• The Korean Journal of Physiology and Pharmacology
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• 제6권2호
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• pp.101-107
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• 2002

In the present study, the postnatal developmental changes in the expressional levels of cardiac sarcoplasmic reticulum (SR) $Ca^{2+}$ regulatory proteins, i.e. $Ca^{2+}-ATPase,$ phospholamban, and $Ca^{2+}$ release channel, were investigated. Both SR $Ca^{2+}-ATPase$ and phospholamban mRNA levels were about 35% of adult levels at birth and gradually increased to adult levels. Protein levels of both SR $Ca^{2+}-ATPase$ and phospholamban, which were measured by quantitative immunoblotting, were closely correlated with the mRNA levels. The initial rates of $Ca^{2+}$ uptake at birth were about 40% of adult rates and also increased gradually during the myocardial development. Consequently, the relative phospholamban/$Ca^{2+}-ATPase$ ratio was 1 in developmental hearts. $Ca^{2+}$ release channel (ryanodine receptor) mRNA was about $50{\sim}60%$ at birth and increased gradually to adult level throughout the postnatal rat heart development. $^3[H]ryanodine$ binding increased gradually during postnatal myocardial development, which was closely correlated with ryanodine mRNA expression levels during the development except the ryanodine mRNA level at birth. These findings indicate that cardiac SR $Ca^{2+}-ATPase,$ phospholamban, and $Ca^{2+}$ release channel are expressed coordinately, which may be necessary for intracellular $Ca^{2+}$ regulation during the rat heart development.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2003년도 정기총회 및 학술발표회
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• pp.53-53
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• 2003

Calumenin was previously identified as a high affinity Ca$\^$2+/ binding protein in mouse cardiac sarcoplasmic reticulum (SR). For the present study, a 48 kDa skeletal homologue of calumenin was identified by sucrose-density gradient of rabbit skeletal SR membranes, concanavalin A treatment, 2D-gel electrophoresis, $\^$45/Ca$\^$2+/ overlay, Stains-all staining, and MALDI-TOF analysis. We attempted to clone the skeletal calumenin by RT-PCR based on mouse cardiac and human calumenin sequences. The deduced amino acid sequence (315 residues) of the skeletal calumenin showed high identity to mouse cardiac calumenin (90％). As seen in the cardiac calumenin, the deduced sequence contains a 19 amino acid N-terminal signal sequence and a HDEF C-terminal sequence, a putative retrieval signal to ER. Also, the skeletal calumenin contains one N-glycosylation site, three PKC phosphorylation sites, eight casein kinase 2 phosphorylation sites, and 6 EF-hand domains. GST-calumenin showed a conformational change and increased mobility in the presence of Ca$\^$2+/ in SDS-PAGE. Three calumenin interacting proteins (ryanodine receptor 1, glycogen phosphorylase, and phosphofructo kinase) were identified by pull-down assay with GST-calumenin and solubilized SR. All the interactions were Ca$\^$2+/dependent. The present results suggest that calumenin plays an important role in Ca$\^$2+/ homeostasis of muscle cells.

• 한국수산과학회지
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• 제19권4호
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• pp.333-338
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• 1986

우리 나라 전역에 걸쳐 널리 분포하고 있는 붕어와 가물치의 영양학적 기초자료를 제공하기 위하여 단백질, 구성아미노산 및 유리아미노산의 조성을 분석하고, 육단백질중 근형질단백질과 근원섬유단백질은 SDS-polyacrylamide gel 전기영동하여 그 구성 sub-unit를 검토하였다. 가물치는 붕어에 비하여 조단백질의 함량이 $3\%$가량 높았으며 Ex 분의 함량 또한 월등히 많았다. 육 단백질을 구성하는 단백질 조성은 붕어의 경우 근형질 단백질이 $32.6\%$, 근원섬유 단백질이 $62.0\%$, 알칼리가용성 단백질이 $4.9\%$, 기질 단백질이 $0.6\%$이었으며, 가물치는 근형질 단백질이 $30.7\%$, 근원섬유 단백질이 $64.1\%$, 알칼리가용성 단백질이 $4.7\%$, 기질 단백질이 $0.4\%$를 차지하고 있었다. 근형질 단백질과 근원섬유 단백질 분획의 일부에 대하여 구성 subunit를 분석한 결과, 붕어의 근형질단백질은 10개의 subunit로 구성되어 있었고, 가물치는 12개의 subunit로 구성되어 있었다. 한편 근원직유 단백질은 붕어가 19개의 subunit이었으며, 가물치는 18개 subunit로 이루어져 있었다. 단백질의 구성아미노산 조성은 lysine과 glutamic acid를 제외하고는 대체로 붕어와 가물치가 비슷한 편이었으며, glutamic acid, lysine, aspartic acid 및 arginine이 전체 구성아미노산의 약 $46\%$를 차지하고 있었다. 또한 유리아미노산조성에 있어서 붕어는 histidine이 전체유리아미노산의 $52.2\%$를 차지하고 있었으며, 가물치는 glutamic acid, glycine와 taurine이 전체유리아미노산의 약 $84.5\%$를 차지하였다. 그리고 총 유리아미노산의 양에 있어서 가물치는 붕어의 약 6.2배에 달하였다.

