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Journal articles on the topic 'Sarcoplasmic proteins'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Arai, M., K. Otsu, D. H. MacLennan, and M. Periasamy. "Regulation of sarcoplasmic reticulum gene expression during cardiac and skeletal muscle development." American Journal of Physiology-Cell Physiology 262, no. 3 (March 1, 1992): C614—C620. http://dx.doi.org/10.1152/ajpcell.1992.262.3.c614.

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The expression of major sarcoplasmic reticulum proteins during cardiac and fast-twitch skeletal muscle development was examined using gene-specific probes. Through the use of S1 nuclease mapping, Northern blot, and RNA slot-blot analysis, sarcoplasmic reticulum proteins were shown to exhibit both narrow tissue specificity and plasticity in their expression during muscle development. In fast-twitch skeletal muscle, the cardiac/slow-twitch isoforms of Ca(2+)-ATPase and calsequestrin were detected at high levels in fetal stages but were gradually replaced by fast-twitch isoforms in adult muscle. In contrast, cardiac muscle expressed exclusively cardiac/slow-twitch isoforms of Ca(2+)-ATPase and calsequestrin at all stages. Both fast-twitch and slow-twitch skeletal muscle expressed the same skeletal muscle ryanodine receptor isoform, whereas cardiac muscle expressed a cardiac isoform. Phospholamban expression was restricted to cardiac and slow-twitch skeletal muscle and did not appear in developing fast-twitch skeletal muscle. During in vitro myogenesis of C2C12 cells, the mRNA transcripts encoding sarcoplasmic reticulum proteins were found to be coordinately induced in synchrony with that of contractile protein mRNA. The myogenic factor "myogenin" induced sarcoplasmic reticulum gene transcripts along with contractile protein mRNAs in nonmyogenic cells. These data suggest that the induction of both sarcoplasmic reticulum and contractile protein gene families is under the control of a common myogenic differentiation program.

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12

Chen, Xing Xing, Xiao Hu, Lai Hao Li, Xian Qing Yang, Yan Yan Wu, Wan Ling Lin, Yong Qiang Zhao, Hai Xia Ma, and Ya Wei. "Antioxidant Properties of Tilapia Component Protein Hydrolysates and the Membrane Ultrafiltration Fractions." Advanced Materials Research 1073-1076 (December 2014): 1812–17. http://dx.doi.org/10.4028/www.scientific.net/amr.1073-1076.1812.

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In this study, three kinds of component proteins of tilapia were hydrolyzed with papain for 4h. The effect of hydrolysis and the antioxidant activities of the resulting hydrolysates were characterized. The results showed sarcoplasmic protein hydrolysate had significantly (p < 0.05) highest scavenging ability against hydroxyl, superoxide, DPPH radicals and the total reducing power. Stroma protein hydrolysate had the highest nitrogen recovery (NR) while myofibrillar protein hydrolysate had the highest degree of hydrolysis (DH). Sarcoplasmic protein hydrolysate with high radical scavenging ability was separated by membrane ultrafiltration into four molecular size fractions (<5, 5–10, 10–100, >100kDa). It was found that the antioxidant activities of the <5kDa fraction were higher than that of other fractions. Overall, sarcoplasmic protein is more efficient to obtain antioxidant properties when compared to other component proteins of tilapia.

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13

Vann, Christopher G., Paul A. Roberson, Shelby C. Osburn, Petey W. Mumford, Matthew A. Romero, Carlton D. Fox, Johnathon H. Moore, et al. "Skeletal Muscle Myofibrillar Protein Abundance Is Higher in Resistance-Trained Men, and Aging in the Absence of Training May Have an Opposite Effect." Sports 8, no. 1 (January 10, 2020): 7. http://dx.doi.org/10.3390/sports8010007.

