisera against either fast or slow rabbit myosin were collected from guinea pigs after longterm immunization. After incubation of the paraformaldehyde-fixed muscle thin sections the fibres containing either fast or slow myosin could be distinguished from each other by indirect immunofluorescence. The soleus muscles of 1 day old rabbits were composed of 25% slow and 75% fast fibres. In young-adult (5--8 mo.) rabbits the fibres were mostly slow (over 90%), while in old age (4--7 y.) again up to 50% of the soleus fibres contained fast myosin. In contrast, in the longissimus dorsi muscle constantly around 95% of the fibres contained fast myosin. In accordance with the immunocytochemical finding of an increase of fast fibres in the aging soleus muscle, the presence of fast myosin could also be demonstrated electrophoretically. With this method, soleus myofibrils from young-adult animals were observed to contain virtually slow myosin only. No slow, but only fast myosin was identified in SDS-gels of longissimus dorsi myofibrils at all ages. These results are discussed in relation to the well known metabolic alterations occurring in the mammalian skeletal muscle during aging.

Aging↗