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Academic literature on the topic 'Sarcoplasmic proteins'

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Published: 4 June 2021
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Journal articles on the topic "Sarcoplasmic proteins"

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Grujić, Radoslav, Radoslav Grujić, Danica Savanović, and Danica Savanović. "Analysis of myofibrillar and sarcoplasmic proteins in pork meat by capillary gel electrophoresis." Foods and Raw Materials 6, no. 2 (December 20, 2018): 421–28. http://dx.doi.org/10.21603/2308-4057-2018-2-421-428.

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Myofibrillar and sarcoplasmic proteins were extracted from pork meat (M. Longissimus dorsi) and then separated by capillary gel electrophoresis (CGE). Migration time and peak areas of individual protein molecules in the electropherogram were analysed. The electropherograms obtained after the separation of myofibrillar proteins contained 53 well-separated peaks, of which the following were identified: thymosin, myosin light chain-3 (MLC-3), myosin light chain-2 (MLC-2), troponin C, troponin I, myosin light chain-1 (MLC-1), tropomyosin 1, tropomyosin 2, troponin T, actin, desmin, troponin, C protein, and myosin heavy chain (MHC). The relative concentration of the identified myofibrillar proteins was 74.5%. Of the 56 separated sarcoplasmic proteins the following were identified: myoglobin, myokinase, triosephosphate isomerase, phosphoglycerate mutase, lactate dehydrogenase, glyceraldehyde phosphate dehydrogenase, aldolase, creatine kinase, enolase, phosphoglucose isomerase, pyruvate kinase, phosphoglucomutase, and phosphorylase b. The relative concentration of the identified sarcoplasmic proteins was 83.6% of all sarcoplasmic proteins extracted from the pork meat.
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Fiorotto, Marta L., Teresa A. Davis, and Peter J. Reeds. "Regulation of myofibrillar protein turnover during maturation in normal and undernourished rat pups." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 278, no. 4 (April 1, 2000): R845—R854. http://dx.doi.org/10.1152/ajpregu.2000.278.4.r845.

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The study tested the hypothesis that a higher rate of myofibrillar than sarcoplasmic protein synthesis is responsible for the rapid postdifferentiation accumulation of myofibrils and that an inadequate nutrient intake will compromise primarily myofibrillar protein synthesis. Myofibrillar (total and individual) and sarcoplasmic protein synthesis, accretion, and degradation rates were measured in vivo in well-nourished (C) rat pups at 6, 15, and 28 days of age and compared at 6 and 15 days of age with pups undernourished (UN) from birth. In 6-day-old C pups, a higher myofibrillar than sarcoplasmic protein synthesis rate accounted for the greater deposition of myofibrillar than sarcoplasmic proteins. The fractional synthesis rates of both protein compartments decreased with age, but to a greater degree for myofibrillar proteins (−54 vs. −42%). These decreases in synthesis rates were partially offset by reductions in degradation rates, and from 15 days, myofibrillar and sarcoplasmic proteins were deposited in constant proportion to one another. Undernutrition reduced both myofibrillar and sarcoplasmic protein synthesis rates, and the effect was greater at 6 (−25%) than 15 days (−15%). Decreases in their respective degradation rates minimized the effect of undernutrition on sarcoplasmic protein accretion from 4 to 8 days and on myofibrillar proteins from 13 to 17 days. Although these adaptations in protein turnover reduced overall growth of muscle mass, they mitigated the effects of undernutrition on the normal maturational changes in myofibrillar protein concentration.
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Jafarpour, Ali, and Elisabeth M. Gorczyca. "Contribution of Sarcoplasmic Proteins to Myofibrillar Proteins Gelation." Journal of Food Science 77, no. 2 (January 6, 2012): R73—R81. http://dx.doi.org/10.1111/j.1750-3841.2011.02521.x.

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Fadda, Silvina, Yolanda Sanz, Graciela Vignolo, M. Concepción Aristoy, Guillermo Oliver, and Fidel Toldrá. "Characterization of Muscle Sarcoplasmic and Myofibrillar Protein Hydrolysis Caused by Lactobacillus plantarum." Applied and Environmental Microbiology 65, no. 8 (August 1, 1999): 3540–46. http://dx.doi.org/10.1128/aem.65.8.3540-3546.1999.