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Resistance training generally increases skeletal muscle hypertrophy, whereas aging is associated with a loss in muscle mass. Interestingly, select studies suggest that aging, as well as resistance training, may lead to a reduction in the abundance of skeletal muscle myofibrillar (or contractile) protein (per mg tissue). Proteomic interrogations have also demonstrated that aging, as well as weeks to months of resistance training, lead to appreciable alterations in the muscle proteome. Given this evidence, the purpose of this small pilot study was to examine total myofibrillar as well as total sarcoplasmic protein concentrations (per mg wet muscle) from the vastus lateralis muscle of males who were younger and resistance-trained (denoted as YT, n = 6, 25 ± 4 years old, 10 ± 3 self-reported years of training), younger and untrained (denoted as YU, n = 6, 21 ± 1 years old), and older and untrained (denoted as OU, n = 6, 62 ± 8 years old). The relative abundances of actin and myosin heavy chain (per mg tissue) were also examined using SDS-PAGE and Coomassie staining, and shotgun proteomics was used to interrogate the abundances of individual sarcoplasmic and myofibrillar proteins between cohorts. Whole-body fat-free mass (YT > YU = OU), VL thickness (YT > YU = OU), and leg extensor peak torque (YT > YU = OU) differed between groups (p < 0.05). Total myofibrillar protein concentrations were greater in YT versus OU (p = 0.005), but were not different between YT versus YU (p = 0.325). The abundances of actin and myosin heavy chain were greater in YT versus YU (p < 0.05) and OU (p < 0.001). Total sarcoplasmic protein concentrations were not different between groups. While proteomics indicated that marginal differences existed for individual myofibrillar and sarcoplasmic proteins between YT versus other groups, age-related differences were more prominent for myofibrillar proteins (YT = YU > OU, p < 0.05: 7 proteins; OU > YT = YU, p < 0.05: 11 proteins) and sarcoplasmic proteins (YT = YU > OU, p < 0.05: 8 proteins; OU > YT&YU, p < 0.05: 29 proteins). In summary, our data suggest that modest (~9%) myofibrillar protein packing (on a per mg muscle basis) was evident in the YT group. This study also provides further evidence to suggest that notable skeletal muscle proteome differences exist between younger and older humans. However, given that our n-sizes are low, these results only provide a preliminary phenotyping of the reported protein and proteomic variables.

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14

Leong, Peng, and David H. MacLennan. "Complex interactions between skeletal muscle ryanodine receptor and dihydropyridine receptor proteins." Biochemistry and Cell Biology 76, no. 5 (October 1, 1998): 681–94. http://dx.doi.org/10.1139/o98-079.

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Evidence for functional interactions between the Ca2+ release channel in the skeletal muscle sarcoplasmic reticulum (the ryanodine receptor) and the L-type Ca2+ channel in the sarcolemma (the dihydropyridine receptor), leading to excitation-contraction coupling, is reviewed and experimental systems used to identify candidate sites of interaction are outlined.Key words: sarcoplasmic reticulum, excitation-contraction coupling.

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15

Preedy, V. R., and P. J. Garlick. "Inhibition of protein synthesis by glucagon in different rat muscles and protein fractions in vivo and in the perfused rat hemicorpus." Biochemical Journal 251, no. 3 (May 1, 1988): 727–32. http://dx.doi.org/10.1042/bj2510727.

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The effect of glucagon on the rate of muscle protein synthesis was examined in vivo and in the isolated perfused rat hemicorpus. An inhibition of protein synthesis in skeletal muscles from overnight-fasted rats at various plasma concentrations of glucagon was demonstrated in vivo. The plantaris muscle (Type II, fibre-rich) was more sensitive than the soleus (Type I, fibre-rich). Myofibrillar and sarcoplasmic proteins were equally sensitive in vivo. However, protein synthesis in mixed protein and in sarcoplasmic and myofibrillar fractions of the heart was unresponsive to glucagon in vivo. In isolated perfused muscle preparations from fed animals, the addition of glucagon also decreased the synthesis of mixed muscle proteins in gastrocnemius (Type I and II fibres) and plantaris, but not in the soleus. The sarcoplasmic and myofibrillar fractions of the plantaris were also equally affected in vitro. Similar results were observed in vitro with 1-day-starved rats, but the changes were less marked.

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16

Persson, B., E. Carlenor, N. Clyne, E. Hultman, L. E. Lins, S. K. Pehrsson, and J. Rydström. "Binding of dietary cobalt to sarcoplasmic reticulum proteins." Scandinavian Journal of Clinical and Laboratory Investigation 52, no. 2 (January 1992): 137–40. http://dx.doi.org/10.3109/00365519209088777.

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17

Schulz, Joseph S., Nathan Palmer, Jon Steckelberg, Steven J. Jones, and Michael G. Zeece. "Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1764, no. 9 (September 2006): 1429–35. http://dx.doi.org/10.1016/j.bbapap.2006.06.010.

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18

LeBLANC, E. L., S. SINGH, and R. J. LeBLANC. "Capillary Zone Electrophoresis of Fish Muscle Sarcoplasmic Proteins." Journal of Food Science 59, no. 6 (November 1994): 1267–70. http://dx.doi.org/10.1111/j.1365-2621.1994.tb14692.x.

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19

Tada, Michihiko. "Calcium Cycling Proteins of the Cardiac Sarcoplasmic Reticulum." Circulation Journal 67, no. 9 (2003): 729–37. http://dx.doi.org/10.1253/circj.67.729.

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20

Vary, Thomas C., Erik L. Owens, Jeanette K. Beers, Keith Verner, and Robert N. Cooney. "SEPSIS INHIBITS SYNTHESIS OF MYOFIBRILLAR AND SARCOPLASMIC PROTEINS." Shock 6, no. 1 (July 1996): 13–18. http://dx.doi.org/10.1097/00024382-199607000-00004.

