• Title/Summary/Keyword: Calpain-6

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Calpain-10 SNP43 and SNP19 Polymorphisms and Colorectal Cancer: a Matched Case-control Study

  • Hu, Xiao-Qin;Yuan, Ping;Luan, Rong-Sheng;Li, Xiao-Ling;Liu, Wen-Hui;Feng, Fei;Yan, Jin;Yang, Yan-Fang
    • Asian Pacific Journal of Cancer Prevention
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    • v.14 no.11
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    • pp.6673-6680
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    • 2013
  • Objective: Insulin resistance (IR) is an established risk factor for colorectal cancer (CRC). Given that CRC and IR physiologically overlap and the calpain-10 gene (CAPN10) is a candidate for IR, we explored the association between CAPN10 and CRC risk. Methods: Blood samples of 400 case-control pairs were genotyped, and the lifestyle and dietary habits of these pairs were recorded and collected. Unconditional logistic regression (LR) was used to assess the effects of CAPN10 SNP43 and SNP19, and environmental factors. Both generalized multifactor dimensionality reduction (GMDR) and the classification and regression tree (CART) were used to test gene-environment interactions for CRC risk. Results: The GA+AA genotype of SNP43 and the Del/Ins+Ins/Ins genotype of SNP19 were marginally related to CRC risk (GA+AA: OR = 1.35, 95% CI = 0.92-1.99; Del/Ins+Ins/Ins: OR = 1.31, 95% CI = 0.84-2.04). Notably, a high-order interaction was consistently identified by GMDR and CART analyses. In GMDR, the four-factor interaction model of SNP43, SNP19, red meat consumption, and smoked meat consumption was the best model, with a maximum cross-validation consistency of 10/10 and testing balance accuracy of 0.61 (P < 0.01). In LR, subjects with high red and smoked meat consumption and two risk genotypes had a 6.17-fold CRC risk (95% CI = 2.44-15.6) relative to that of subjects with low red and smoked meat consumption and null risk genotypes. In CART, individuals with high smoked and red meat consumption, SNP19 Del/Ins+Ins/Ins, and SNP43 GA+AA had higher CRC risk (OR = 4.56, 95%CI = 1.94-10.75) than those with low smoked and red meat consumption. Conclusions: Though the single loci of CAPN10 SNP43 and SNP19 are not enough to significantly increase the CRC susceptibility, the combination of SNP43, SNP19, red meat consumption, and smoked meat consumption is associated with elevated risk.

Melittin Inhibits DU-145 Cell Proliferation Through Induction of Apoptosis (멜라틴이 세포자멸사 유발에 의해 DU-145 세포증식에 미치는 영향)

  • Shim, Yoon-Seop;Song, Ho-Sueb
    • Journal of Acupuncture Research
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    • v.26 no.3
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    • pp.49-58
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    • 2009
  • 목적 : 본 연구는 봉약침의 주요성분인 멜리틴이 전립선 암세포주인 DU-145 세포성장에 어떤 영향을 미치는지를 알아보기 위하여 시행하였다. 방법 : 멜리틴이 DU-145의 성장에 미치는 영향을 알아보기 위한 cell viability 측정으로는 WST-1 assay를, 세포자멸사의 관찰에는 DAPI(4,6-diamidino-2-phenylindole)와 TUNEL staining assay를 시행하였으며, 세포자멸사 조절단백질(calpain, Bax, caspase-3, -9, cleaved caspase-3, cleavaged PARP, cleaved caspase-9, Bcl-2, XIAP, cIAP2, Akt, p-Akt, MMP-2, MMP-13)의 관찰을 위하여 western blot analysis를 시행하였다. 결과 : 1. DU-145 세포에서 멜리틴을 처리한 후 세포자멸사가 유도되어 세포성장이 억제되었다. 2. 세포자멸사 관련 단백질 중 분리된 caspase-3, caspase-9은 유의한 증가를, Bcl-2, p-Akt, XIAP, cXIAP는 유의한 감소를 나타내었다. 결론 : 이상의 결과는 멜리틴이 인간 전립선암세포주인 DU-145의 세포자멸사를 유발함으로써 증식억제 효과가 있음을 나타낸 것으로, 전립선암의 예방과 치료에 대한 효과적인 치료제 개발에 도움이 될 것으로 기대된다.

