• Title, Summary, Keyword: bovine muscle

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Purification and Properties of Bovine Skeletal Muscle Proteasome

  • Yamamoto, S.;Gerelt, B.;Nishiumi, T.;Suzuki, A.
    • Asian-Australasian Journal of Animal Sciences
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    • v.18 no.6
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    • pp.884-891
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    • 2005
  • This paper describes the purification and properties of a multicatalytic proteinase complex, proteasome, from bovine skeletal muscle, in comparision with proteasome prepared from other species or organs. The purified bovine skeletal muscle proteasome exhibited a single band on polyacrylamide gel electrophoresis under nondenaturing conditions. Bovine skeletal muscle proteasome degraded synthetic peptides maximally at pH 8.0. Relative to pH 8.0, activities were gradually decreased with the lowering pH, but the extent of decrease was substrate-dependent, and the activity at pH 5.5 still retained 78-10% of the activity at pH 8.0, indicating the possibility that the proteasome is active in muscle during aging. When the proteasome was heated at 60$^{\circ}C$ for 15 or 30 min and treated in the presence of 0.0125% SDS, the activity increased over 1.8 and 3.1 times (LLVY (Suc-Leu-Leu-Val-Tyr-NH-Mec) as a substrate), respectively. These results (activation with heat or SDS) indicate that the hydrolytic activity of proteasome was stimulated under mild denaturing conditions. The characteristics of the bovine skeletal muscle proteasome obtained in our experiment were almost the same as those of the proteasome prepared from other species or organs.

Muscle Fiber Typing in Bovine and Porcine Skeletal Muscles Using Immunofluorescence with Monoclonal Antibodies Specific to Myosin Heavy Chain Isoforms

  • Song, Sumin;Ahn, Chi-Hoon;Kim, Gap-Don
    • Food Science of Animal Resources
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    • v.40 no.1
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    • pp.132-144
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    • 2020
  • The aim of this study was to optimize staining procedures for muscle fiber typing efficiently and rapidly in bovine and porcine skeletal muscles, such as longissimus thoracis, psoas major, semimembranosus, and semitendinosus muscles. The commercially available monoclonal anti-myosin heavy chain (MHC) antibodies and fluorescent dye-conjugated secondary antibodies were applied to immunofluorescence histology. Two different procedures, such as cocktail and serial staining, were adopted to immunofluorescence analysis. In bovine muscles, three pure types (I, IIA, and IIX) and one hybrid type, IIA+IIX, were identified by the cocktail procedure with a combination of BA-F8, SC-71, BF-35, and 6H1 anti-MHC antibodies. Porcine muscle fibers were typed into four pure types (I, IIA, IIX, and IIB) and two hybrid types (IIA+IIX and IIX+IIB) by a serial procedure with a combination of BA-F8, SC-71, BF-35, and BF-F3. Unlike for bovine muscle, the cocktail procedure was not recommended in porcine muscle fiber typing because of the abnormal reactivity of SC-71 antibody under cocktail procedure. Within the four antibodies, combinations of two or more anti-MHC antibodies allowed us to distinguish pure fiber types or all fiber types including hybrid types. Application of other secondary antibodies conjugated with different fluorescent dyes allowed us to get improved image resolution that clearly distinguished hybrid fibers. Muscle fiber characteristics differed depending on species and muscle types.

Effects of Hydrostatic Pressure Treatment on the Physicochemical, Morphological, and Textural Properties of Bovine Semitendinosus Muscle

  • Kim, Yun-Ji;Lee, Eun-Jung;Lee, Nam-Hyouck;Kim, Young-Ho;Yamamoto, Katsuhiro
    • Food Science and Biotechnology
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    • v.16 no.1
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    • pp.49-54
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    • 2007
  • The effects of hydrostatic pressure (HP) treatment on the physicochemical, morphological, and textural properties of bovine semitendinosus (ST) muscle were assessed. Based on SDS-PAGE, the decrease in HP-treated ST muscle protein solubility in 0.1 M KCl buffer (pH 7.0) was attributable to a reduction in the levels of sarcoplasmic protein, and the protein solubility decrease observed in 0.6 M KCl buffer (PH 7.0) was attributable to a reduction in the levels of myosin heavy-chain and actin. Scanning electron microscope (SEM) observations showed that muscle fibers became finer and more compact with increasing pressures. The shear force and hardness of ST muscle pressurized to 300 MPa decreased significantly (p<0.05), however samples pressurized at 100 and 500 MPa exhibited a significant increase in both attributes relative to the control sample (p<0.05).

