• Food Science of Animal Resources
• /
• v.18 no.4
• /
• pp.292-300
• /
• 1998

This study was undertaken to determine the influence in the Z-disk domain of titin on the tenderization of meat by the structure change of myofibrillar Z-disks during post-mortem aging. After weakening the structure of Z-disks, the Z-disk region was splitted. As the results, myofibrils were fragmented by mechanical strength. Using indirect immunofluorescence microscopy, we show that the Z-disk domain of titin was disappeared from myofibrils in this period. There phenomenon were also shown by treating myofibrils with a solution containing 0.1mM $Ca^{2+}$. We conclude that change in Z-disk domain of titin is directly effected on the tenderization of meat during post-mortem aging and these change is due to manily calcium ions.

• Asian-Australasian Journal of Animal Sciences
• /
• v.7 no.3
• /
• pp.405-411
• /
• 1994

Purified myofibrils were prepared from ante-mortem stress and control lots of Taiwan country chicken breast and thigh muscles at death and afler storage at $4^{\circ}C$ for 0, 1, 2, 3, and 7 days post-mortem. Sodium dodecyl sulfate polycrylamide gel electrophoresis (3.2%) and densitometer were used to examine the effect of ante-mortem stress and control storage of muscle on titin and nebulin. Results indicated that titin and nebulin were more rapidly degraded in the control and the ante-mortem stress light muscles than in the control and ante-mortem dark muscles of Taiwan country chicken. In contrast, nebulin was shown to be more resistance to degradation in the ante-mortem stress dark muscle than in the control light muscle.

• Biomedical Science Letters
• /
• v.12 no.4
• /
• pp.303-310
• /
• 2006

Ankyrins are a ubiquitously expressed family of intracellular adaptor proteins involved in targeting diverse proteins to specialized membrane domains in both the plasma membrane and the endoplasmic reticulum. We described here that the C-terminal domain of ankyrin-B interact specifically with Z-line portion of titin in yeast two-hybrid analysis, in vitro pull-down assays and localization experiments in COS-7 cells. In this study we provide the first experimental evidence that Z-line portion of titin is necessary for the localization of ankyrin-B and ankyrin-B links between the sarcolemma and the myofibril in costameres.

• Asian-Australasian Journal of Animal Sciences
• /
• v.17 no.10
• /
• pp.1344-1349
• /
• 2004

Titin-cap (TCAP), one of the abundant transcripts in skeletal muscles, was nvestigated in this study in cattle because of its role in regulating the proliferation and differentiation of myoblasts by interacting with the myostatin gene. From the 5, and 3, RACE experiments, full-length TCAP coding sequence was identified, comprising 166 amino acids. The amino acid comparison showed high sequence similarities with previously identified human (95.8%) and mouse (95.2%) TCAP genes. The TCAP expression, addressed by northern blot, is limited in muscle tissues as indicated by Valle et al. (1997). The radiation hybrid analysis localized the gene on BTA19, where the comparative human and porcine counterparts are on HSA17 and SSC12. A few muscle-related genetic disorders were mapped on HSA17 and some growth-related QTLs were identified on SSC12. The bovine TCAP gene found in this study opens up new possibilities for the investigation of muscle-related genetic diseases as well as meat yield traits in cattle.

• BMB Reports
• /
• v.41 no.12
• /
• pp.846-851
• /
• 2008

This study was conducted to identify marbling-related candidate genes in M. longissimus dorsi of high- and low-marbled Hanwoo. The longissimus dorsi muscles were selected for gene expression from eight Hanwoo steer carcasses based on crude fat content. In the analysis of variance, gene expression of five candidate genes, FABP4, SCD, $PPAR\gamma$, Titin and Nebulin was determined to be significantly different between high- and low-marbled Hanwoo steers (P < 0.0001). The Pik-4 and CaMK II genes were also shown to have a significant effect on crude fat content (P < 0.01). In the analysis of the differential expression between high- and low marbled groups, FABP4 gene expression was approximately 2 times higher in the high marbled group relative to the low marbled group. However, the $PPAR\gamma$ and SCD gene were highly expressed in the low marbled group. In addition, Titin and Nebulin were highly expressed in the low marbled group when placed under relatively high shear force. Finally, the Pik-4 and CaM K II gene also displayed a high expression pattern in the low marbled group.

• Asian-Australasian Journal of Animal Sciences
• /
• v.19 no.5
• /
• pp.739-743
• /
• 2006

Postmortem proteolysis of breast (BM) and leg (LM) muscles from Taiwan colored chickens (TCC) and silkie bantams (SB) at $5^{\circ}C$ were compared. Myofibrils were prepared from BM and LM samples that were randomly taken from the carcasses of SB and TCC after 0, 1, 3, 7 and 14 days of storage at $5^{\circ}C$. pH of samples was determined, and degradation of myofibrillar proteins was analyzed by the SDS-PAGE and western blots. The results showed that pH was lower in BM than in LM samples from both avian strains. Appearance of 30 kDa components and disappearance of titin and nebulin were more rapidly as seen on SDS-PAGE in BM than in LM samples. Western blots labeled with a monoclonal antibody to desmin also demonstrated that desmin degraded more quickly in BM samples. Our data might suggest that postmortem proteolysis occurred more rapidly in BM than in LM from both TCC and SB.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.27 no.3
• /
• pp.482-488
• /
• 1998