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Aging mechanism for improving the tenderness and taste characteristics of meat

  • Seon-Tea Joo;Eun-Yeong Lee;Yu-Min Son;Md. Jakir Hossain;Chan-Jin Kim;So-Hee Kim;Young-Hwa Hwang
    • Journal of Animal Science and Technology
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    • v.65 no.6
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    • pp.1151-1168
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    • 2023
  • Tenderness and taste characteristics of meat are the key determinants of the meat choices of consumers. This review summarizes the contemporary research on the molecular mechanisms by which postmortem aging of meat improves the tenderness and taste characteristics. The fundamental mechanism by which postmortem aging improves the tenderness of meat involves the operation of the calpain system due to apoptosis, resulting in proteolytic enzyme-induced degradation of cytoskeletal myofibrillar proteins. The improvement of taste characteristics by postmortem aging is mainly explained by the increase in the content of taste-related peptides, free amino acids, and nucleotides produced by increased hydrolysis activity. This review improves our understanding of the published research on tenderness and taste characteristics of meat and provides insights to improve these attributes of meat through postmortem aging.

Limb-girdle Muscular Dystrophy (지대형 근이양증)

  • Kim, Dae-Seong
    • Annals of Clinical Neurophysiology
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    • v.6 no.2
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    • pp.65-74
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    • 2004
  • Limb-girdle muscular dystrophy (LGMD) is a heterogeneous group of inherited muscle disorders caused by the mutations of different genes encoding muscle proteins. In the past, when the molecular diagnostic techniques were not available, the subtypes of muscular dystrophies were classified by the pattern of muscle weakness and the mode of inheritance, and LGMD had been considered as a 'waste basket' of muscular dystrophy because many unrelated heterogeneous cases with 'limb-girdle' weakness were put into the category of LGMD. With the advent of molecular genetics at the end of the last century, it has been known that there are many subtypes of LGMD caused by the mutation of different genes, and now, LGMD is classified according to the results of the linkage analysis and the genes or proteins affected. Only small proportion (probably less than 10%) of LGMD is dominantly inherited, and autosomal dominant LGMD (AD-LGMD) consists of six subtypes (LGMD1A to 1F) so far. In autosomal recessive LGMD (AR-LGMD), more than 10 subtypes (LGMD2A to 2J) have been linked and most of the causative genes have been identified. Among AR-LGMDs, LGMD2A (calpain 3 deficiency), 2B (dysferlin deficiency), and sarcoglycanopathy (LGMD2C-2F) are major subtypes. The defective proteins in LGMDs are components of nuclear envelope, cytosol, sarcomere, or sarcolemma, and seem to play a different role in the pathogenesis of muscular dystrophy. It is notable that many causative genes of LGMDs are also responsible for other categories of muscular dystrophy or diseases affecting other tissue. However, by which mechanism they produce such a broad phenotypic variability is still unknown. The identification of mutation in the relevant gene is confirmative for the diagnosis, and is essential for genetic counseling and antenatal diagnosis of LGMD. Because many different genes are responsible for LGMD, differentiation of subtypes using immunohistochemistry and western blotting is the essential step toward the detection of mutation. For the effective research and medical care of the patients with muscular dystrophy in Korea, a research center with a medical facility supported by the government seems to be needed.

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Purification of a 17,000-Dalton Inhibitor of Ca2+_Activated Protease from Neoplastic Tissues of Human Stomach (사람의 위암조직으로부터 Ca2+_Activated Protease를 저해하는 17kDa_단백질의 분리)

  • Seol, Jae-Hong;Park, Sang-Cheol;Ha, Du-Bong;Jeong, Jin-Ha
    • The Korean Journal of Zoology
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    • v.31 no.4
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    • pp.295-299
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    • 1988
  • An endogenous 17-6a inhibitor of Caa+_activated protease has been purified from neo-plastic tissues of human stomach using heat treahent and conventional chromatographir procedures. It appears to consist of a single polvpeptide since the same molecular weight was obtained by both gel fntration under nondenaturing condition and gel electrophoresis in the presence of SDS. Since the size of the inhibitor or is the smallest amens those reported so far, it may represent a functional unit for inhibiting Caa+_activated protease. This protein is also capable of inhibiting the protease isolated loom chick skeletal muscle. Thus, the functional unit of the inhibitor most well be conserved during evolution. Howrver, it remains unclear what may be the physiological significance of the presence of the Iow-molecular weight form of the inhibitor in neoplastic tissues of human stomach. 사람의 위암조직으로부터 Ca2)_activated protease을 저해하는 단백질을 열처리 및 여러 크로마토그라피 방법을 이용하여 순수분리 하였다. 이 저해단백질은SDS-전기영동카자1 filtra-tion의 방법에 의하여 그 분자량이 17 kDa으로 나타남으로 보아 단일 Polypeptide로 구성되어 있음을 알 수 있었다. 이 저해 단백질의 분자량은 지금까지 알려진 CaB+_activated protease의 저해단백질에 비하여 가장 작은 것이었다. 따라서, 이 단.백질은 Ca2)에 의하여 활성화되는 단백질 분해효소의 작용을 저해하는 기능적 단위로 추측되었다. 한편, 이 저해제는 계 골격근에서 추출한 Ca2+ _activated protease의 촹성 도 억제 하는 것으로 나타났다. 이러 한 결과는 이 저 해 단백질의 기능적 단위가 진화과정 동안 오래 보존되어 왔음을 시사한다. 그러나, 사람의 위암조직에서 이 저해제가 무슨 이유로 가장 작은 분자량의 단백질로 존재하는지에 대한 생리학적 중요성에 관한 문제는 앞으로 많이 연구되어져 야 할 것이다.