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ABSTRACT Strains of Lactobacillus plantarum originally isolated from sausages were screened for proteinase and aminopeptidase activities toward synthetic substrates; on the basis of that screening,L. plantarum CRL 681 was selected for further assays on muscle proteins. The activities of whole cells, cell extracts (CE), and a combination of both on sarcoplasmic and myofibrillar protein extracts were determined by protein, peptide, and free-amino-acid analyses. Proteinase from whole cells initiated the hydrolysis of sarcoplasmic proteins. The addition of CE intensified the proteolysis. Whole cells generated hydrophilic peptides from both sarcoplasmic and myofibrillar proteins. Other peptides of a hydrophobic nature resulted from the combination of whole cells and CE. The action of both enzymatic sources on myofibrillar proteins caused maximal increases in lysine, arginine, and leucine, while the action of those on sarcoplasmic proteins mainly released alanine. In general, pronounced hydrolysis of muscle proteins required enzyme activities from whole cells in addition to those supplied by CE.
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Fliegel, Larry, Kimberly Burns, Ken Wlasichuk, and Marek Michalak. "Peripheral membrane proteins of sarcoplasmic and endoplasmic reticulum. Comparison of carboxyl-terminal amino acid sequences." Biochemistry and Cell Biology 67, no. 10 (October 1, 1989): 696–702. http://dx.doi.org/10.1139/o89-104.

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Peripheral endoplasmic reticulum membrane proteins residing in the lumen of the endoplasmic reticulum occupy the same space as other secreted proteins. The presence of a four amino acid salvage or retention signal (KDEL-COOH = Lys-Asp-Glu-Leu-COOH) at the carboxyl-terminal end of peripheral membrane proteins has been shown to represent a signal or an essential part of a signal for their retention within the endoplasmic reticulum membrane. In heart and skeletal muscle, a number of sarcoplasmic reticulum proteins have recently been identified which are peripheral membrane proteins. The high-affinity calcium-binding protein (55 kilodaltons (kDa)) appears to conform to the above described mechanisms and contains the KDEL carboxyl-terminal tetrapeptide. Thyroid hormone binding protein is present in the sarcoplasmic reticulum, in addition to its endoplasmic reticulum location, and has a modified but related tetrapeptide sequence (RDEL = Arg-Asp-Glu-Leu), which also probably functions as the retention signal. Calsequestrin and a 53-kDa glycoprotein, two other peripheral membrane proteins residing in the lumen of the sarcoplasmic reticulum, do not contain the KDEL retention signal. The sarcoplasmic reticulum may have developed a unique retention mechanism(s) for these muscle-specific proteins.Key words: sarcoplasmic reticulum, endoplasmic reticulum, amino acid sequences, peripheral membrane proteins, KDEL retention sequence.
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LEHNART, STEPHAN E., WOLFGANG SCHILLINGER, BURKERT PIESKE, JURGEN PRESTLE, HANJORG JUST, and GERD HASENFUSS. "Sarcoplasmic Reticulum Proteins in Heart Failure." Annals of the New York Academy of Sciences 853, no. 1 CARDIAC SARCO (September 1998): 220–30. http://dx.doi.org/10.1111/j.1749-6632.1998.tb08270.x.

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Fischer, T. H., D. W. Barton, K. H. Krause, T. E. White, K. P. Campbell, and G. C. White. "The identification of sarcoplasmic reticulum terminal cisternae proteins in platelets." Biochemical Journal 263, no. 2 (October 15, 1989): 605–8. http://dx.doi.org/10.1042/bj2630605.

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Two new proteins with apparent molecular masses of 53 kDa and 190 kDa have been identified in both sarcoplasmic reticulum and human blood platelets using a monoclonal antibody, FII1b5. The sarcoplasmic reticulum FII1b5 antigens were present in the terminal cisternae fraction, but were absent from light sarcoplasmic reticulum. The platelet and skeletal muscle proteins were not sensitive to digestion with endoglycosidase H under conditions that removed carbohydrate from the 53 kDa glycoprotein in sarcoplasmic reticulum or GPIIIa in platelet microsomes and did not bind 45Ca in a nitrocellulose overlay calcium-binding assay. These results distinguished the FII1b5 antigens from the 53 kDa glycoprotein and calsequestrin of sarcoplasmic reticulum. The 190 kDa platelet and sarcoplasmic reticulum proteins were extracted from membranes with high concentrations of NaCl, indicating that the high molecular mass FII1b5 antigens are peripherally associated with the bilayers. In contrast, the platelet and muscle 53 kDa proteins remained membrane-bound in the presence of high salt concentrations, suggesting that they are integral proteins.
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KIM, YOUNG S., JIRAWAT YONGSAWATDIGUL, JAE W. PARK, and SUPAWAN THAWORNCHINSOMBUT. "CHARACTERISTICS OF SARCOPLASMIC PROTEINS AND THEIR INTERACTION WITH MYOFIBRILLAR PROTEINS." Journal of Food Biochemistry 29, no. 5 (October 2005): 517–32. http://dx.doi.org/10.1111/j.1745-4514.2005.00023.x.

