A comparison of heart and liver fatty acid-binding proteins: interactions with fatty acids and possible functional differences studied with fluorescent fatty acid analogues.
A comparison of heart and liver fatty acid-binding proteins: interactions with fatty acids and possible functional differences studied with fluorescent fatty acid analogues.
复制标题
心脏和肝脏脂肪酸结合蛋白的比较：与脂肪酸的相互作用以及用荧光脂肪酸类似物研究的可能的功能差异。
DOI：
10.1007/bf00231378
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发表时间：
1990
影响因子：
4.3
通讯作者：
Storch,J
中科院分区：
文献类型：
--
作者：
Storch,J
脂肪酸结合蛋白（FABP）是一类存在于哺乳动物细胞中的基因产物。它们通常以高丰度存在，并且发现于游离脂肪酸（ffa）通量高的那些组织中。FABP的功能未知。同样不知道的是，是否所有的FABP在它们各自的细胞类型中功能相似，或者不同的FABP是否具有独特的功能。这些研究的目的是评估FABP家族的不同成员是否表现出不同的结构和功能特性。ffa的两种荧光类似物用于比较肝脏（L-FABP）和心脏（H-FABP）结合蛋白。使用二苯基己三烯的丙酸衍生物（PADPH）来检查L-和H-FABP上的ffa结合位点的物理性质，以及ffa在FABP和膜之间的相对分布。一个蒽氧基衍生物的棕榈酸，2AP，用于监测FFA从肝脏或心脏FABP受体膜的转移动力学，使用共振能量转移测定。结果表明两种FABP的ffa结合位点本质上是疏水的，尽管L-FABP位点比H-FABP位点更非极性。PADPH在L-FABP和磷脂酰胆碱（PC）双层之间的平衡导致摩尔分配偏好> 20：1，L-FABP：PC。用H-FABP进行的类似研究导致PADPH分配偏好仅为3：1，H-FABP：PC。最后，发现2AP从H-FABP转移到受体膜比从L-FABP转移快50倍。这些研究表明，重要的结构和功能的差异存在于不同的FABP家族成员之间，因此意味着不同的FABP的作用可能是独特的。
Fatty acid-binding proteins (FABP) are distinct but related gene products which are found in many mammalian cell types. They are generally present in high abundance, and are found in those tissues where free fatty acid (ffa) flux is high. The function(s) of FABP is unknown. Also not known is whether all FABP function similarly in their respective cell types, or whether different FABP have unique functions. The purpose of these studies was to assess whether different members of the FABP family exhibit different structural and functional properties. Two fluorescent analogues of ffa were used to compare the liver (L-FABP) and heart (H-FABP) binding proteins. The propionic acid derivative of diphenylhexatriene (PADPH) was used to examine the physical properties of the ffa binding site on L- and H-FABP, as well as the relative distribution of ffa between FABP and membranes. An anthroyloxy-derivative of palmitic acid, 2AP, was used to monitor the transfer kinetics of ffa from liver or heart FABP to acceptor membranes, using a resonance energy transfer assay. The results demonstrate that the ffa binding sites of both FABP are hydrophobic in nature, although the L-FABP site is more nonpolar than the H-FABP site. Equilibration of PADPH between L-FABP and phosphatidylcholine (PC) bilayers resulted in a molar partition preference of > 20: 1, L-FABP: PC. Similar studies with H-FABP resulted in a PADPH partition preference of only 3:1, H-FABP: PC. Finally, the transfer of 2AP from H-FABP to acceptor membranes was found to be 50-fold faster than transfer from L-FABP. These studies demonstrate that important structural and functional differences exist between different members of the FABP family, and therefore imply that the roles of different FABP may be unique.