지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2013.1
- 수록면
- 303 - 314 (12page)
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Knowledge regarding lipid catabolism has been of great interest in the field of animal sciences. In the livestock industry, excess fat accretion in meat is costly to the producer and undesirable to the consumer. However, intramuscular fat(marbling) is desirable to enhance carcass and product quality. The manipulation of lipid content to meet the goals of animal production requires an understanding of the detailed mechanisms of lipid catabolism to help meticulously design nutritional, pharmacological, and physiological approaches to regulate fat accretion. The concept of a basic system of lipases and their co-regulators has been identified. The major lipases cleave triacylglycerol(TAG) stored in lipid droplets in a sequential manner. In adipose tissue, adipose triglyceride lipase(ATGL) performs the first and rate-limiting step of TAG breakdown through hydrolysis at the sn-1 position of TAG to release a non-esterified fatty acid(NEFA) and diacylglycerol(DAG). Subsequently, cleavage of DAG occurs via the rate-limiting enzyme hormone-sensitive lipase(HSL) for DAG catabolism, which is followed by monoglyceride lipase (MGL) for monoacylglycerol(MAG) hydrolysis. Recent identification of the co-activator(Comparative Gene Identification-58) and inhibitor [G(0)/G(1) Switch Gene 2] of ATGL have helped elucidate this important initial step of TAG breakdown, while also generating more questions. Additionally, the roles of these lipolysis-related enzymes in muscle, liver and skin tissue have also been found to be of great importance for the investigation of systemic lipolytic regulation.
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참고문헌 (25)
참고문헌 신청
Ailhaud, G. / 2004 / Development of white adipose tissue. Handbook of Obesity, Etiology and Pathophysiology / Marcel Dekker : 48 ~
Bernlohr, D. A. / 2002 / Adipose tissue and lipid metabolism, In Biochemistry of Lipids, Lipoproteins and Membrances / Elsevier : 263 ~ 289
Bertrand, T. / 2010 / Structural basis for human monoglyceride lipase inhibition / J. Mol. Biol 396 : 663 ~ 673
Borgstrom, B / 1971 / Pancreatic juice co-lipase: physiological importance / Biochim. Biophys. Acta 20 : 509 ~ 513
Chakrabarti, P. / 2010 / Mammalian target of rapamycin complex 1 suppresses lipolysis, stimulates lipogenesis, and promotes fat storage / Diabetes 59 : 775 ~ 781
Bernlohr, D. A. / 2002 / Adipose tissue and lipid metabolism, In Biochemistry of Lipids, Lipoproteins and Membrances / Elsevier : 263 ~ 289
Bertrand, T. / 2010 / Structural basis for human monoglyceride lipase inhibition / J. Mol. Biol 396 : 663 ~ 673
Borgstrom, B / 1971 / Pancreatic juice co-lipase: physiological importance / Biochim. Biophys. Acta 20 : 509 ~ 513
Chakrabarti, P. / 2010 / Mammalian target of rapamycin complex 1 suppresses lipolysis, stimulates lipogenesis, and promotes fat storage / Diabetes 59 : 775 ~ 781
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