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  • 1
    Electronic Resource
    Electronic Resource
    Human Liver Calreticulin: Characterization and Zn^2^+-Dependent Interaction with Phenyl-Sepharose
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 193 (1993), S. 611-616 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/bbrc.1993.1668
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  • 2
    Electronic Resource
    Electronic Resource
    The fast-twitch muscle calsequestrin isoform predominates in rabbit slow-twitch soleus muscle
    Amsterdam : Elsevier
    FEBS Letters 242 (1989), S. 297-300 
    Details
    ISSN: 0014-5793
    Keywords: Calsequestrin ; Slow-twitch muscle ; cDNA cloning
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(89)80488-0
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  • 3
    Electronic Resource
    Electronic Resource
    Distribution of sarcoplasmic reticulum Ca-ATPase and of calsequestrin in rabbit and rat skeletal muscle fibers (1986)
    Springer
    Histochemistry and cell biology 86 (1986), S. 63-69 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Muscle fibers in rabbit extensor digitorum longus (EDL), tibialis anterior (TA) and soleus, and rat soleus, were examined immunohistochemically for two proteins of the sarcoplasmic reticulum, Ca-ATPase and calsequestrin (CaS). Fibers were typed with the histochemical reaction for actomyosin ATPase. In the rabbit EDL and TA, type I fibers clearly reacted less for Ca-ATPase and CaS than type II fibers, but the difference was less with CaS than with Ca-ATPase. Although the differences were relatively small, HB fibers consistently presented greater amounts of Ca-ATPase than IIA fibers. No types II subgroups could be recognized after incubation with anti-CaS. These findings confirm results from previous immunochemical measurements on whole muscles containing different proportions of IIA and IIB fibers (Leberer and Pette 1986). Type IIA and IIC in the rabbit and rat soleus reacted stronger for Ca-ATPase and for CaS than type I fibers. Small differences in Ca-ATPase, but not in CaS, were recognized within the type I fiber population. Therefore, type I fibers in the rabbit and rat soleus are not a homogeneous population.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00492347
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  • 4
    Electronic Resource
    Electronic Resource
    Lactate dehydrogenase isozymes in type I, IIA and IIB fibres of rabbit skeletal muscles (1984)
    Springer
    Histochemistry and cell biology 80 (1984), S. 295-298 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Lactate dehydrogenase (LDH) isozyme patterns were analysed by polyacrylamide (PAA) slab gel electrophoresis in extracts prepared from various rabbit skeletal muscles of defined fibre composition and by PAA microelectrophoresis of microdissected, histochemically typed single muscle fibres. The results obtained by electrophoresis of whole muscle extracts generally agreed with the data obtained from single fibre electrophoresis, i.e. the LDH isozyme pattern corresponded to that of the predominant fibre type. Type I Fibres from soleus and semitendinosus muscles were characterized by a unique pattern of all 5 LDH isozymes with a predominance of LDH-1, 2 and 3. The major fraction (80%) of the type II fibres from extensor digitorum longus and tibialis anterior muscles contained only LDH-5 (M4). About 20% of the type II fibres contained in addition to LDH-5 small amounts of LDH-4 and LDH-3. The fraction of fibres containing LDH-5, LDH-4, and LDH-3 was similar (ca. 20%) in the histochemically defined IIA and IIB subpopulations In view of the fact that the major fractions of rabbit IIB fibres display low and of IIA fibres high aerobic oxidative capacities (Reichmann and Pette 1982), these data indicate that the expression of the H-subunit of LDH is not correlated with the aerobic-oxidative capacity of the fibre. It also appears not to be correlated with the presence of different myosin isoforms in IIA and IIB fibres.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495780
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  • 5
    Electronic Resource
    Electronic Resource
    Distribution of sarcoplasmic reticulum Ca-ATPase and of calsequestrin at the polar regions of rat, rabbit and cat intrafusal fibers (1988)
    Springer