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21

Pauls, T. L., J. A. Cox, C. W. Heizmann, and A. Hermann. "Sarcoplasmic Calcium-binding Proteins inAplysiaNerve and Muscle Cells." European Journal of Neuroscience 5, no. 6 (June 1993): 549–59. http://dx.doi.org/10.1111/j.1460-9568.1993.tb00520.x.

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22

M�ller, Frank U., Uwe Kirchhefer, Frank Begrow, Uta Reinke, Joachim Neumann, and Wilhelm Schmitz. "Junctional sarcoplasmic reticulum transmembrane proteins in the heart." Basic Research in Cardiology 97, no. 7 (May 1, 2002): 1. http://dx.doi.org/10.1007/s003950200030.

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23

Márquez-Lázaro, Johana, Darío Méndez-Cuadro, and Erika Rodríguez-Cavallo. "Residues of Fluoroquinolone Antibiotics Induce Carbonylation and Reduce In Vitro Digestion of Sarcoplasmic and Myofibrillar Beef Proteins." Foods 9, no. 2 (February 11, 2020): 170. http://dx.doi.org/10.3390/foods9020170.

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Although the impact of oxidation on human health has been of growing interest, the oxidation of proteins, major component of meat, has received little attention. This paper describes the in vitro effect of five fluoroquinolones (FQs) on carbonylation of sarcoplasmic and myofibrillar proteins of beef when found at concentrations close to the maximum residue limit (MRL). Samples were treated individually with the FQs, determining in each protein fraction the carbonyl index, protein content and oxidized proteins identification, using 2,4-dinitrophenyhydrazine (DNPH) alkaline assay, Western blot and Bradford methods, and mass spectrometry, respectively. Besides, the in vitro effect of these residues on gastric and duodenal digestion of proteins was evaluated. The carbonylation induced by FQs affected both protein fractions being significant with respect to the blank in 73.3% of cases. This damage was correlated with loss of solubility and digestibility, with sarcoplasmic proteins the most affected. Danofloxacin and enrofloxacin were the FQs with greatest oxidant effects, especially affecting glycolysis and glycogen proteins. Our results suggest that these residues induce irreversible oxidative damage on the main beef proteins and could affect their nutritional value.

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24

Mandinova, A., D. Atar, B. W. Schafer, M. Spiess, U. Aebi, and C. W. Heizmann. "Distinct subcellular localization of calcium binding S100 proteins in human smooth muscle cells and their relocation in response to rises in intracellular calcium." Journal of Cell Science 111, no. 14 (July 30, 1998): 2043–54. http://dx.doi.org/10.1242/jcs.111.14.2043.

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Changes in cytosolic Ca2+ concentration control a wide range of cellular responses, and intracellular Ca2+-binding proteins are the key molecules to transduce Ca2+ signaling via interactions with different types of target proteins. Among these, S100 Ca2+-binding proteins, characterized by a common structural motif, the EF-hand, have recently attracted major interest due to their cell- and tissue-specific expression pattern and involvement in various pathological processes. The aim of our study was to identify the subcellular localization of S100 proteins in vascular smooth muscle cell lines derived from human aorta and intestinal smooth muscles, and in primary cell cultures derived from arterial smooth muscle tissue under normal conditions and after stimulation of the intracellular Ca2+ concentration. Confocal laser scanning microscopy was used with a specially designed colocalization software. Distinct intracellular localization of S100 proteins was observed: S100A6 was present in the sarcoplasmic reticulum as well as in the cell nucleus. S100A1 and S100A4 were found predominantly in the cytosol where they were strongly associated with the sarcoplasmic reticulum and with actin stress fibers. In contrast, S100A2 was located primarily in the cell nucleus. Using a sedimentation assay and subsequent electron microscopy after negative staining, we demonstrated that S100A1 directly interacts with filamentous actin in a Ca2+-dependent manner. After thapsigargin (1 microM) induced increase of the intracellular Ca2+ concentration, specific vesicular structures in the sarcoplasmic reticulum region of the cell were formed with high S100 protein content. In conclusion, we demonstrated a distinct subcellular localization pattern of S100 proteins and their interaction with actin filaments and the sarcoplasmic reticulum in human smooth muscle cells. The specific translocation of S100 proteins after intracellular Ca2+ increase supports the hypothesis that S100 proteins exert several important functions in the regulation of Ca2+ homeostasis in smooth muscle cells.

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25

Eisenberg, Brenda R., David J. Dix, Zhaoying W. Lin, and Mary P. Wenderoth. "Relationship of membrane systems in muscle to isomyosin content." Canadian Journal of Physiology and Pharmacology 65, no. 4 (April 1, 1987): 598–605. http://dx.doi.org/10.1139/y87-101.

