• Journal of Animal Science and Technology
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• 제55권6호
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• pp.515-520
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• 2013

Pyruvate kinase M2 (PKM2) is a key regulatory enzyme in the glycolytic pathway. It is one of four pyruvate kinase isoenzymes that widely differ in their occurrence according to tissue type. PKM2 is expressed in differentiated tissues, such as fat tissues, lung, as well as normal proliferating cells, embryonic cells, and tumor cells. The objective of this study was to investigate the association of single nucleotide polymorphisms (SNPs) in the PKM2 gene with meat quality traits in Berkshire pigs. We detected a SNP (g.34341 A>G) in the 3'UTR region of the PKM2 gene in 670 Berkshire pigs through DNA sequencing. Three genotypes, AA, AG, and GG, were found for this SNP, but based on an association analysis with meat quality traits, genotype AA was significantly associated with thicker back fat than genotype GG (p=0.027). Therefore, the g.34341 A>G polymorphism in the 3'UTR region of the porcine PKM2 gene could be applied in pig breeding programs to improve back fat thickness.

• 대한약학회:학술대회논문집
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• 대한약학회 2001년도 Proceedings of the Pharmaceutical Society of Korea
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• pp.119.1-119.1
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• 2001

• 대한약학회:학술대회논문집
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• 대한약학회 2000년도 춘계총회 및 학술대회
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• pp.116.1-116.1
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• 2000

• 대한약학회:학술대회논문집
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• 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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• pp.267.3-268
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• 2002

Aggregation of the high affinity 1gE receptor on mast cells results in many biochemical. events leading to the release of histamine. serotonin. prostaglandins arachidonic acid metabolites, and cytokines. Previously we have shown that M2 pyruvate kinase interacts with the gamma chain of 1gE receptor on the ITAM (immunoreceptor tyrosine-based activation motif) region. (omitted)

• Toxicological Research
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• 제32권1호
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• pp.47-56
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• 2016

The identification of biomarkers for the early detection of acute kidney injury (AKI) is clinically important. Acute kidney injury (AKI) in critically ill patients is closely associated with increased morbidity and mortality. Conventional biomarkers, such as serum creatinine (SCr) and blood urea nitrogen (BUN), are frequently used to diagnose AKI. However, these biomarkers increase only after significant structural damage has occurred. Recent efforts have focused on identification and validation of new noninvasive biomarkers for the early detection of AKI, prior to extensive structural damage. Furthermore, AKI biomarkers can provide valuable insight into the molecular mechanisms of this complex and heterogeneous disease. Our previous study suggested that pyruvate kinase M2 (PKM2), which is excreted in the urine, is a sensitive biomarker for nephrotoxicity. To appropriately and optimally utilize PKM2 as a biomarker for AKI requires its complete characterization. This review highlights the major studies that have addressed the diagnostic and prognostic predictive power of biomarkers for AKI and assesses the potential usage of PKM2 as an early biomarker for AKI. We summarize the current state of knowledge regarding the role of biomarkers and the molecular and cellular mechanisms of AKI. This review will elucidate the biological basis of specific biomarkers that will contribute to improving the early detection and diagnosis of AKI.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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• pp.260-260
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• 1994

Mammalian pyruvate dehydrogenase complex(PDC) enzyme consists of multiple oopies of three major oligomeric enzymes-El, E2 E3. And protein X is one of the enzymatic constituents which is tightly bound to E2 subunit This complex enzyme is responsible for the oxidative decarboxylation of pyruvate producing of acetyl CoA which is a key intermediate for the entry of carbohydrates into the TCA cycle for its complete metabolic conversion to CO$_2$. And the overall activity of the complex enzyme is regulated via covalent nodification of El subunit by a El specific phosphatase ad kinase. Protein X has lipoyl moiety that undergoes reduction and acetylation during ezymatic reaction and has been known h be involved in the binding of E3 subunit to E2 core and in the regulatory activity of kinase. The purification of protein X has not been achieved majorly because of its tight binding to E2 subunit The E2-protein X subcomplex was obtained by the established methods and the detachment of protein X from E2 was accomplished in the 0.1M borate buffer containing 150mM NaCl. During the storage of the subcomplex in frozen state at -70$^{\circ}C$, the E2 subunit was precipitated and the dissociated protein X was obtained by cntrifegation into the supernatant The verification of protein X was accomplished by (1)the migration on SDS-PAGE, (2)acetylation by 〔2$\^$-l4/C〕 pyruvate, and (3)internal amino acid sequence analysis of tryptic digested enzyme.