• 한국축산식품학회지
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• 제41권6호
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• pp.997-1011
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• 2021

The processing characteristics of freeze-dried pork powder as raw meat for comminuted meat products were compared with those of freeze-thawed pork. The tertiary structural properties, oxidation, and solubility of proteins in the freeze-dried pork powder were investigated. In addition, the properties of the emulsion gels manufactured with freeze-dried pork powder (GFD) and freeze-thawed pork (GFT) at 1.5% and 2.0% NaCl were evaluated. The surface hydrophobicity and intrinsic tryptophan fluorescence intensity of myofibrillar proteins between the freeze-dried pork powder and freeze-thawed pork were similar. However, freeze-dried pork powder had higher carbonyl compounds and lower solubility of sarcoplasmic and myofibrillar proteins than freeze-thawed pork (p<0.05). GFD had higher cooking loss than GFT in 2.0% NaCl, and lower hardness and a^* value of GFD were observed regardless of NaCl level (p<0.05). Moreover, GFD had higher malondialdehyde content than GFT at the two NaCl concentrations (p<0.05). Therefore, our study demonstrated that freeze-dried pork powder has lower functional properties than freeze-thawed pork as raw meat for comminuted meat products.

• BMB Reports
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• 제47권2호
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• pp.69-79
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• 2014

$Ca^{2+}$ release from intracellular stores and influx from extracellular reservoir regulate a wide range of physiological functions including muscle contraction and rhythmic heartbeat. One of the most ubiquitous pathways involved in controlled $Ca^{2+}$ influx into cells is store-operated $Ca^{2+}$ entry (SOCE), which is activated by the reduction of $Ca^{2+}$ concentration in the lumen of endoplasmic or sarcoplasmic reticulum (ER/SR). Although SOCE is pronounced in non-excitable cells, accumulating evidences highlight its presence and important roles in skeletal muscle and heart. Recent discovery of STIM proteins as ER/SR $Ca^{2+}$ sensors and Orai proteins as $Ca^{2+}$ channel pore forming unit expedited the mechanistic understanding of this pathway. This review focuses on current advances of SOCE components, regulation and physiologic and pathophysiologic roles in muscles. The specific property and the dysfunction of this pathway in muscle diseases, and new directions for future research in this rapidly growing field are discussed.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2003년도 정기총회 및 학술발표회
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• pp.66-66
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• 2003

In skeletal muscle cells, depolarization of the transverse tubules (T-tubules) results in Ca$\^$2+/ release from the sarcoplasmic reticulum (SR), leading to elevated cytoplasmic Ca$\^$2+/ and muscle contraction. This process has been known as excitation-contraction coupling (E-C coupling). Several proteins, such as the ryanodine receptor (RyR), triadin, junctin, and calsequestrin (CSQ), have been identified to be involved in the Ca$\^$2＋/ release process. However, the molecular interactions between the SR proteins have not been resolved. In the present study, the mechanisms of interaction between RyRl and triadin have been studied by in vitro protein binding and $\^$45/Ca$\^$2+/ overlay assays. Our data demonstrate that the intraluminal loop II of RyR1 binds to triadin in Ca$\^$2+/-independent manner. Moreover, we could not find any Ca$\^$2+/ binding sites in the loop II region. GST-pull down assay revealed that a KEKE motif of triadin, which was previously identified as a CSQ binding site (Kobayasi et al.,2000 JBC) was also a binding site for RyR1. Our results suggest that the intraluminal loop II of RyR could participate in the RyR-mediated Ca$\^$2+/ release process by offering a direct binding site to luminal triadin.