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The structures and functions of the various subdivisions of the membrane systems of muscle are reviewed. Morphometric data have been recalculated using functional definitions of the membranes as identified by their proteins. Thus, the junctional coupling between the sarcoplasmic reticulum and T system is separated from the remaining longitudinal sarcoplasmic reticulum that bears the calcium ATPase protein. In addition, the morphometry of the membrane systems is related to the various muscle fiber types as defined histochemically and by protein isoforms. The relation of isomyosin type and membrane quantities are compared for guinea pig, chicken, frog, and lobster skeletal muscles and rat and rabbit cardiac muscles. Fiber plasticity is considered in terms of the mixing and matching of amounts and kinds of membranes and proteins.

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26

Nakagawa, Takayuki, Shugo Watabe, and Kanehisa Hashimoto. "Identification of three major components in fish sarcoplasmic proteins." NIPPON SUISAN GAKKAISHI 54, no. 6 (1988): 999–1004. http://dx.doi.org/10.2331/suisan.54.999.

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27

Santos, N. "Hydrolysis of pork muscle sarcoplasmic proteins by Debaryomyces hansenii." International Journal of Food Microbiology 68, no. 3 (September 1, 2001): 199–206. http://dx.doi.org/10.1016/s0168-1605(01)00489-5.

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28

Farouk, M. M., K. Wieliczko, R. Lim, S. Turnwald, and G. A. MacDonald. "Cooked sausage batter cohesiveness as affected by sarcoplasmic proteins." Meat Science 61, no. 1 (May 2002): 85–90. http://dx.doi.org/10.1016/s0309-1740(01)00168-1.

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29

Wilson, George G., and Ri�tte L?J?M van Laack. "Sarcoplasmic proteins influence water-holding capacity of pork myofibrils." Journal of the Science of Food and Agriculture 79, no. 13 (October 1999): 1939–42. http://dx.doi.org/10.1002/(sici)1097-0010(199910)79:13<1939::aid-jsfa469>3.0.co;2-t.

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30

Su, Judy Y., and Luo-Jia Tang. "Effects of Halothane on the Sarcoplasmic Reticulum Ca2+Stores and Contractile Proteins in Rabbit Pulmonary Arteries." Anesthesiology 88, no. 4 (April 1, 1998): 1096–106. http://dx.doi.org/10.1097/00000542-199804000-00031.

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Background The authors' purpose of this study was to elucidate the mechanisms of direct effects of halothane on the contractile proteins and Ca2+ release from the sarcoplasmic reticulum Ca2+ stores using isolated skinned strips (sarcolemma permealized with saponin) from rabbit pulmonary arteries. Methods The sarcoplasmic reticular Ca2+ stores were examined by immersing the skinned strips sequentially in solutions to load Ca2+ into and release Ca2+ from the sarcoplasmic reticulum using caffeine, inositol 1,4,5-trisphosphate, or halothane. The contractile proteins were assessed by activating the strips with Ca2+ followed by administration of halothane (with or without protein kinase C inhibitors). Tension, fura-2 fluorescence activated by Ca2+ release, and phosphorylation of myosin light chains were measured. Results Halothane (0.07-3.00%) increased Ca2+, tension, and phosphorylation of myosin light chains in a dose-dependent manner. Halothane decreased accumulation of Ca2+ in the sarcoplasmic reticulum and enhanced the caffeine-induced tension transients. In strips pretreated with caffeine or inositol 1,4,5-trisphosphate, halothane-induced tension transients were reduced but Ca2+ was not. In strips activated by 1 microM Ca2+, halothane (0.5-3.0%) decreased 20-45% of the activated force at 15 min. Halothane (3%) transiently increased the force (20%) associated with increases in Ca2+ and phosphorylation of myosin light chains. The increased force was abolished and the subsequent relaxation was enhanced by the protein kinase C inhibitor bisindolylmaleimide but not by indolocarbazole Gö-6976. Conclusions In skinned pulmonary arterial strips, halothane, at clinical concentrations, inhibits uptake of Ca2+ by and induces release of Ca2+ from intracellular stores possibly shared by caffeine and inositol 1,4,5-trisphosphate, which are regulated by phosphorylation of myosin light chains. The time-dependent inhibition of the contractile proteins by halothane may be mediated by Ca2+-independent protein kinase C.

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31

Weaver, LaShawn A., Ronald C. Lundstrom, and A. Ann Colbert. "Identification of Shark Species by Polyacrylamide Gel Isoelectric Focusing of Sarcoplasmic Proteins." Journal of AOAC INTERNATIONAL 82, no. 5 (September 1, 1999): 1163–70. http://dx.doi.org/10.1093/jaoac/82.5.1163.

