Stress protein induction in skeletal muscle: comparison of laboratory models to naturally occurring hypertrophy

1994 ◽  
Vol 76 (2) ◽  
pp. 598-601 ◽  
Author(s):  
J. L. Kilgore ◽  
B. F. Timson ◽  
D. K. Saunders ◽  
R. R. Kraemer ◽  
R. D. Klemm ◽  
...  

The purpose of the study was to compare stress protein [heat shock protein (HSP) 72] response in laboratory models of hypertrophy to naturally occurring work-induced hypertrophy. Two laboratory models of hypertrophy inducement, namely, compensatory hypertrophy and stretch hypertrophy, were compared with hypertrophy resulting from migratory flight in the blue-winged teal. We hypothesized that HSP 72 would be expressed more strongly in hypertrophied muscle than in control muscle. Furthermore, we hypothesized that changes occurring in laboratory models would also occur in work-induced enlargement. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analyses were used to assess HSP 72 levels in control and hypertrophied muscle. Laboratory models elicited similar responses, with increased HSP 72 content in hypertrophied muscle. Work-induced hypertrophy or disuse atrophy did not change the degree of HSP 72 expression in the blue-winged teal. The presence of HSP 72 in these conditions may indicate that stressors eliciting changes in muscle protein expression, including the loss of muscle mass, may elicit HSP 72 synthesis.

1982 ◽  
Vol 28 (11) ◽  
pp. 1265-1272
Author(s):  
E. Pinina Norrod ◽  
Robert P. Williams

Phenotypic changes in the colonial morphology of four opacity variants of Neisseria gonorrhoeae strain F62 occurred upon growth in the presence of 14 mM pyruvate. Each of the naturally occurring opacity variants, a transparent, an opaque, and two deeply opaque, became more opaque; in addition, colonies of the opaque variants became rougher. Pyruvate did not appear to have a direct function in these colonial changes. Its effects were due to the ability of pyruvate to retard the oxidation of cysteine that was added to the medium in a defined supplement. Sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE) of outer membranes showed that the opacity-associated proteins of the naturally occurring variants were not affected by growth in the presence of pyruvate; therefore, the induced opacity changes appear to have another basis. However, other proteins were affected. SDS–PAGE of the outer membranes, as well as of cell fractions composed predominantly of cytosol and of cytoplasmic membranes, revealed quantitative differences in the protein profiles after growth in the presence of pyruvate of each variant.


2006 ◽  
Vol 12 (5) ◽  
pp. 417-421 ◽  
Author(s):  
J. Val ◽  
M. A. Gracia ◽  
A. Blanco ◽  
E. Monge ◽  
M. Pérez

Polypeptides from the apple pulp of Smoothee Golden Delicious and White Renete apples were resolved by 1-D denaturing sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). According to the electropherograms, there were lower concentrations of 88, 74, 70.6 and 47.5-42kDa proteins in bitter pit spots. Proteins weighing 30 and 26kDa were rare in sound pulp but frequently appeared in pits and adjacent tissue. Finally, a novel 18kDa protein was found in bitter pit spots in both varieties, and also in chemically induced corky lesions either by magnesium infiltration or ammonium oxalate cortical injections. The available data suggested that the novel protein might be an inhibitor of pectinmethylesterase, a small heat stress protein (smHSP) or a product of the Ypr-10 gene family identified with ‘Mal d 1’, the main allergen of apples. To elucidate the possible smHSP nature of the 18kDa, a set of apples were heated at 40°C for 20h, developing this protein in both the oxidised tissue and in the adjacent.


2000 ◽  
Vol 68 (3) ◽  
pp. 1608-1619 ◽  
Author(s):  
Christopher Elkins ◽  
K. John Morrow ◽  
Bonnie Olsen

ABSTRACT Haemophilus ducreyi is resistant to killing by normal serum antibody and complement. We discovered an H. ducreyiouter membrane protein required for expression of serum resistance and termed it DsrA (for “ducreyi serum resistance A”). ThedsrA locus was cloned, sequenced, and mutagenized. An isogenic mutant (FX517) of parent strain 35000 was constructed and characterized, and it was found to no longer express dsrA. FX517 was at least 10-fold more serum susceptible than 35000. DsrA was expressed by all strains of H. ducreyi tested, except three naturally occurring, avirulent, serum-sensitive strains. FX517 and the three naturally occurring dsrA-nonexpressing strains were complemented in trans with a plasmid expressingdsrA. All four strains were converted to a serum-resistant phenotype, including two that contained truncated lipooligosaccharide (LOS). Therefore, serum resistance in H. ducreyi does not require expression of full-length LOS but does require expression ofdsrA. The dsrA locus from eight additionalH. ducreyi strains was sequenced, and the deduced amino acid sequences were more than 85% identical. The major difference between the DsrA proteins was due to the presence of one, two, or three copies of the heptameric amino acid repeat NTHNINK. These repeats account for the variability in apparent molecular mass of the monomeric form of DsrA (28 to 35 kDa) observed in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Since DsrA is present in virulent strains, is highly conserved, and is required for serum resistance, we speculate that it may be a virulence factor and a potential vaccine candidate.