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Morioka, Katsuji, and Yutaka Shimizu. "Heat-Coagulation Property of Fish Sarcoplasmic Proteins." NIPPON SUISAN GAKKAISHI 58, no. 8 (1992): 1529–33. http://dx.doi.org/10.2331/suisan.58.1529.

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MacLennan, David H. "Expression and mutagenesis of sarcoplasmic reticulum proteins." Journal of Molecular and Cellular Cardiology 24 (May 1992): 34. http://dx.doi.org/10.1016/0022-2828(92)90132-j.

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Dissertations / Theses on the topic "Sarcoplasmic proteins"

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Gilchrist, James Stuart Charles. "Calcium regulation of calcium transport by sarcoplasmic reticulum." Thesis, University of British Columbia, 1990. http://hdl.handle.net/2429/30880.

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The sarcoplasmic reticulum (SR) of skeletal muscle is an intracellular membraneous network that, through the cyclical release and re-uptake of Ca²⁺ into and from, respectively, the cytoplasmic space, regulates myofilament shortening and, therefore, muscle contraction. SR derived from the terminal cisternae (HSR) demonstrates the property of Ca²⁺-induced Ca²⁺ release. Upon attainment of a threshold intralumenal Ca²⁺ load, application of a small pulse of extralumenal Ca²⁺ stimulates the release of a pool of intralumenal Ca²⁺ via the ligand gated Ca²⁺ permeable pore of the Ca²⁺ release channel/ryanodine receptor complex. It was hypothesised that intralumenal Ca²⁺ regulates the opening of the release channel. HSR vesicles were purified from skeletal and cardiac muscle by a novel technique. Structural characterisation of these membranes demonstrated an enrichment of harvested fractions in the Ca²⁺ release channel and the intralumenal Ca²⁺ binding protein, calsequestrin. In radiometric studies, skeletal HSR vesicles were shown to bind ryanodine with high capacity at both low and high affinity sites, with 2 fold stimulation of Ca²⁺ accumulation by the polyorganic cation Ca²⁺ channel blocker, ruthenium red. HSR vesicles passively loaded Ca²⁺. Passive loading of HSR vesicles with Ca²⁺ was found to be non-linearly dependent upon the concentration of Ca²⁺ within the loading medium. This suggested the presence of 2 intralumenal Ca²⁺ binding sites with different affinities for Ca²⁺. A spectroscopic dual-wavelength assay of Ca²⁺ release was developed that took advantage of peculiar spectral properties of the metallochromic sensitive dye Antipyrylazo III. In the presence of mM MgATP and mM Mg2+ the initial fast phase of HSR Ca²⁺ was well resolved. Evidence was presented that initial rapid uptake was associated with high affinity binding to an intralumenal compartment. Ca²⁺ -induced Caz+ release was shown to occur with a threshold loading of intralumenal Ca²⁺. The intralumenal Ca²⁺ threshold for Ca²⁺-induced Ca²⁺ release was decreased in the presence of ryanodine. Ryanodine induced Ca²⁺ release was also dependent upon the amount of intralumenal Ca²⁺. Ryanodine was also shown to inhibit sustained Ca²⁺-induced Ca²⁺ release by apparent inhibition of the binding of Ca²⁺ to intralumenal sites. These results suggested that junctional state transitions of the Ca²⁺ channel and calsequestrin were interdependent. Purified mM and mM Ca²⁺ activated neutral protease isoforms selectively cleaved the Ca²⁺ channel into 410 and 150kDa peptides with limited proteolysis. This was demonstrated in both HSR vesicles and the purified Ca²⁺ release channel. A novel 88kDa protein was also shown to be fragmented by both CANP isoforms. The identity of this prominent HSR associated protein remains obscure. CANP fragmentation of HSR protein elevated passive and active 4^Ca²⁺ loading in vesicles. This indicated that selective structural modification of the cytoplasmic portion of the release channel modified the comformational states of a intralumenal Ca²⁺ binding compartment in HSR vesicles. In spectroscopic studies, CANP proteolysis of HSR proteins increased the sensitivity to Ca²⁺ and ryanodine-induced Ca²⁺ release through decreases in the required intralumenal Ca²⁺ threshold for release. These functional alterations coincided with apparent single site cleavage of the release channel. Further proteolysis of the initial 410 and 150kDa peptides was without further significant effect upon function. Based upon the hypothesis that primary sequences rich in proline (P), glutamate (E), aspartate (D), serine (S) and threonine (T) (PEST regions) are recognition sites for CANP binding to substrates, a search for PEST regions within the Ca²⁺ channel was undertaken. It was tentatively proposed that two PEST regions near the N-terminal of the Caz release channel may represent sites close to the CANP cleavage site. The results of this work were discussed in relation to a possible role of Ca²⁺-induced Ca²⁺ release in regulating the patterning of Ca²⁺ cytosolic transients. The frequency and amplitude of cytosolic Ca²⁺ transients appear to be important in regulating protein expression. The requirement of intralumenal Ca²⁺-induced Ca²⁺ release may be a means by which the cyclical uptake and release of Ca²⁺ during muscle relaxation and contraction can be coordinated. This coordination may define the patterning of cytosolic Ca²⁺ transients. The increased sensitivity to Ca²⁺-induced Ca²⁺ release by HSR after CANP treatment may represent a means by which the patterning of cytosolic Ca²⁺ transients can be altered to effect changes in protein synthesis.
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Kim, Eunjung. "Biochemical studies of cardiac calsequestrin : its interaction with pharmaceutical drugs and its deleterious mutations." Online access for everyone, 2007. http://www.dissertations.wsu.edu/Dissertations/Spring2007/ej_kim_050107.pdf.