Analysis of Differentially Expressed Proteins in Bovine Longissimus Dorsi and Biceps Femoris Muscles

  • Kim, S.M.;Park, M.Y.;Seo, K.S.;Yoon, D.H.;Lee, H.-G.;Choi, Y.J.;Kim, S.H.
    • Asian-Australasian Journal of Animal Sciences
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    • v.19 no.10
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    • pp.1496-1502
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    • 2006
  • Skeletal muscle contains slow and fast twitch fibers. These skeletal muscle fibers express type I and type II myosin, respectively, and these myosin isoenzymes have different ATPase activity. The aim of this study was to investigate protein profiles of bovine skeletal muscles by proteomic analysis. Fifty seven spots of distinct proteins were excised and characterized. The expression of sixteen spots was differed in longissimus dorsi muscle with a minimal 2-fold change compared to biceps femoris muscle. The majority of differentially expressed proteins belonged to metabolic regulation-related proteins such as glyceraldehyde 3-phosphate dehydrogenase, triosephosphate isomerase and carbonic anhydrase 3. The real time-PCR assay confirmed an increase or induction of specific genes: RGS12TS isoform, GAPDH, triosephosphate isomerase and carbonic anhydrase. These results suggest that the expression of metabolic proteins is under a specific control system in different bovine skeletal muscle. These observations could have significant implications for understanding the physiological regulation of bovine skeletal muscles.

Comparison of Myosin ATPase Activities from Red Muscle and White Muscle (Red muscle myosin과 White muscle myosin의 생물활성의 비교)

  • Shin, Wan-Chul;Oh, Doo-Whan;Jhin, Hong-Seung;Kim, Kee-Tae;Yang, Ryung
    • Korean Journal of Food Science and Technology
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    • v.18 no.3
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    • pp.181-186
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    • 1986
  • Myosin were prepared from red muscle and white muscle, and their ATPase activities were compared. Ca-ATPase activity of bovine myosin from red muscle was higher than that of myosin from white muscle, while Ca-ATPase activity of chicken myosin from red muscle differed hardly from that of myosin from whitemuscle. Atso EDTA-ATPase activity of bovine red muscle myosin was higher than that of white muscle myosin ,although EDTA-ATPase activity of chicken myosin from red muscle differed hardly from that of white muscle myosin. When myosins were treated with trypsin, bovine myosin from white muscle was hydrolysed moreeasily than red muscle myosin was. Chicken myosin from red muscle , however, was hydrolysed by trypsin more easily than white muscle myosin was.

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Effect of Gender-Specific Adult Bovine Serum on Gene Expression During Myogenesis

  • Lee, Eun-Ju;Pokharel, Smritee;Kim, Jie-Hoe;Nam, Sang-Sup;Choi, In-Ho
    • Journal of Animal Science and Technology
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    • v.54 no.3
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    • pp.219-226
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    • 2012
  • Gender specificity in muscle growth and development is well known. Genesis of muscle is dependent on proliferation and differentiation potential of resident myogenic satellite cells (MSCs) present in muscle fibers. Multipotential capacity of forming myocyte, osteocyte, and adipocyte like cell makes MSCs a unique stem cell. To understand the molecular mechanism involved in determination of muscle quality due to difference in hormone concentration of different gender of animals, MSCs were isolated from bovine skeletal muscle and cultured in male, female, and castrated serum supplemented media. DNA microarray used consisted of 24,000 spots with 70 mer oligo in each spot. A total of 88 genes were up-regulated and 551 genes were down-regulated by more than two fold. Among up-regulated gene, 33, 34, and 21 genes were found up-regulated in cells grown in male, female, and castrated serum, respectively. Interestingly, male serum showed 4, female 11 and castrated male showed 4 genes expressed highly in each gender. Further study on the highly up-regulated gene may unfold the mystery of gender specificity found in muscle development. Also, the identification of differentially expressed genes in gender-specific serum will add information on infrastructure of bovine genome research.