    Histochemistry and cell biology 88 (1988), S. 273-276 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sarcoplasmic reticulum (SR) Ca2+-pumping ATPase (Ca-ATPase) and calsequestrin (CaS) were visualized by indirect immunofluorescence at the polar regions of adult rat, rabbit and cat intrafusal fibers. The immunohistochemical reaction products were regarded as histochemical markers of the SR and as valid indicators of the distribution of the two Ca2+sequestering proteins. Static nuclear bag2 fibers displayed lower levels of both Ca-ATPase and CaS than the other two intrafusal fiber types. Nuclear chain fibers presented the highest Ca-ATPase levels and, together with dynamic nuclear bag1 fibers, they also exhibited relatively high amounts of CaS. The level of Ca-ATPase was lower in bag1 fibers than in nuclear chain fibers, but not as low as in bag2 fibers. The comparatively high levels of Ca-ATPase and CaS seen in nuclear chain fibers coincided with their reported faster contractile speeds compared to nuclear bag fibers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00570284
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  • 6
    Electronic Resource
    Electronic Resource
    Effects of different patterns of long-term stimulation on blood flow, fuel uptake and enzyme activities in rabbit fast skeletal muscles (1984)
    Springer
    Pflügers Archiv 402 (1984), S. 306-311 
    Details
    ISSN: 1432-2013
    Keywords: Stimulated fast muscle ; Enzyme activities ; Oxygen consumption ; Blood flow
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Long-term electrical stimulation (14–28 days) of rabbit fast muscles (tibialis anterior, TA and extensor digitorum longus, EDL) using intermittent high frequency (3 trains per min of 5 s duration at 40 Hz, for 8 h per day) produced changes in enzyme activities similar to those found with continuous stimulaton at a frequency occuring in nerves to slow muscles (10 Hz). The activity of citrate synthetase, 3-hydroxyacyl-CoA dehydrogenase and succinate dehydrogenase increased two to 3-fold within 28 days. There was a 4-fold increase in hexokinase whereas phosphofructokinase, pyruvate kinase, lactate dehydrogenase and fructose-1,6-diphosphatase decreased to about 60% of the activity levels in the contralateral unstimulated muscles. Blood flow and oxygen consumption at rest were not changed even after 28 days of stimulation, but were increased during contractions in muscles stimulated at either frequency, the level being twice as high as in control muscles. Glucose uptake was similar to that in control muscles both at rest and during contractions and the output of lactate was similar to that found in control muscles in muscles stimulated at 40 Hz. Muscles stimulated at 10 Hz had smaller lactate output. Thus intermittent stimulation at high frequency (40 Hz) and continuous low frequency (10 Hz) produced similar changes in aerobic metabolism and fuel uptake provided that the total number of stimuli was comparable and that the stimulation was carried out for sufficiently long period.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00585514
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  • 7
    Electronic Resource
    Electronic Resource
    Genetic interactions indicate a role for Mdg1p and the SH3 domain protein Bem1p in linking the G-protein mediated yeast pheromone signalling pathway to regulators of cell polarity (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 608-621 
    Details
    ISSN: 1617-4623
    Keywords: Cell polarity ; G-protein ; MDG1 gene ; Signal transduction ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The pheromone signal in the yeastSaccharomyces cerevisiae is transmitted by theβ andγ subunits of the mating response G-protein. TheSTE20 gene, encoding a protein kinase required for pheromone signal transduction, has recently been identified in a genetic screen for high-gene-dosage suppressors of a partly defective Gβ mutation. The same genetic screen identifiedBEM1, which encodes an SH3 domain protein required for polarized morphogenesis in response to pheromone, and a novel gene, designatedMDG1 (multicopy suppressor ofdefectiveG-protein). TheMDG1 gene was independently isolated in a search for multicopy suppressors of abem1 mutation. TheMDG1 gene encodes a predicted hydrophilic protein of 364 amino acids with a molecular weight of 41 kDa that has no homology with known proteins. A fusion of Mdg1p with the green fluorescent protein fromAequorea victoria localizes to the plasma membrane, suggesting that Mdg1p is an extrinsically bound membrane protein. Deletion ofMDG1 causes sterility in cells in which the wild-type Gβ has been replaced by partly defective Gβ derivatives but does not cause any other obvious phenotypes. The mating defect of cells deleted forSTE20 is partially suppressed by multiple copies ofBEM1 andCDC42, which encodes a small GTP-binding protein that binds to Ste20p and is necessary for the development of cell polarity. Elevated levels ofSTE20 andBEM1 are capable of suppressing a temperature-sensitive mutation inCDC42. This complex network of genetic interactions points to a role for Bem1p and Mdg1p in G-protein mediated signal transduction and indicates a functional linkage between components of the pheromone signalling pathway and regulators of cell polarity during yeast mating.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172407