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Koban, Maren Ulrike. "Calcium handling proteins in cardiac relaxation : regulation and expression during development and growth in rat heart." Thesis, Imperial College London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325105.

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Flinn, Rory J. "Novel use of glycosylation scanning to map the intracellular trafficking of sarco(endo)plasmic reticulum calcium ATPase 1A." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 0.55 Mb., 80 p, 2005. http://wwwlib.umi.com/dissertations/fullcit/1428192.

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Jafarpour, Khozaghi Seyed Ali, and ali jafarpour@rmit edu au. "Quality characteristics of common carp (Cyprinus carpio) Surimi and Kamaboko and the role of Sarcaoplasmic Proteins." RMIT University. Applied Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081216.144930.

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This study was carried out to determine the characteristics of common carp surimi. In Australia, common carp (Cyprinus carpio) is an environmental pest, strongly coloured (dark-muscle fish), large (2-3 kg), low cost (AUD 2.5/kg) and not highly valued as it is every where else. Surimi could add value to carp, but the colour would have to be modified as surimi manufacturers prefer white coloured flesh. So, firstly the efficiency of Hydrogen peroxide (H2O2; 1-3% v/v) solution at alkaline side of pH (7.0-11.5) on whitening of light fillets of common carp was examined. The whiteness (L*-3b*) of surimi produced from treated (3% H2O2, pH 8.2) common carp light fillets was significantly (p less than 0.05) greater than that of threadfin bream surimi and was not significantly different to that of Alaska pollock. Based on a temperature sweep test, a similar pattern in G of tested surimi was observed which started at ca. 47?C and was completed at ca. 73-74?C. However, thread fin bream kamaboko showed better texture profile characteristics (hardness and gel strength) than that of the other kamaboko tested. To improve the quality of common carp surimi and kamaboko, alternative methods were applied such as modified conventional method (MCM), alkaline-aided method (AAM) and pH modified method (PMM) and the resultant surimi and kamaboko were compared with those produced by the traditional method (TM). In MCM each washing cycle was followed by a centrifugation step for a more effective dewatering and removal of sarcoplasmic proteins (Sp-P). Kamaboko prepared from MCM was whiter and had significantly (p less than 0.05) improved textural characteristics (hardness and gel strength) than that from TM, AAM and PMM. Furthermore, SEM of surimi and kamaboko showed higher number of polygonal structure/mm2 in the gel matrix of MCM kamaboko, as a result of more cross-linking of the myofibrillar proteins, than that recorded for TM, AAM and PMM samples tested. Finally, this study examined the effect of adding common carp sarcoplasmic proteins (Sp-P) on the gel characteristics of threadfin bream surimi and kamaboko. Based on the temperature sweep test, the depths of the valley in the G thermograph of the gels decreased as the concentration of added Sp-P increased from 5% to 35%. Storage modulus (G) of the gels showed greater elasticity in the samples with added Sp-P compared with the control samples without added Sp-P. Furthermore, the breaking force and breaking distance and consequently gel strength of the resultant kamaboko were improved, significantly (p less than 0.05) with added Sp-P. Thus, added Sp-P did not interfere with the gelling of myofibrillar proteins during sol-gel transition phase and was associated with textural quality enhancement for the resultant kamaboko. However, the addition of freeze-dried Sp-P from the dark muscle of the carp decreased the whiteness of the resultant surimi. Furthermore, the gel strength could not be associated with either the number of polygonal structures/mm2 or the area of the polygonal structures.
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Zibrova, Darya. "Adenovirus-mediated gene transfer of FK506-binding proteins FKBP12.6 and FKBP12 in failing and non-failing rabbit ventricular myocytes." Doctoral thesis, [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972602275.