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Abstract Isoelectric focusing of muscle proteins is a fast and highly reproducible technique that has been used to identify fish species. Application of isoelectric focusing of sarcoplasmic proteins is described for identification of shark species. Sarcoplasmic protein patterns from muscle tissue of single individuals from 26 shark species and multiple individuals from 2 of the 26 shark species are shown on 1 mm thick polyacrylamide gels. Eight of these species showed pattern polymorphisms in major and minor bands; however, no individual within a species displayed the same protein pattern as that in any other species. Protein banding patterns of each species were visually distinguishable, and patterns generated on the basis of defined parameters were analyzed by a computer to obtain isoelectric points of bands, to produce schematic representations of banding patterns, and to distinguish between species-specific patterns. Isoelectric focusing appears to be an excellent method for identifying sharks. Additionally, isoelectric focusing of muscle proteins is readily applicable as a forensic tool to identify the species of shark samples received as evidence for law enforcement actions supporting shark fishery management plans.

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32

Goblet, C., and Y. Mounier. "Activation of skinned muscle fibers by calcium and strontium ions." Canadian Journal of Physiology and Pharmacology 65, no. 4 (April 1, 1987): 642–47. http://dx.doi.org/10.1139/y87-107.

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Intact and mechanically skinned skeletal muscle fibers of the crab Carcinus maenas have been used. The aim of the experiments was to determine the origin of the mechanical activity recorded in intact crab muscle fibers exhibiting an inward strontium current in strontium solution without calcium. To do so, the effect of strontium ions in inducing activation of contractile proteins and calcium release from the sarcoplasmic reticulum has been studied. The properties of the sarcoplasmic reticulum membrane towards strontium ions, i.e., the efficiency of the calcium ATPase towards strontium ions and the capability to release strontium ions have been investigated. Results show that the contractile proteins have a lower affinity for strontium than for calcium ions. However, the maximum bound strontium is identical to the maximum bound calcium. As for the sarcoplasmic reticulum, strontium ions can induce a calcium release and also can be taken up by the calcium ATPase and be released. We concluded that the mechanical activity in intact fibers bathed in a strontium medium has two origins: first, a direct and partial activation of the contractile proteins by strontium ions flowing through the calcium channel; second, a contractile proteins activation of calcium ions released by the sarcoplasmic reticulum by a "strontium-induced calcium release" mechanism.

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Ávila, Felipe, Natalia Ravello, Camila Manriquez, Felipe Jiménez-Aspee, Guillermo Schmeda-Hirschmann, and Cristina Theoduloz. "Antiglycating Effect of Phenolics from the Chilean Currant Ribes cucullatum under Thermal Treatment." Antioxidants 10, no. 5 (April 25, 2021): 665. http://dx.doi.org/10.3390/antiox10050665.

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Numerous dietary polyphenols possess antiglicating activity, but the effects of thermal treatment on this activity are mostly unknown. The effect of thermal treatment in the antiglycating activity of polyphenolic enriched extracts (PEEs) from Ribes cucullatum towards glyoxal-induced glycation of sarcoplasmic proteins was assessed. Sarcoplasmic proteins from chicken, beef, salmon, and turkey, were incubated 2 h at 60 °C with and without glyoxal and different concentrations of PEEs (0.25, 0.5, 1, and 5 mg/mL). The antiglycating activity was evaluated by: (1) Lys and Arg consumption, (2) Carboxymethyl lysine (CML) generation, and (3) lipid-derived electrophiles inhibition in a gastric digestion model. Protective effects were observed against CML generation in proteins and a decrease of electrophiles in the gastric digestion model. A dose-dependent consumption of Lys and Arg in proteins/PEEs samples, indicated the possible occurrence of quinoproteins generation from the phenolics. Protein/PEEs incubations were assessed by: (1) High pressure liquid chromatography analysis, (2) Gel electrophoresis (SDS-PAGE), and (3) Redox cycling staining of quinoproteins. Protein/PEEs incubations produced: (1) Decrease in phenolics, (2) increase of protein crosslinking, and (3) dose-dependent generation of quinoproteins. We demonstrate that phenolic compounds from R. cucullatum under thermal treatment act as antiglycating agents, but oxidative reactions occurs at high concentrations, generating protein crosslinking and quinoproteins.

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Tsutsui, H., Y. Ishibashi, K. Imanaka-Yoshida, S. Yamamoto, T. Yoshida, M. Sugimachi, Y. Urabe, and A. Takeshita. "Alterations in sarcoplasmic reticulum calcium-storing proteins in pressure-overload cardiac hypertrophy." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 1 (January 1, 1997): H168—H175. http://dx.doi.org/10.1152/ajpheart.1997.272.1.h168.