Investigation into the Distribution of Total, Free, Peptide-bound, Protein-bound, Soluble-and Insoluble-Collagen Hydroxyproline in Various Bovine Tissues

  • Siddiqi, Nikhat J.;Alhomida, Abdullah S.
    • BMB Reports
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    • v.36 no.2
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    • pp.154-158
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    • 2003
  • Collagen is a family of proteins which consists of several genetically distinct molecular species and is intimately involved in tissue organization, function, differentiation and development. The purpose of this study was to investigate the concentration of different hydroxyproline (Hyp) fractions viz., total, free, peptide-bound, protein-bound, soluble- and insoluble-collagen hydroxyproline (Hyp) in various bovine tissues. Results showed that liver had the highest concentration of free Hyp followed by kidney, brain, spleen, lungs, muscle and heart. Liver also had the highest concentration of peptide-bound collagen Hyp followed by kidney, heart, spleen, lungs, brain and muscle. The concentration of protein-bound collagen Hyp was highest in the liver, followed by kidney, spleen, lungs, muscle, brain and heart. Total Hyp was highest in the liver, followed by kidney, spleen, brain, heart, muscle and lungs. Liver also had significantly high concentration of collagen as compared to other tissues examined (P<0.001). Spleen had the significantly higher concentration of soluble-collagen Hyp when compared to other tissues (P<0.001). This was followed by heart, muscle, lungs, brain, kidney and liver. Heart had the highest concentration of insoluble-collagen Hyp followed by lungs, kidney, liver, muscle, spleen and brain. The variation among the insoluble-collagen Hyp concentration of heart and muscle, spleen and brain was significant (P<0.001). We speculate that these differences could be due to the variation in turn over of rate of collagen metabolism in this species.

Functional study of Villin 2 protein expressed in longissimus dorsi muscle of Korean native cattle in different growth stages

  • Jin, Yong-Cheng;Han, Jeng-A;Xu, Cheng-Xiong;Kang, Sang-Kee;Kim, Sang-Hun;Seo, Kang-Suk;Yoon, Du-Hak;Choi, Yun-Jaie;Lee, Hong-Gu
    • BMB Reports
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    • v.45 no.2
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    • pp.102-107
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    • 2012
  • The aim of this study was to investigate protein profiles related to the induction of adipogenesis within the bovine longissimus dorsi muscle (BLDM) by proteomic analysis. We analyzed BLDM proteins at different growth stages to clarify the physiological mechanisms of marbled muscle development in 20 head of Korean native cattle (11 month: 10 head, 17 month: 10 head). BLDM proteins were analyzed by two-dimensional electrophoresis and image analysis. Villin 2 was specifically identified by mass spectrometry and a protein search engine. Villin 2 protein expression in BLDM decreased during the fat development stage in test steers. In a Western blot cell culture study of spontaneously immortal bovine muscle fibroblasts, the abundance of Villin 2 was shown to be down-regulated during differentiation into muscle. In 3T3-L1 mouse embryonic fibroblasts, Villin 2 was decreased during differentiation into adipocytes. The results suggest that Villin 2 may be related to the induction of transdifferentiation and adipogenesis in bovine longissimus dorsi muscle.

Steroid Effects on Cell Proliferation, Differentiation and Steroid Receptor Gene Expression in Adult Bovine Satellite Cells

  • Lee, Eun Ju;Choi, Jinho;Hyun, Jin Hee;Cho, Kyung-Hyun;Hwang, Inho;Lee, Hyun-Jeong;Chang, Jongsoo;Choi, Inho
    • Asian-Australasian Journal of Animal Sciences
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    • v.20 no.4
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    • pp.501-510
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    • 2007
  • The present study was conducted to establish primary bovine muscle satellite cell (MSC) culture conditions and to investigate the effects of various steroid hormones on transcription of the genes involved in muscle cell proliferation and differentiation. Of three different types of proteases (type II collagenase, pronase and trypsin-EDTA) used to hydrolyze the myogenic satellite cells from muscle tissues, trypsin-EDTA treatment yielded the highest number of cells. The cells separated by hydrolysis with type II collagenase and incubated on gelatin-coated plates showed an enhanced cell attachment onto the culture plate and cell proliferation at an initial stage of cell growth. In this study, the bovine MSCs were maintained in vitro up to passage 16 without revealing any significant morphological change, and even to when the cells died at passage 21 with decreased or almost no cell growth or deformities. When the cells were incubated in a steroid-depleted environment (DMEM(-)/10% CDFBS (charcoal-dextran stripped FBS)), they grew slowly initially, and were widened and deformed. In addition, when the cells were transferred to an incubation medium containing steroid (DMEM(+)/10% FBS), the deformed cells resumed their growth and returned to a normal morphology, suggesting that steroid hormones are crucial in maintaining normal MSC morphology and growth. The results demonstrated that treatments with 19-nortestosterone and testosterone significantly increased AR gene expression (p<0.05), implying that both testosterone and 19-nortestosterone bind with AR and that the hormone bound-AR complex up-regulates the genes of its own receptor (AR) plus other genes involved in satellite cell growth and differentiation in bovine muscle.