Fiber type composition of the human female trapezius muscle: enzyme-histochemical characteristics

Tne anatomy of the human trapezius muscle is complex, with an extensive origin and fibers running in different directions. The muscle is commonly divided into three different muscle portions according to the fiber direction: the descending, transverse, and ascending portions. In a previous study in males, the structure of the muscle differed between different portions with respect to the enzyme-histochemical fiber-type profile. The lower regions of the descending portion and the transverse and the ascending portions had a predominance of type I fibers. The type II fibers were more frequent in the upper regions of the descending portion, and the cross-sectional fiber area in this region of the muscle was smaller. In this study, we have investigated the trapezius muscle in females and compared the results with those from males. The different portions of the female muscle had a relatively even fiber-type composition. However, there tended to be fewer type I fibers and more type IIB fibers in the descending portion of the muscle, and the fibers of the lower regions of the descending portion were somewhat larger. The fiber-type distribution pattern was similar to that of the male trapezius muscle, but the mean cross-sectional area of the fibers in the female muscle was considerably smaller. Thus, our conclusion is that the trapezius muscle of females has a similar activity pattern as that of males. The significantly smaller cross-sectional fiber area, however, may indicate a lower functional capacity which may be of importance in the development of neck and shoulder dysfunction in females.     

Vimentin is hyperphosphorylated in primary human fibroblasts treated with okadaic acid.

Okadaic acid and dinophysistoxin-1 (35-methylokadaic acid) induced hyperphosphorylation of a 58 kDa protein in primary human fibroblasts, due to inhibition of protein phosphatase 1 and 2A activities. The protein was present in the nuclear and cytosolic fractions. Its pI was 5.3. The hyperphosphorylated protein reacted with monoclonal and polyclonal anti-vimentin antibodies, but not with anti-nucleolin antibody. Phosphorylation of vimentin was stimulated in vitro by dinophysistoxin-1 dose-dependently in the presence of protein phosphatase 2A and protein kinases.     

DDT and pyrethroids--ecotoxicological considerations.

1. DDT, and a DDT metabolite, DDOH, conjugated to palmitic acid, DDOH-PA, as well as bioallethrin and deltamethrin have all been shown to affect muscarinic cholinergic receptors (MAChR) in the neonatal mouse brain after administration to 10-day-old mice during the period of rapid brain growth. 2. This early exposure has also been shown to lead to permanent changes in cholinergic and behavioural variables in the animals as adults.     

Utilization of zeolite Y in the removal of anionic,cationic and nonionic detergents during purification of proteins

Summary Hydrophobie zeolite Y was used to adsorb detergents from protein solutions and within one minute the commonly used detergents sodium dodecyl sulfate, cetyl trimethyl ammonium bromide, and Triton X-100 at concentrations of 10 mg/ml were adsorbed to a level below their critical micelle concentrations. From the detergent depleted solutions 77 to 85 % of the proteins were recovered; the lower value was obtained with protein concentration below one mg/ml.     

Selective inactivation of the deoxyadenosine phosphorylating activity of pure human deoxycytidine kinase: stabilization of different forms of the enzyme by substrates and biological detergents

Deoxycytidine kinase, purified from human leukemic spleen to apparent homogeneity, is a multisubstrate enzyme that also phosphorylates purine deoxyribonucleosides [Bohman & Eriksson (1988) Biochemistry 27, 4258-4265]. In the present investigation we show that the stability and temperature dependence of dCyd kinase activity differed appreciably from the dAdo kinase activity of the same pure enzyme. Selective inactivation of dAdo activity was observed upon an incubation of the enzyme at both 4 and 37 degrees C. The half-life of dAdo activity at 4 degrees C increased from 36 to 84 h, when the protein concentration was increased by addition of bovine serum albumin. However, the half-life of dCyd activity increased from 72 h to more than 7 days under the same conditions. dCyd activity was stable for at least 6 h at 37 degrees C while the half-life of dAdo activity was 2 h. The presence of substrates like ATP, dTTP, or dAdo stabilized dAdo activity at both temperatures, and full maintenance of both activities at 37 degrees C was obtained by the addition of the zwitterionic detergent CHAPS. Furthermore, thermal inactivation of the dAdo activity occurred at a lower temperature (48 degrees C) as compared to the dCyd activity (54 degrees C). The presence of protease inhibitors had no effect on enzyme inactivation, nor was there a difference in the subunit structure of the selectively inactivated enzyme as compared to the fully active form, as revealed by size-exclusion chromatography.(ABSTRACT TRUNCATED AT 250 WORDS)     

