Characterization of an Acyl-CoA Thioesterase That Functions as a Major Regulator of Peroxisomal Lipid Metabolism
作者:Mary C. Hunt、Karianne Solaas、B. Frode Kase、Stefan E.H. Alexson
DOI:10.1074/jbc.m106458200
日期:2002.1
sequestration and to facilitate excretion of chain-shortened carboxylic acids, acyl-CoA thioesterases, which catalyze the hydrolysis of acyl-CoAs to the free acid and CoASH, may play important roles. Here we have cloned and characterized a peroxisomal acyl-CoA thioesterase from mouse, named PTE-2 (peroxisomal acyl-CoA thioesterase 2). PTE-2 is ubiquitously expressed and induced at mRNA level by treatment
过氧化物酶体在极长链脂肪酸和长链脂肪酸,二羧酸脂肪酸,胆汁酸中间体,前列腺素,白三烯,血栓烷,pristanic酸和异种生物羧酸的β-氧化中起作用。这些脂质主要是作为羧酸排泄缩短链,或运输到线粒体进行进一步代谢。这些羧酸中的几种被缓慢氧化,因此可能螯合辅酶A(CoASH)。为防止CoASH螯合并促进链缩短的羧酸的排泄,可催化酰基CoA水解为游离酸和CoASH的酰基CoA硫酯酶可能起重要作用。在这里,我们从小鼠克隆并表征了过氧化物酶体酰基辅酶A硫酯酶,称为PTE-2(过氧化物酶体酰基辅酶A硫酯酶2)。通过用过氧化物酶体增殖物WY-14643处理和禁食,PTE-2在mRNA水平普遍表达和诱导。这些治疗方法所见的诱导作用取决于过氧化物酶体增殖物激活的受体α。重组PTE-2对酰基辅酶A表现出宽的链长特异性,从短链,中链到长链酰基辅酶A,以及其他底物,包括三羟基辅前列腺酸辅酶A,羟甲基戊二酰辅酶A和