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  • 8
    Electronic Resource
    Electronic Resource
    Genetic interactions indicate a role for Mdg1p and the SH3 domain protein Bem1p in linking the G-protein mediated yeast pheromone signalling pathway to regulators of cell polarity (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 608-621 
    Details
    ISSN: 1617-4623
    Keywords: Key words Cell polarity ; G-protein ; MDG1 gene ; Signal transduction ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The pheromone signal in the yeast Saccharomyces cerevisiae is transmitted by the β and γ subunits of the mating response G-protein. The STE20 gene, encoding a protein kinase required for pheromone signal transduction, has recently been identified in a genetic screen for high-gene-dosage suppressors of a partly defective Gβ mutation. The same genetic screen identified BEM1, which encodes an SH3 domain protein required for polarized morphogenesis in response to pheromone, and a novel gene, designated MDG1 (multicopy suppressor of defective G-protein). The MDG1 gene was independently isolated in a search for multicopy suppressors of a bem1 mutation. The MDG1 gene encodes a predicted hydrophilic protein of 364 amino acids with a molecular weight of 41 kDa that has no homology with known proteins. A fusion of Mdg1p with the green fluorescent protein from Aequorea victoria localizes to the plasma membrane, suggesting that Mdg1p is an extrinsically bound membrane protein. Deletion of MDG1 causes sterility in cells in which the wild-type Gβ has been replaced by partly defective Gβ derivatives but does not cause any other obvious phenotypes. The mating defect of cells deleted for STE20 is partially suppressed by multiple copies of BEM1 and CDC42, which encodes a small GTP-binding protein that binds to Ste20p and is necessary for the development of cell polarity. Elevated levels of STE20 and BEM1 are capable of suppressing a temperature-sensitive mutation in CDC42. This complex network of genetic interactions points to a role for Bem1p and Mdg1p in G-protein mediated signal transduction and indicates a functional linkage between components of the pheromone signalling pathway and regulators of cell polarity during yeast mating.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02172407
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    Paper (German National Licenses)
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  • 9
    Electronic Resource
    Electronic Resource
    Immunochemical quantification of sarcoplasmic reticulum Ca2+-ATPase and calsequestrin in muscle biopsies from patients with myotonia congenita and paramyotonia congenita Eulenburg (1994)
    Springer
    Journal of neural transmission 95 (1994), S. 29-38 
    Details
    ISSN: 1435-1463
    Keywords: Sarcoplasmic reticulum ; Ca2+-ATPase ; calsequestrin ; myotonia congenita ; paramyotonia congenita Eulenburg
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A sensitive enzyme-linked immunoadsorbant assay was developed to quantify Ca2+ -ATPase and calsequestrin from sarcoplasmic reticulum in human muscle biopsies. Tissue levels of Ca2+ -ATPase and calsequestrin averaged 51.5 ± 28.1 and 6.4 ± 1.8mg/g muscle protein, respectively, in control muscles (means ± SD, n=12). The high sensitivity and specificity of the antibodies make the assay a useful tool in the diagnosis of human neuromuscular disorders where defects in sarcoplasmic reticulum function may be expected. The assay was applied to muscle biopsies from patients with myotonia congenita and paramyotonia congenita Eulenburg. The calsequestrin concentration was normal in all patient muscles. The Ca2+ -ATPase content was also within the normal range but varied considerably with the percentage distribution of slowtwitch fibres. This indicates that the prolonged relaxation observed in the muscles of patients with these disorders is not caused by faulty expression of Ca2+-ATPase and calsequestrin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01283028
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