Hepatocellular uptake of 3H-dihydromicrocystin-LR, a cyclic peptide toxin

The cellular uptake of microcystin-LR, a cyclic heptapeptide hepatotoxin from the cyanobacterium Microcystis aeruginosa, was studied by means of a radiolabelled derivative of the toxin. 3H-dihydromicrocystin-LR. The uptake of 3H-dihydromicrocystin-LR was shown to be specific for freshly isolated rat hepatocytes whereas the uptake in the human hepatocarcinoma cell line Hep G2 as well as the mouse fibroblast cell line NIH-3T3, and the human neuroblastoma cell line SH-SY5Y, was negligible. By means of a surface barostat technique it was shown that the membrane penetrating capacity (surface activity) of microcystin-LR was low, indicating that the toxin requires an active uptake mechanism. The hepatocellular uptake of microcystin-LR could be inhibited in the presence of bile acid transport inhibitors such as antamanide (5 microM), sulfobromophthalein (50 microM) and rifampicin (30 microM). The uptake was also reduced in a concentration dependent manner when the hepatocytes were incubated in the presence the bile salts cholate and taurocholate. A complete inhibition of the hepatocellular uptake was achieved by 100 microM of either bile salt. The overall results indicate that the uptake of microcystin-LR is through the multispecific transport system for bile acids. This mechanism of cell entry would explain the previously observed cell specificity and organotropism of microcystin-LR.     

Fiber type composition of the human male trapezius muscle: enzyme-histochemical characteristics

The human trapezius muscle has an origin that is more extensive than that of any other body muscle; it has a complex macroscopic structure with fibers running in different directions. Histochemical analysis of multiple samples, obtained from different parts of the trapezius muscle from five males, showed marked differences in the distribution and the cross-sectional fiber area of the fiber types among different parts of the muscle as well as among individuals. As revealed by the mATPase activity, after different levels of alkaline and acidic preincubations, the lower third of the descending portion, the transverse, and the ascending portions of the muscle had a predominance of type I fibers (low mATPase activity at pH 9.4), whereas the most superior parts of pars descendens had a higher frequency of type II fibers (high mATPase activity at pH 9.4). The fibers of the most superior parts of the muscle were considerably smaller compared with those in all the other parts. In sections stained for NADH-TR, moth-eaten fibers were observed within parts of the descending portion. Their location and their larger fiber area, compared with that of ordinary type I fibers, may be related to frequent and/or continuous use of these fibers. In conclusion, the differences in fiber type composition between the different parts of the muscle probably reflect different functional demands on the trapezius muscle in various head, neck, and shoulder movements. We suggest that the interindividual differences in muscle fiber composition are due, at least in part, to genetic factors.     

Vanillic acid metabolism by selected soft-rot,brown-rot,and white-rot fungi

Metabolism of vanillic acid, a product of lignin degradation, has been studied in selected representatives of soft-rot, brown-rot and white-rot fungi. All of the brown-and white-rot species examined decarboxylated vanillate to methoxyhydroquinone oxidatively. Mycelium extracts of all these fungi, except Pleurotus ostreatus contained high levels of an NAD(P)H-dependent vanillate hydroxylase. P. ostreatus also released ¹⁴CO₂ from ¹⁴COOH-vanillate but by a different mechanism possibly involving phenoloxidases. Most of these fungi also contained a dioxygenase which catalysed the intra-diol cleavage of hydroxyquinol (1,2,4-trihydroxybenzene) to form maleylacetate. No 3-O-demethylase activity was detected, and data indicate that in some of the fungi examined cleavage of the aromatic ring occurs without prior removal of the methoxyl group. None of the soft-rot fungi tested contained vanillate hydroxylase or hydroxyquinol 1,2-dioxygenase, but very low levels of protocatechuate 3,4-dioxygenase were detected in mycelium extracts. Vanillate catabolism among members of this group occurs via a different route which may involve ring demethylation although no 3-O-demethylase activity was detected in this study. The enzyme NAD(P)H-quinone oxidoreductase was demonstrated to exist in all the studied groups of fungi.     

Ligninolytic activity and levels of ammonia assimilating enzymes in Sporotrichum pulverulentum

Levels of ammonia-assimilating enzymes (glutamate dehydrogenase, glutamine synthetase, glutamate synthase) were determined in extracts of Sporotrichum pulverulentum grown under different conditions with respect to both nitrogen source and concentration. Evolution of ¹⁴CO₂ from ¹⁴C-synthetic lignin by fungal cultures grown under parallel conditions was also determined as a measure of lignin decomposition and the suppressive effect of nitrogen on ligninolysis confirmed. Under low nitrogen conditions, fungal extracts exhibited relatively high levels of NADP-dependent glutamate dehydrogenase and glutamine synthetase dehydrogenase. Conversely, in high nitrogen extracts, lower levels of NADP-dependent glutamate dehydrogenase and glutamine synthetase activity, and higher levels of NAD-dependent glutamate dehydrogenase, were recorded. Possible effects of enzyme activities on intracellular pool concentrations of glutamate/glutamine, and the implications for the regulation of lignin metabolism, are discussed.A preliminary report was presented at The Ekman Days 1981, International Symposium on Wood and Pulping Chemistry, Stockholm, Sweden, June 9–12, 1981.