Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes.
Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes.
复制标题
荧光脂肪酸从脂肪细胞脂肪酸结合蛋白转移到细胞膜的机制。
DOI:
10.1021/bi00084a033
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发表时间:
1993
期刊:
影响因子:
2.9
通讯作者:
Storch,J
中科院分区:
文献类型:
--
作者:
Wootan,MG;Bernlohr,DA;Storch,J
Revised Manuscript Received May 4, 1993 abstract: Adipocyte fatty acid binding protein (A-FABP) is a 15-kDa protein found in high abundance in the cytosol of adipose cells. Tobetter understand the role of this protein in intracellular free fatty acid (ffa) transport, the mechanism of ffa transfer from A-FABP to model membranes was examined by monitoring the transfer of fluorescent anthroyloxy ffa (AOffa) to smallunilamellar phospholipid vesicles, using a resonance energy transfer assay. Structural features of ffa that increase aqueous solubility, such as shorter chain length and unsaturation, did not increase the AOffa transfer rate. In addition, solution conditions that increase the aqueous solubility of ffa, such as decreasing ionic strength and increasing pH, had little effect on AOffa transfer from A-FABP to membranes. These results suggest that AOffa do not transfer through theaqueous phase. The smallentropic contribution to the free energy of the transfer process provides further evidence that AOffa maynot travel through the surrounding aqueous environment when transferred from A-FABP to phospholipid membranes. Finally, the rate of AOffa transfer from A-FABP was directly dependent on the concentration of the acceptor membranes. These studies suggest that AOffa transfer from A-FABP to phospholipid vesicles may occur via transient collisional interactions between the protein and membranes. Such a mechanism is similar to that found recently for AOffa transfer from heart FABP [Kim,. K., & Storch, J.(1992) J. Biol. Chem. 267, 20051-20056], an FABP which possesses a high degree of sequence homology (62% identity) with A-FABP, but different from the aqueous diffusion mechanism described for the more distantly related (20% homology) liverFABP [Kim,. K., & Storch, J.(1992) J. Biol. Chem. 267, 77-82]. These differences indicate that structural divergence among FABP may be translated into functional differences, as evidenced here by the mechanism of AOffa transfer to membranes.
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DOI:
10.1016/0005-2736(77)90168-7
发表时间:
1977
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
L. Thilo
通讯作者:
L. Thilo
影响因子:
4.7
作者:
K. Uyemura;T. Kato;K. Kitamura
通讯作者:
K. Kitamura
DOI:
--
发表时间:
1990
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Storch,J;Bass,NM
通讯作者:
Bass,NM
DOI:
--
发表时间:
1988
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Steck,TL;Kezdy,FJ;Lange,Y
通讯作者:
Lange,Y
DOI:
10.1073/pnas.81.17.5468
发表时间:
1984-01-01
期刊:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子:
--
作者:
BERNLOHR, DA;ANGUS, CW;KELLY, TJ
通讯作者:
KELLY, TJ