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Tentes, I. "Studies on the sarcoplasmic reticulum (Ca'2'+ + Mg'2'+) - ATPase." Thesis, University of Salford, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.381695.

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Tryptic digestion of SRV labelled with N-cyclohexyl-N'-(4-dimethylamino--naphthyl) carbodiimide (NCD-4), was shown to expose Ca^2+-protectable NCD-4-labelled amino acid residues, manifested by a time dependent quench (38%) of the initial fluorescence of the preparation. This finding is discussed in terms of a 3D model of the (Ca2+ + Mg2+)-ATPase. The inhibition of the sarcoplasmic reticulum (Ca2+ + Mg2+)-ATPase by the diphenolic antioxidants: 4,4'-isopropylidene diphenol, 4-hydroxy, 4'-methoxy isopropylidene diphenol, 4,4'dimethoxy isopropylidene diphenol and bis (2-hydroxy-3,5-methyl phenyl) methane, was studied, using the fluorescence response to bound NCD-4. They were shown to modulate conformational transitions of the ATPase subsequent to Ca2+ binding. It is suggested that the diphenolic antioxidants may have a target/binding site on the ATPase polypeptide via which they compete with Ca2+ ion binding and translocation. The stoichiometry of incorporation into the ATPase of tritated NCD-4 was studied. The ATPase was incubated with [3H]-NCD-4 for 4h. in the presence and in the absence of Ca2+ ions and then treated with trypsin for 35 mins. The four fragments: A(Mr= 50KD), B(Mr= 45KD), A1(Mr= 30KD) and A2(Mr= 20KD) were purified by preparative SDS-PAGE. The stoichiometry of incorporation of the radioactive label into fragments A1, A2 and the A2 subfragments SI (Mr= 13KD) and SII(Mr= 8.5KD) from CNBr cleavage, was measured by liquid scintillation counting of the gel eluates. In the absence of Ca2+, fragment A2 was found to incorporate 2.3 nmol [^3H]-NCD-4 per nmol of protein more than the equivalent preparation in the presence of Ca^2+. Subfragment S_I was shown to incorporate roughly equal amounts of label in both cases. S_II, however, in the absence of Ca^2+ was found to incorporate 1.15-2.3 nmol [^3H]-NCD-4 more than the equivalent preparation in the presence of Ca^2+. These differences were attributed to inhibitor binding at the Ca^2+-binding sites of the enzyme. However, discrepancies in the absolute incorporation values when experiments were compared, were related to loss of bound label due to nucleophilic attack. Four isomers of NCD-4 were prepared and evaluated in terms of inhibitory capacity towards the (Ca^2+ + Mg^2+)-ATPase. Preliminary evidence suggested that even related (isomeric) carbodimides can label different sites on the ATPase polypeptide. The synthesis and the evaluation of (N-cyclohexyl, N'-dimethylamino phenylazophenyl) carbodiimide (ACD) as a chromophoric probe for the Ca^2+ sites of the ATPase, is also described: this compound emerged as a relatively poor inhibitor of the enzyme, despite showing favourable chromophoric properties.
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GREGORY, KIMBERLY NICOLE. "SARCOPLASMIC RETICULUM CALCIUM CYCLING AND CARDIAC DISEASE." University of Cincinnati / OhioLINK, 2005. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1116008332.