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Mapping of the Porcine Calpastatin Gene and Association Study of Its Variance with Economic Traits in Pigs

  • Choi, B.H.;Lee, J.S.;Jang, G.W.;Lee, H.Y.;Lee, J.W.;Lee, K.T.;Chung, H.Y.;Park, H.S.;Oh, S.J.;Sun, S.S.;Myung, K.H.;Cheong, I.C.;Kim, T.H.
    • Asian-Australasian Journal of Animal Sciences
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    • v.19 no.8
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    • pp.1085-1089
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    • 2006
  • The objectives of this study were to confirm a location of the calpastatin (CAST) gene in chromosome 2 and to detect associations of genetic variations with economic traits in the porcine CAST gene as a candidate gene for growth and meat quality traits in pigs. Calpastatin is a specific endogenous inhibitor of calpains. The calpain protease system is ubiquitous, and is involved in numerous growth and metabolic processes. Three single nucleotide variations were identified within a 1.6 kb fragment of the porcine CAST gene and these polymorphisms were used for genetic linkage mapping. Linkage and QTL mapping were performed with the National Livestock Research Institute (NLRI) reference families using eight microsatellites and SNP makers in the CAST gene. The porcine CAST gene was mapped adjacent to the markers, SW395 and SW1695 on SSC2 with LOD scores of 15.32 and 8.50, respectively. According to the QTL mapping, a significant association was detected at 82 cM between SW395 and CAST-Hinf I for weight at the age of 30 weeks. In addition, an association study was performed with the $F_2$ animals of NLRI reference families for Hinf I, Msp I and Rsa I polymorphisms in the CAST gene. Two polymorphisms, CAST-Rsa I and CAST-Hinf I, showed significant correlation for growth traits at p<0.01 and p<0.05, respectively.

The Influence of Vacuum Packaging of Hot-Boned Lamb at Early Postmortem Time on Meat Quality during Postmortem Chilled Storage

  • Zhao, Yingxin;Chen, Li;Bruce, Heather L.;Wang, Zhenyu;Roy, Bimol C.;Li, Xin;Zhang, Dequan;Yang, Wei;Hou, Chengli
    • Food Science of Animal Resources
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    • v.42 no.5
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    • pp.816-832
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    • 2022
  • To evaluate the effects of early postmortem vacuum packaging (VP) on meat quality during postmortem chilled storage, hot-boned lamb was vacuum-packaged at 1, 6, 12, 24, and 48 h postmortem and stored around 2℃ until 168 h postmortem, with lamb packaged in plastic wrap as the control (aerobic packaging). Intramuscular pH decline was delayed when lamb was vacuum packaged at 1, 6, and 12 h postmortem (p<0.05). The lamb vacuum-packaged at 1 h postmortem (VP-1h group) had significantly lower shear force values and purge losses accompanied by lower free thiol group values than other treatments during postmortem storage and was also higher in extractable calpain-1 activity by 6 h postmortem (p<0.05). Free thiol group concentrations were significantly higher after VP at 6 and 12 h postmortem (p<0.05). Packaging lamb under vacuum very early postmortem produced the lowest shear force and purge loss, likely by slowing heat loss and muscle temperature decline, implying that lamb quality is improved by VP when applied very early postmortem. This was at the expense of protein oxidation, which was unrelated to other meat quality measurements, most likely because potential contracture during hot boning confounded its impact. Further research is required to understand the implications of the interaction between protein oxidation, VP, and hot boning on the acceptability of lamb.