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The alterations of intracellular calcium (Ca2+) homeostasis may be responsible for the contractile defects in pressure-overload cardiac hypertrophy. The Ca(2+)-adenosinetriphosphatase (ATPase) protein level of the sarcoplasmic reticulum (SR) is reduced in the hypertrophied or failing heart. However, it is not known whether Ca(2+)-storing proteins, including calsequestrin and calreticulin, are also altered during cardiac hypertrophy. We quantified SR Ca(2+)-regulatory proteins using Western blot analysis in left ventricular (LV) muscle isolated from sham-operated control rats (n = 6) and rats with pressure overload 4 wk after abdominal aortic constriction (n = 7). The contractile function of isolated LV myocytes, assessed by the sarcomere motion measured with laser diffraction, was depressed in aortic-constricted rats. The SR Ca(2+)-ATPase protein level was decreased to 56 +/- 9% (SE) of the control value in hypertrophied myocardium (P < 0.01). The calsequestrin protein level was not altered, whereas calreticulin was increased by 120 +/- 3% of the control value in aortic-constricted rats (P < 0.05). The alterations in SR Ca(2+)-regulatory proteins were equally observed in hypertrophied hearts even when the results were normalized using the amounts of myosin heavy chain proteins in each sample. Immunohistochemical staining of calsequestrin in the control heart showed cross striations at the Z lines, whereas calreticulin was hardly observed within myocytes but was intense within interstitial fibroblasts. In the hypertrophied heart, calreticulin was observed at the perinuclear region within the myocyte cytoplasm. These data indicate that pressure-overload cardiac hypertrophy causes the alterations in SR Ca(2+)-storing proteins as well as in Ca(2+)-ATPase, which may contribute to the contractile dysfunction of the hypertrophied myocytes.

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Morioka, Katsuji, and Yutaka Shimizu. "Contribution of sarcoplasmic proteins to gel formation of fish meat." NIPPON SUISAN GAKKAISHI 56, no. 6 (1990): 929–33. http://dx.doi.org/10.2331/suisan.56.929.

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GROSSMAN, WILLIAM. "The Role of Sarcoplasmic Reticulum Proteins in Heart Disease: Introduction." Annals of the New York Academy of Sciences 853, no. 1 CARDIAC SARCO (September 1998): 207–8. http://dx.doi.org/10.1111/j.1749-6632.1998.tb08268.x.

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JORGENSEN, ANNELISE O. "Immunolocalization of Sarcoplasmic Reticulum Proteins in Mammalian Skeletal Muscle Fibers." American Zoologist 27, no. 4 (November 1987): 1021–32. http://dx.doi.org/10.1093/icb/27.4.1021.

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Mosca, Barbara, Osvaldo Delbono, Maria Messi, Leda Bergamelli, Mirko Vukcevic, Ruben Lopez, Susan Treves, Miyuki Nishi, Hiroshi Takeshima, and Francesco Zorzato. "Role of sarcoplasmic reticulum junctional proteins in skeletal muscle strength." BMC Anesthesiology 14, Suppl 1 (2014): A19. http://dx.doi.org/10.1186/1471-2253-14-s1-a19.

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39

Meyer, Markus, Wolfgang Schillinger, Burkert Pieske, Christian Holubarsch, Claus Heilmann, Herbert Posival, Goro Kuwajima, Katsuhiko Mikoshiba, Hanjörg Just, and Gerd Hasenfuss. "Alterations of Sarcoplasmic Reticulum Proteins in Failing Human Dilated Cardiomyopathy." Circulation 92, no. 4 (August 15, 1995): 778–84. http://dx.doi.org/10.1161/01.cir.92.4.778.

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40

Stephansen, Karen, Ioannis S. Chronakis, and Flemming Jessen. "Bioactive electrospun fish sarcoplasmic proteins as a drug delivery system." Colloids and Surfaces B: Biointerfaces 122 (October 2014): 158–65. http://dx.doi.org/10.1016/j.colsurfb.2014.06.053.

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41

Barone, Virginia, Davide Randazzo, Valeria Del Re, Vincenzo Sorrentino, and Daniela Rossi. "Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers." Journal of Muscle Research and Cell Motility 36, no. 6 (September 15, 2015): 501–15. http://dx.doi.org/10.1007/s10974-015-9421-5.

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Essig, David A., and Thomas M. Nosek. "Muscle Fatigue and Induction of Stress Protein Genes: A Dual Function of Reactive Oxygen Species?" Canadian Journal of Applied Physiology 22, no. 5 (October 1, 1997): 409–28. http://dx.doi.org/10.1139/h97-026.