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Kaisto, T. (Tuula). "Special features of vesicle trafficking in skeletal muscle cells." Doctoral thesis, University of Oulu, 2003. http://urn.fi/urn:isbn:9514271521.

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Abstract Skeletal muscles are composed of long, multinucleated cells called myofibers, which are highly differentiated cells and therefore unique in structure. In the present study the organization of the endocytic and exocytic pathways in isolated rat skeletal myofibers was defined with confocal and electron microscopic methods. In isolated myofibers the I band areas were shown to be active in endocytosis. The sorting endosomes were distributed in a cross-striated fashion while the recycling and late endosomal compartments were located to perinuclear areas and interfibrillar spaces, where they followed the course of microtubules. Protein trafficking in the different stages of muscle cell differentation was also analyzed. The studies with L6 myoblasts and myotubes showed that during myogenesis varying fractions of different viral glycoproteins were sorted from the endoplasmic reticulum (ER) into a specific compartment that did not recycle with the Golgi apparatus. This compartment is suggested to be the sarcoplasmic reticulum (SR). The studies with living muscle cells showed further changes in vesicle trafficking taking place during myogenesis. With GFP-tagged tsO45G protein, transport containers were detected in 20% of the infected myofibers, while all infected L6 myoblasts or myotubes showed intense movement of corresponding structures. We also detected significant differences between the pre-and post-Golgi traffickings in myofibers. When the distribution of the ER in adult myofibers was studied, the confocal microscopic data showed that the labeling patterns of the rough endoplasmic reticulum (RER) and the SR markers were different. Blocking of different cargo proteins in the RER revealed two discrete distribution patterns, neither of them identical with the SR. The collected electron microscopic data supported the idea that in mature myofibers there are two separate RER compartments. We suggest that the RER compartment capable of export function located around the myonuclei and on the Z lines, while the non-exporting RER compartment localized to terminal cisternae and probably took care of the synthesis of the SR proteins.
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Allen, Emily E. "Changes in Skeletal Muscle Sarcoplasmic Reticulum Calcium Handling and Regulatory Protein Content in Congestive Heart Failure." Thesis, Virginia Tech, 2002. http://hdl.handle.net/10919/31865.

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Fatigue and skeletal muscle weakness are problems associated with congestive heart failure. Research does not support the theory that the affected cardiac function is responsible for the fatigue. During skeletal muscle fatigue, calcium handling is altered. Thus, the fatigue associated with congestive heart failure could be attributed to altered calcium handling. The main proteins involved in calcium release are the ryanodine receptor (RyR) and the dihydropyridine receptor (DHPR). The main proteins involved in calcium uptake are the fast and slow isoforms of sarco(endo)plasmic reticulum calcium ATPase (SERCA 1 and SERCA 2 respectively). Calsequestrin (Csq) and calmodulin (CaM) play regulatory roles in calcium handling. Changes in the levels of these proteins could explain alterations in calcium handling and subsequent muscle function. The purpose of this study was to use a genetic model of heart failure, the SHHF rat, to examine the levels of regulatory calcium handling proteins to determine if changes in the amounts of RyR, DHPR, SERCA1, SERCA2, Csq and CaM are altered in congestive heart failure. A significant decrease was found in the amounts of RyR, DHPR, and SERCA 1 of the SHHF gastrocnemius and diaphragm samples in comparison to the control. There was no significant difference found in the amounts of CaM or SERCA 2 between the two groups. Csq was not found to be statistically different between the two groups of the gastrocnemius samples. However, there was an increase in Csq in the SHHF diaphragm samples in comparison to the control. In conclusion, the calcium handling proteins are affected in the genetic model of heart failure. These changes could explain previous reports of altered calcium handling within the skeletal muscles of congestive heart failure animals.
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Books on the topic "Sarcoplasmic proteins"

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1952-, Johnson Robert G., Kranias Evangelia G, and New York Academy of Sciences., eds. Cardiac sarcoplasmic reticulum function and regulation of contractility. New York, N.Y: New York Academy of Sciences, 1998.