This study was carried out to determine the effect of treating with salt-fermented shrimp on quality of pig meat. The treated pig meats were stored at 4$^{\circ}C$, 1$0^{\circ}C$, 2$0^{\circ}C$ or 4$^{\circ}C$ after placing 2$0^{\circ}C$ for 35 hours, respectively. Meat tenderness was improved more at 2$0^{\circ}C$ storage than at 1$0^{\circ}C$ and 4$^{\circ}C$ storage. However, in water holding capacity, the meat stored at 4$^{\circ}C$ was increased more than them of 1$0^{\circ}C$ and 2$0^{\circ}C$. Cooking loss was decreased more at 4$^{\circ}C$ than the other storage temperatures. When meat color observed, it was good at the early stage of storage but went down to the worse gradually. According to the result of SDS-PAGE, myofibrillar proteins were degraded more after treated with salt-fermented shrimp than the control. Among them, titin-I was especially degraded after 2 days at 4$^{\circ}C$ storage even though it was degraded after 1 day at 1$0^{\circ}C$ and 2$0^{\circ}C$ storage. These results suggest that salt-fermented shrimps cause to improve the quality of pork meats by increasing the meat color, meat tenderness and water holding capacity at the early stage of storage.

• Asian-Australasian Journal of Animal Sciences
• /
• v.15 no.5
• /
• pp.721-724
• /
• 2002

Postmortem Proteolysis of breast (BM) and leg (LM) muscles in Chiayi native chickens at $5^{\circ}C$ were compared. Myofibrils were purified from BM and LM samples that were randomly taken from carcasses after 0, 1, 3, 7 and 14 days of storage at $5^{\circ}C$. Fragmentation of myofibrils were determined, and degradation of myofibrillar proteins were analyzed by the SDS-PAGE and western blots. The results showed that myofibril fragmentation index (MFI) was significantly (p<0.05) higher in BM than in LM samples. Disappearance of titin and nebulin and appearance of the 30 kDa component were more rapidly as seen on SDS-PAGE in BM than in LM samples. Western blots labeled with a monoclonal antibody to desmin also demonstrated that desmin degraded more quickly in BM samples. Our data suggested that postmortem proteolysis occurred more rapidly in breast muscles in Chiayi native chickens.

• Animal cells and systems
• /
• v.16 no.6
• /
• pp.431-437
• /
• 2012

Calpains are a class of proteins that belong to the calcium-dependent, non-lysosomal cysteine proteases. There are three major types of calpains expressed in the skeletal muscle, namely, ${\mu}$-calpain, m-calpain, and calpain 3, which show proteolytic activities. Skeletal muscle fibers possess all three calpains, and they are $Ca^{2+}$-dependent proteases. The functional role of calpains was found to be associated with apoptosis and myogenesis. However, calpain 3 is likely to be involved in sarcomeric remodeling. A defect in the expression of calpain 3 leads to limb-girdle muscular dystrophy type 2A. Calpain 3 is found in skeletal muscle fibers at the N2A line of the large elastic protein, titin. A substantial proportion of calpain 3 is activated 24 h following a single bout of eccentric exercise. In vitro studies indicated that calpain 3 can be activated 2-4 fold higher than normal resting cytoplasmic [$Ca^{2+}$]. Characterization of the calpain system in the developing muscle is essential to explain which calpain isoforms are present and whether both ${\mu}$-calpain and m-calpain exist in differentiating myoblasts. Information from such studies is needed to clarify the role of the calpain system in skeletal muscle growth. It has been demonstrated that the activation of ubiquitous calpains and calpain 3 in skeletal muscle is very well regulated in the presence of huge and rapid changes in intracellular [$Ca^{2+}$].

• Journal of the Korean Society of Surveying, Geodesy, Photogrammetry and Cartography
• /
• v.40 no.4
• /
• pp.305-313
• /
• 2022

The evolution of the GNSS (Global Navigation Satellite System) technology has enhanced positioning performance in terms of positioning accuracy and time efficiency. The technology makes it possible to determine orthometric heights at a few centimeter accuracies by transforming accurate ellipsoid heights if an accurate geoid model has been employed. This study aims to generate a correction surface using GNSS/leveling co-points and a local geoid model, Thailand Geoid Model 2017 (TGM2017), through the Kriging interpolation method in a small local area. Combining the surface and TGM2017 significantly improves height transformation with the 1-cm RMSE (Root Mean Square Error) fit of 10 GNSS/leveling reference points and a mean offset of +0.1 cm. The evaluation of the correction surface at 5 GNSS/leveling checkpoints shows the RMSE of 1.0 cm, which is 82.6 percent of accuracy improvements. The GNSS leveling method can possibly be used to replace a conventional leveling technique at a few centimeter uncertainties in the case of small areas with clear-sky and high satellite visibility environments.