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Definitive characterization of the mechanisms of skeletal muscle fatigue is still an area of active investigation. One emerging theory concerns a role for the reactive oxygen species (ROS) produced primarily as a consequence of elevated rates of mitochondrial respiration. It has been theorized that the long-lasting effects of low-frequency fatigue (LFF) can be attributed to disruption of some stage of the excitation contraction coupling (ECC) process. Recent evidence suggests that ROS likely denature one or more proteins directly associated with the sarcoplasmic reticulum (SR) Ca2+ release mechanism. Given the potential of ROS to damage intracellular proteins during subsequent bouts of muscle contractions, the capacity of preexisting antioxidant pathways may be complemented by the synthesis of inducible heat-stress proteins (HSPs). HSPs collectively function to maintain cellular protein conformation during stressful proteotoxic insults. The goal of this article is to illustrate how recent findings suggest a dual role of ROS generated during muscle contractions. Key words: skeletal muscle, gene expression, sarcoplasmic reticulum

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Berchtold, Martin W., Heinrich Brinkmeier, and Markus Müntener. "Calcium Ion in Skeletal Muscle: Its Crucial Role for Muscle Function, Plasticity, and Disease." Physiological Reviews 80, no. 3 (July 1, 2000): 1215–65. http://dx.doi.org/10.1152/physrev.2000.80.3.1215.

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Mammalian skeletal muscle shows an enormous variability in its functional features such as rate of force production, resistance to fatigue, and energy metabolism, with a wide spectrum from slow aerobic to fast anaerobic physiology. In addition, skeletal muscle exhibits high plasticity that is based on the potential of the muscle fibers to undergo changes of their cytoarchitecture and composition of specific muscle protein isoforms. Adaptive changes of the muscle fibers occur in response to a variety of stimuli such as, e.g., growth and differentition factors, hormones, nerve signals, or exercise. Additionally, the muscle fibers are arranged in compartments that often function as largely independent muscular subunits. All muscle fibers use Ca2+ as their main regulatory and signaling molecule. Therefore, contractile properties of muscle fibers are dependent on the variable expression of proteins involved in Ca2+ signaling and handling. Molecular diversity of the main proteins in the Ca2+ signaling apparatus (the calcium cycle) largely determines the contraction and relaxation properties of a muscle fiber. The Ca2+ signaling apparatus includes 1) the ryanodine receptor that is the sarcoplasmic reticulum Ca2+ release channel, 2) the troponin protein complex that mediates the Ca2+ effect to the myofibrillar structures leading to contraction, 3) the Ca2+pump responsible for Ca2+ reuptake into the sarcoplasmic reticulum, and 4) calsequestrin, the Ca2+storage protein in the sarcoplasmic reticulum. In addition, a multitude of Ca2+-binding proteins is present in muscle tissue including parvalbumin, calmodulin, S100 proteins, annexins, sorcin, myosin light chains, β-actinin, calcineurin, and calpain. These Ca2+-binding proteins may either exert an important role in Ca2+-triggered muscle contraction under certain conditions or modulate other muscle activities such as protein metabolism, differentiation, and growth. Recently, several Ca2+signaling and handling molecules have been shown to be altered in muscle diseases. Functional alterations of Ca2+ handling seem to be responsible for the pathophysiological conditions seen in dystrophinopathies, Brody's disease, and malignant hyperthermia. These also underline the importance of the affected molecules for correct muscle performance.

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Franzini-Armstrong, Clara. "Architecture and regulation of the Ca2+ delivery system in muscle cellsThis paper is one of a selection of papers published in this Special Issue, entitled 14th International Biochemistry of Exercise Conference – Muscles as Molecular and Metabolic Machines, and has undergone the Journal’s usual peer review process." Applied Physiology, Nutrition, and Metabolism 34, no. 3 (June 2009): 323–27. http://dx.doi.org/10.1139/h09-017.

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The junctional domain of sarcoplasmic reticulum (jSR) is specialized for receiving signals from the plasmalemma–transverse tubules and for releasing Ca2+ during muscle activation. The junctional face of the jSR, facing the transverse tubules, is occupied by a molecular complex composed of the transmembrane Ca2+ release channels (ryanodine receptors); the luminal protein calsequestrin (CSQ); the 2 membrane proteins, junctin (Jct), and triadin (Tr), which mediate CSQ-ryanodine receptor interactions; and several other components. Under the conditions prevailing within the sarcoplasmic reticulum lumen (physiological ionic strength, mostly due to K+ and Ca2+ ions), CSQ forms long linear polymers and the fixed protein gel is clearly visible in the electron microscope. The luminal domains of Jct and Tr are detectable but, overall, the 2 molecules are not clearly delineated. Cardiac muscles either overexpressing or bearing null mutations for 3 proteins of the junctional complex (CSQ, Jct, and Tr) reveal the contribution of these 3 components to the general architecture of the jSR.

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Fadda, Silvina, Yolanda Sanz, Graciela Vignolo, M. Concepción Aristoy, Guillermo Oliver, and Fidel Toldrá. "Hydrolysis of Pork Muscle Sarcoplasmic Proteins byLactobacillus curvatus and Lactobacillus sake." Applied and Environmental Microbiology 65, no. 2 (February 1, 1999): 578–84. http://dx.doi.org/10.1128/aem.65.2.578-584.1999.