• The Journal of Korean Physical Therapy
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• 제19권4호
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• pp.1-14
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• 2007

Background: It is generally accepted that skeletal muscle contraction is triggered by nerve impulse and intracellular $Ca^{2+}\;([Ca^{2+}]_i)$ released from intracellular $Ca^{2+}$ stores such as sarcoplasmic reticulum (SR). Specifically, this process, called excitation-contraction (E-C) coupling, takes place at intracellular junctions between the plasma membrane, the transverse (T) tubule L-type $Ca^{2+}$ channel (dihydropyridine-sensitive L-rype $Ca^{2+}$ channel, DHPR, also called tetrads), and the SR $Ca^{2+}$ release channel (ryanodine-sensitive $Ca^{2+}$ release channel, RyR, also called feet) of internal $Ca^{2+}$ stores in skeletal muscle cells. Furthermore, it has been reported that the $Ca^{2+-}$ dependent and -independent contraction determine the expression of skeletal muscle genes, thus providing a mechanism for tightly coupling the extent of muscle contraction to regulation of muscle plasticity-related excitation-transcription (E-T) coupling. Purpose: Expression and activity of plasticity-associated enzymes in gastrocnemius muscle strips have not been well studied, however. Methods: Therefore, in this study the expression and phosphorylation of E-C and E-T coupling-related mediators such as protein kinases, ROS(reactive oxygen species)- and apoptosis-related substances, and others in gastrocnemius muscles from rats was examined. Results: I found that expression and activity of MAPKs (mitogen-activated protein kinases, ERK1/2, p38MAPK, and SAPK/JNK), apoptotic proteins (cleaved caspase-3, cytochrome c, Ref-1, Bad), small GTP-binding proteins (RhoA and Cdc42), actin-binding protein (cofilin), PKC (protein kinase C) and $Ca^{2+}$ channel (transient receptor potential channel 6, TRPC6) was observed in rat gastrocnemius muscle strips. Conclusion: These results suggest that MAPKs, ROS- and apoptosis-related enzymes, cytoskeleton-regulated proteins, and $Ca^{2+}$ channel may in part functionally import in E-C and E-T coupling from rat skeletal muscles.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2001년도 학술 발표회 진행표 및 논문초록
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• pp.67-67
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• 2001

Our previous studies showed that the relaxation defect of diabetic heart was due to the changes in the expressional levels of SR $Ca^{2＋}$-ATPase and PLB. In the diabetic heart contractile abnormalities were also observed, and one of the mechanisms for these changes could include alterations in the expression and/or activity levels of various $Ca^{2＋}$ regulatory proteins involving cardiac contraction.(omitted)

• Applied Biological Chemistry
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• 제14권2호
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• pp.165-169
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• 1971

Slushed ice와 dry chilling chamber에 각각 도계 직후 냉장한 12주생 영계의 가슴 및 다리 근육으로부터 KCl-phosphate buffer를 사용하여 도계후 $1{\sim}25$시간 사이에 함질소물을 추출했다. Extractable nitrogen의 변화는 주로 myosin의 extractability 감소, 그리고 어느정도 actomyosin의 extractability 증가 결과로 일어남이 밝혀졌으며, 한편 stroma. sarcoplasmic protein 및 비단백함질소물(none protein nitrogen)의 변화는 적었다. Myosin extractability는 도계후 처음 3시간 동안에 급격히 감소하여 그후 계속적으로 wet chilling 동안 감소했으나 dry chilling의 경우 myosin extractability의 감소는 가슴근육보다 다리근육에서 더 많았으며 extractability는 도계 17시간 후부터 증가했다. Actomyosin은 wet chilling의 경우 계속적으로 소량밖에 추출되지 않았으나 dry chilling의 경우 도계후 17시간 이후부터 증가했는데, 이런 경향은 breast muscle과 leg muscle이 동일했다.

• 한국축산식품학회지
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• 제31권5호
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• pp.663-667
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• 2011

This study was performed to measure the angiotensin I-converting enzyme (ACE) inhibitory activity of peptide extracts derived from the enzymatic proteolysis of Hanwoo Musculus longissimus (M. longissimus) during cold storage. Thermolysin (80 ppm, w/w) and protease type XIII (100 ppm, w/w) were injected separately or in combination for the enzymatic proteolysis of sarcoplasmic and myofibrillar proteins prior to storage at $5^{\circ}C$ (T1) or at $-1^{\circ}C$ (T2) in a chilling room for 9 days. Beef injected with thermolysin (E2) and thermolysin+protease type XIII (E3) showed a significantly higher degree of hydrolysis at both storage temperatures (p<0.05). During the storage period, T1E2 at day 6 and T1E3 at day 9 showed the strongest ACE inhibitory activity with sarcoplasmic and myofibrillar protein proteolysates. Macromolecules greater than 10,000 Da were removed by ultra filtration, and the filtrates were separated into fractions using gel filtration. Five and three major fractions were collected from S-T1E2-6 and M-T1E3-9 extracts, respectively, and the $4^{th}$ fraction of the S-T1E2-6 extracts showed the highest ACE inhibitory rate of $61.96{\pm}7.41%$.