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Comparison of the protein composition of Ca2+ - Storage/release sites in postnatal and adult cardiac sarcoplasmic reticulum. Ottawa: National Library of Canada, 2000.

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A biochemical analysis of the exercise-induced dysfunction of the rat gastrocnemius sarcoplasmic reticulum Cap2+s-ATPase protein. 1992.

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Book chapters on the topic "Sarcoplasmic proteins"

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Haard, Norman F., Benjamin K. Simpson, and Bonnie Sun Pan. "Sarcoplasmic Proteins and Other Nitrogenous Compounds." In Seafood Proteins, 13–39. New York, NY: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-7828-4_3.

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Soyer, Ayla, and Herbert O. Hultin. "Oxidation of Fish Sarcoplasmic Reticular Lipids and Proteins." In Quality Attributes of Muscle Foods, 269–76. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4731-0_18.

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Dillmann, Wolfgang H. "Regulation of expression of cardiac sarcoplasmic reticulum proteins under pathophysiological conditions." In Biochemistry of Signal Transduction in Myocardium, 125–28. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1275-8_16.

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Lamers, Jos M. J., Karin Eizema, Karel Bezstarosti, Henry Fechner, Sonja Schneider-Rasp, Haili Wang, and Wolfgang C. Poller. "Sarcoplasmic Reticulum Proteins as Potential Targets for Gene Therapy of Heart Failure." In Cardiac Remodeling and Failure, 87–101. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9262-8_6.

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Schwartz, K., L. Carrier, A. M. Lompré, J. J. Mercadier, and K. R. Boheler. "Contractile proteins and sarcoplasmic reticulum calcium-ATPase gene expression in the hypertrophied and failing heart." In Cellular and Molecular Alterations in the Failing Human Heart, 285–90. Heidelberg: Steinkopff, 1992. http://dx.doi.org/10.1007/978-3-642-72474-9_24.

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Netticadan, Thomas, Rana M. Temsah, and Naranjan S. Dhalla. "Sarcoplasmic Reticulum Gene Expression of Ca2+-Cycling Proteins as a Target for the Treatment of Heart Failure." In Cardiac Remodeling and Failure, 103–21. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4419-9262-8_7.

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Hayama, Emiko, and Toshio Nakanishi. "Developmental Differences in the Maturation of Sarcoplasmic Reticulum and Contractile Proteins in Large Blood Vessels Influence Their Contractility." In Etiology and Morphogenesis of Congenital Heart Disease, 259–61. Tokyo: Springer Japan, 2016. http://dx.doi.org/10.1007/978-4-431-54628-3_36.

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Cardi, Delphine, Cédric Montigny, Bertrand Arnou, Marie Jidenko, Estelle Marchal, Marc Maire, and Christine Jaxel. "Heterologous Expression and Affinity Purification of Eukaryotic Membrane Proteins in View of Functional and Structural Studies: The Example of the Sarcoplasmic Reticulum Ca2+-ATPase." In Methods in Molecular Biology, 247–67. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-344-2_15.

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Shimoyama, Makoto, Nobumasa Hara, Mikako Tsuchiya, Koichi Mishima, and Yoshinori Tanigawa. "ADP-Ribosyltransferase and Endogenous Acceptor Proteins in Animal Muscle Tissues: ADP-Ribosylation of Ca2+-Dependent ATPase in Rabbit Skeletal Muscle Sarcoplasmic Reticulum and the Effect of Basic Peptides." In ADP-Ribose Transfer Reactions, 7–12. New York, NY: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4615-8507-7_2.

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Tada, Michihiko, Masaaki Kadoma, Junichi Fujii, Yoshihiro Kimura, and Yoshiyuki Kijima. "Molecular Structure and Function of Phospholamban: The Regulatory Protein of Calcium Pump in Cardiac Sarcoplasmic Reticulum." In Calcium Protein Signaling, 79–89. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_9.

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Reports on the topic "Sarcoplasmic proteins"

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Braun, Alexander. The Interaction between a Thiol Specific Probe (OPA) and the Single Channel Characteristics of the Reconstituted Ca++ Release Protein from Skeletal Muscle Sarcoplasmic Reticulum. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.6745.

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You might also be interested in the extended bibliographies on the topic 'Sarcoplasmic proteins' for particular source types:
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