• 한국미생물·생명공학회지
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• 제14권6호
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• pp.495-500
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• 1986

단백질, 아미노산 등 각종 질소화합물의 공존하에서 $10^{-5}$M (0.01 $\mu$mole/$m{\ell}$)의 미량암모니아 정량이 가능한 효소적 분석법에 관하여 검토하였다. Glutamine synthetase의 L-glutamine합성 반응에서 생성되는 무기린정량법에 의하면 암모니아정량 범위는 0.01-0.10mM이였다. Glutamine synthetase와 pyruvate kinase 및 lactate dehydrogenase의 공역계를 이용하여 340nm에서의 NADH 산화에 의한 흡광도감소에 의하여 암모니아를 정량하였다. 이 방법의 정량범위는 0.01-0.05mM이었으며 반응계의 조성은 phosphoenol pyruvate, 3mM; L-glutamate, 10mM; ATP, 1mM; MgSO$_4$, 20mM;KCl, 75mM; NADH, 0.2mM; Tris-HCl buffer(pH 7.0), 100mM; pyruvate kinase, 10U/$m{\ell}$; lactate dehydrogenase, 12U/$m{\ell}$과 glutamine synthetase, 4U/$m{\ell}$이었다. 효소반응은 3$0^{\circ}C$에서 20분간 예비반응 후 각 농도의 염화암모니움을 가한후 3$0^{\circ}C$에서 30분간 반응시켰다. Glutamine synthetase와 glutamate synthase의 공역계를 사용한 암모니아정량법의 암모니아정량 범위는 0.01-0.05mM이었으며 반응계의 조성은 ATP, 5mM; L-glutamate, 5mM; $\alpha$-ketoglutarate, 5mM; MgCl$_2$, 1.5mM; NADPH, 0.15mM; Tris- HCl buffer(pH7.0) 100mM;glutamine synthetase, 1U/$m{\ell}$과 glutamate synthase, 0.5U/$m{\ell}$ 이었다. 효소반응은 3$0^{\circ}C$에서 20분간 예비반응시킨 후 각 농도의 염화암모니움을 가하여 3$0^{\circ}C$에서 30분간 반응시켰다.

• 대한약학회:학술대회논문집
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• 대한약학회 2000년도 NEW STRATEGY FOR DRUG DEVELOPMENT IN POST-GENOMIC ERA(대한약학회)
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• pp.147.1-147.1
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• 2000

• 대한약학회:학술대회논문집
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• 대한약학회 2001년도 Proceedings of International Convention of the Pharmaceutical Society of Korea
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• pp.133.2-133.2
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• 2001

• Molecules and Cells
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• 제42권9호
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• pp.628-636
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• 2019

Altered genetic features in cancer cells lead to a high rate of aerobic glycolysis and metabolic reprogramming that is essential for increased cancer cell viability and rapid proliferation. Pyruvate kinase muscle (PKM) is a rate-limiting enzyme in the final step of glycolysis. Herein, we report that PKM is a potential therapeutic target in triple-negative breast cancer (TNBC) cells. We found that PKM1 or PKM2 is highly expressed in TNBC tissues or cells. Knockdown of PKM significantly suppressed cell proliferation and migration, and strongly reduced S phase and induced G2 phase cell cycle arrest by reducing phosphorylation of the CDC2 protein in TNBC cells. Additionally, knockdown of PKM significantly suppressed $NF-{\kappa}B$ (nuclear factor kappa-light-chain-enhancer of activated B cells) activity by reducing the phosphorylation of p65 at serine 536, and also decreased the expression of $NF-{\kappa}B$ target genes. Taken together, PKM is a potential target that may have therapeutic implications for TNBC cells.