2018 ◽  
Vol 10 (1) ◽  
pp. 41-46
Author(s):  
R.N. OLADOSU-AJAYI ◽  
I.T. OMONIYI ◽  
H.E. DIENYE

Oladosu-Ajayi RN, Omoniyi IT, Dienye HE. 2018. Muscle protein bands resolved by Sarotherodon melanotheron from fresh and brackish water habitats. Nusantara Bioscience 10: 40-45. An electrophoretic analysis of muscle protein of Sarotherodon melanotheron from freshwater (Eleiyele Reservoir, Ibadan, Nigeria) and brackish water (Lekki Lagoon, Lagos, Nigeria) was carried out using the Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). The protein banding patterns for the fish species were distinguishable. The freshwater S. melanotheron samples displayed 15-22 protein bands with the male samples having the highest while the brackish water S. melanotheron samples displayed 13-20 protein bands with the female having the highest. The freshwater S. melanotheron were also observed to have resolved a higher range of protein bands of molecular weights ranging between 20 kd to 99 kd than the brackish water species, which resolved protein bands of lower molecular weights ranging between 20 kd to 95 kd. The electrophoretic analysis of muscle proteins revealed that SDS-PAGE can be considered a good taxonomic criterion to differentiate among and within fish species.


1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).


1976 ◽  
Vol 36 (01) ◽  
pp. 071-077 ◽  
Author(s):  
Daniel E. Whitman ◽  
Mary Ellen Switzer ◽  
Patrick A. McKee

SummaryThe availability of factor VIII concentrates is frequently a limitation in the management of classical hemophilia. Such concentrates are prepared from fresh or fresh-frozen plasma. A significant volume of plasma in the United States becomes “indated”, i. e., in contact with red blood cells for 24 hours at 4°, and is therefore not used to prepare factor VIII concentrates. To evaluate this possible resource, partially purified factor VIII was prepared from random samples of fresh-frozen, indated and outdated plasma. The yield of factor VIII protein and procoagulant activity from indated plasma was about the same as that from fresh-frozen plasma. The yield from outdated plasma was substantially less. After further purification, factor VIII from the three sources gave a single subunit band when reduced and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. These results indicate that the approximately 287,000 liters of indated plasma processed annually by the American National Red Cross (ANRC) could be used to prepare factor VIII concentrates of good quality. This resource alone could quadruple the supply of factor VIII available for therapy.


1982 ◽  
Vol 47 (01) ◽  
pp. 014-018 ◽  
Author(s):  
H Sumi ◽  
N Toki ◽  
S Takasugi ◽  
S Maehara ◽  
M Maruyama ◽  
...  

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.


2018 ◽  
Vol 26 (2) ◽  
pp. 058
Author(s):  
Anna P. Roswiem ◽  
Triayu Septiani

<em>Bahan<strong> </strong>baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE).<strong> </strong>Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi  dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.</em>


2020 ◽  
Vol 20 (8) ◽  
pp. 970-981
Author(s):  
Hamed A. Ghramh ◽  
Essam H. Ibrahim ◽  
Mona Kilnay

Background: Juniperus procera and Majra honey are well-known as a folk medicine in many countries. Objectives: This work aimed to study the immunomodulatory effects after mixing Majra honey, J. procera water leaves extract and silver Nanoparticles (AgNPs) on immune or cancer cells. Methods: Juniperus procera water leaves extract and 20% Majra honey were prepared. Both the extract and honey were used separately to synthesize AgNPs. AgNPs were characterized using UV/Vis spectrophotometry and electron microscopy. Bioactive molecules in honey and the extract were explored using Fourier Transform Infrared (FT-IR) spectroscopy. Protein profile of honey was explored using Sodium Dodecyl Sulfate- Polyacrylamide Gel Electrophoresis (SDS-PAGE) and honey sugar content was determined using High- Performance Liquid Chromatography (HPLC). Biological activities of honey and the extract were tested. Results: The results demonstrated the ability of the extract/honey to produce AgNPs in a spherical shape. The extract/honey contained many functional groups. SDS-PAGE of Majra honey showed many protein bands. HPLC revealed honey is of good quality and no external additives are added to it. The extract and extract+ AgNPs inhibited the growth of normal rat splenic cells while honey stimulated it. The extract+honey turned stimulatory to the splenic cells’ growth and significantly diminished the inhibitory potential of the extract containing AgNPs. Both the extract and honey have antimicrobial activities, this potential increased in the presence of AgNPs. Honey and Honey+AgNPs inhibited HepG2 cancer cell proliferation while Hela cell growth inhibited only with honey+AgNPs. Conclusion: Both honey and the extract have antibacterial and immunomodulatory potentials as well as the power to produce AgNPs. Majra honey alone showed anticancer activity against HepGe2 cells, but not against Hela cells, and when contained AgNPs had anticancer activity on both cell lines. Mixing of Majra honey with J. procera extract showed characterized immunomodulatory potentials that can be described as immunostimulant.


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