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ABSTRACT Lactobacillus curvatus CECT 904 and Lactobacillus sake CECT 4808 were selected on the basis of their proteolytic activities against synthetic substrates. Further, the effects of whole cells, cell extracts, and a combination of both enzymatic sources on muscle sarcoplasmic proteins were determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography analyses. Strains of both species displayed proteinase activities on five sarcoplasmic proteins. The inoculation of whole cells caused a degradation of peptides, whereas the addition of cell extracts resulted in the generation of both hydrophilic and hydrophobic peptides. This phenomenon was remarkably more pronounced when L. curvatus was involved. Whole cells also consumed a great amount of free amino acids, while the addition of intracellular enzymes contributed to their generation.L. sake accounted for a greater release of free amino acids. In general, cell viability and also proteolytic events were promoted when cell suspensions were provided with cell extracts as an extra source of enzymes.

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MIYAGUCHI, Yuji, Kiyami NAGAYAMA, and Masakazu TSUTSUMI. "Thermal and Functional Properties of Porcine Sarcoplasmic Proteins: A Comparison with Some Wateroluble Animal Proteins." Nihon Chikusan Gakkaiho 71, no. 4 (2000): 416–24. http://dx.doi.org/10.2508/chikusan.71.416.

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Babu, Gopal J., Debra Wheeler, Oscar Alzate, and Muthu Periasamy. "Solubilization of membrane proteins for two-dimensional gel electrophoresis: identification of sarcoplasmic reticulum membrane proteins." Analytical Biochemistry 325, no. 1 (February 2004): 121–25. http://dx.doi.org/10.1016/j.ab.2003.10.024.

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48

Feng, Xiaolong, Di Wu, Kun Yang, Limei Wang, Xian Wang, Jing Ma, Yunhua Zhang, Caili Wang, Yuanhua Zhou, and Weiqing Sun. "Effect of sarcoplasmic proteins oxidation on the gel properties of myofibrillar proteins from pork muscles." Journal of Food Science 86, no. 5 (April 15, 2021): 1835–44. http://dx.doi.org/10.1111/1750-3841.15687.

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49

Lygren, B., and K. Taskén. "Compartmentalized cAMP signalling is important in the regulation of Ca2+ cycling in the heart." Biochemical Society Transactions 34, no. 4 (July 21, 2006): 489–91. http://dx.doi.org/10.1042/bst0340489.

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Co-ordinated myocyte handling of calcium is essential for efficient excitation–contraction coupling in the heart. The calcium cycling activity can be modulated by adrenergic stimulation and subsequent phosphorylation. Important functional consequences of phosphorylation include a greater influx of calcium through the voltage-dependent L-type Ca2+ channel and a greater release of calcium from SR (sarcoplasmic reticulum) through the ryanodine R2 receptor. Furthermore, a more efficient reuptake through SERCA2 (sarcoplasmic/endoplasmic-reticulum Ca2+-ATPase 2) is a result of phosphorylation of its regulatory protein phospholamban. Compartmentalized signalling is important in this signalling cascade, and A-kinase-anchoring proteins play a central role by providing a high level of specificity.

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Elgamouz, Alsaidi, Alsaidi, Zahri, Almehdi, and Bajou. "The Effects of Storage on Quality and Nutritional Values of Ehrenberg’s Snapper Muscles (Lutjanus Ehrenbergi): Evaluation of Natural Antioxidants Effect on the Denaturation of Proteins." Biomolecules 9, no. 9 (September 2, 2019): 442. http://dx.doi.org/10.3390/biom9090442.

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: Protein denaturation in frozen minced fillets (Ehrenberg’s Snapper), stored at −25°C was studied; 50.0 mg biomass/50g mince fillets treated with cinnamon, cumin, turmeric, garlic, ginger and 25.0 mg of vitamin C were used to slow protein denaturation. FT-IR stretching vibration of Amide-A (νNH) at 3300 cm−1; Amide-I stretching (νC=O) between 1600−1690 cm−1 and Amide-II stretching (νCN) and bending (δNH) between 1480 and 1575cm−1 were used as marker peaks. Garlic was the most significant (P ≤0.01) in controlling the rate of protein denaturation when νNH was used as a marker peak. DSC analysis showed that turmeric presented the highest effect on delaying the denaturation of sarcoplasmic proteins with a ∆H0=73.7J/g followed by garlic-treated mince fillets ∆H0=70.1J/g. All spices used were efficient in stopping the denaturation of myosin with the highest ∆H0=769.3 J/g registered for cinnamon-treated mince fillets. Actin was less vulnerable to denaturation in comparison to myosin and sarcoplasmic proteins.

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