Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes

Wootan, Margo G.; Bernlohr, David A.; Storch, Judith

doi:10.1021/bi00084a033

Cited by 64 publications

(72 citation statements)

References 50 publications

(62 reference statements)

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“…With few exceptions [19][20][21], no significant difference in binding affinity has been found among FABP types or among fatty acids within a type [6,[22][23][24]. However, the rate of transfer of FABP-bound fatty acids to acceptor membranes varies greatly among types [25][26][27][28] and may reflect the functional diversity of FABPs. In particular, hearttype FABP transfers fatty acids to acceptor membrane 50-fold faster than does liver-type FABP [29].…”

Section: Figure 6 Differences Between Primary Structure Of Teleost H mentioning

confidence: 99%

“…In particular, hearttype FABP transfers fatty acids to acceptor membrane 50-fold faster than does liver-type FABP [29]. Heart and adipose FABPs both transfer FABPs at a ' fast ' rate relative to liver FABP and both transfer fatty acids via similar collisional mechanisms [25,26], but the rate of fatty acid transfer is affected by pH, ionic strength, phospholipid head-group charge on acceptor membranes and surface charge on donating FABPs [25,26,28,30]. Accordingly, Herr et al [30] proposed that FABPs may target fatty acid delivery to different intracellular compartments based on variation in organelle membrane lipid composition.…”

Section: Figure 6 Differences Between Primary Structure Of Teleost H mentioning

confidence: 99%

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Two distinct types of fatty acid-binding protein are expressed in heart ventricle of Antarctic teleost fishes

Vayda

Londraville

Cashon

et al. 1998

Biochemical Journal

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This report provides the first evidence for the existence of two distinct types of fatty acid-binding protein (FABP) in cardiac tissue of vertebrates. Four species of Antarctic teleost fish (Chaenocephalus aceratus, Cryodraco antarcticus, Gobionotothen gibberifrons and Notothenia coriiceps) exhibited two FABP mRNAs of 1.0 kb and 0.8 kb, which we have termed Hh-FABP and Had-FABP (isolated from eart tissue, with similarity to mammalian eart-type FABP or mammalian ipose-type FABP respectively). These FABP types appear to be products of distinct genes. Both FABP transcripts were abundant in cardiac and aerobic pectoral muscle. However, relative abundance of the two types varied distinctly among other tissues such as kidney, brain, spleen and white muscle. Neither FABP type was expressed in liver or intestine. The coding regions of Hh-FABP and Had-FABP cDNAs from the same species are only ~ 60% identical with one another. However, homologues of each FABP species, which exhibit > 98% identity to their respective types, were isolated from three other Antarctic teleosts. Phylogenetic analysis of aligned amino-acid sequences places Hh-FABP with other vertebrate heart-type FABPs, and Had with adipose/cutaneous FABPs. Expression of two distinct FABPs in cardiac tissue of Antarctic teleosts may be related to their ability to both utilize fatty acid as the primary metabolic fuel and to store lipid intracellularly.

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Section: Figure 6 Differences Between Primary Structure Of Teleost H mentioning

confidence: 99%

Section: Figure 6 Differences Between Primary Structure Of Teleost H mentioning

confidence: 99%

Two distinct types of fatty acid-binding protein are expressed in heart ventricle of Antarctic teleost fishes

Vayda

Londraville

Cashon

et al. 1998

Biochemical Journal

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“…Alternatively, metabolic abnormalities may arise due to ineffi cient interactions between KLBP and intracellular proteins or membranes. Differences in the mechanism of ligand transfer from protein to phospholipid vesicles have been documented between LBPs, and in some cases, have been attributed to specifi c charged residues [8][9][10][11]. These observations have prompted us to explore the biochemical and biophysical characteristics of the two proteins.…”

Section: Introductionmentioning

confidence: 99%

Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes

Simpson

LiCata

Coe

et al. 1999

Lipid Binding Proteins Within Molecular and Cellular Biochemistry

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“…A FABP has been proposed to be involved in the intracellular trafficking and targeting of fatty acids (3,4). In vitro studies have indicated that the transfer of fatty acids from AFABP to vesicles occurs during direct collisional interactions between the protein and acceptor membranes; however, the fatty acid transfer properties of KFABP have not been reported.…”

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confidence: 99%

“…5 µmol/l phospholipid. Higher concentrations of AFABP were necessitated by the low 12AO quantum yield (3). The decrease in n-(9-anthroyloxy) fatty acid (AOFA) fluorescence upon mixing with acceptor membranes containing 10 mol% of the energy transfer quencher 2-{12-[(7-nitrobenz-2-oxa-1,3-d i a z o l -4 -y l ) a m i n o ] d o d e c a n o y l } -1 -h e x a d e c a n o y l -s n -g l y e r c o -3 -p h o s p h o c h o l i n e (NBDPC) was monitored with a DX-17MV stopped-flow spectrofluorimeter (Applied Photophysics, Leatherhead, U.K.), and data were analyzed by exponential fitting, as previously described (15).…”

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confidence: 99%

Adipocyte metabolism in adipocyte fatty acid binding protein knockout mice (aP2-/-) after short-term high-fat feeding: functional compensation by the keratinocyte [correction of keritinocyte] fatty acid binding protein.

et al. 2000

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Mice null for adipocyte fatty acid binding protein ( A FABP) compensate by increasing expression of keratinocyte fatty acid binding protein (KFABP) (Hotamisligil et al. S c i e n c e 274:1377-1379, 1996). In the present s t u d y, AFABP knockout (KO) and wild-type (WT) mice became equally obese on a high-fat diet, as judged by fat pad weights, adipocyte size, and body composition analysis. High-fat feeding led to moderate insulin resistance in both WT and AFABP knockout mice, as indicated by an ~2-fold increase in plasma insulin. H o w e v e r, in the high fat-fed mice, plasma glucose levels were ~15% lower in the AFABP-KO mice. Adipocytes isolated from AFABP-KO and WT mice fed high-or low-fat diets exhibited similar rates of basal and norepinephrine-stimulated lipolysis and insulinstimulated rates of glucose conversion to fatty acids and glyceride-glycerol. However, basal glucose conversion to fatty acids was higher in adipocytes of AFA B P -KO mice. Adipocyte tumor necrosis factor-r e l e a s e was similarly increased by high-fat diet-induced obesity in both WT and AFABP-KO mice. As assessed by We s tern blot analysis, the level of KFABP protein in A FABP-KOs was ~40% of the level of AFABP in WT controls. The binding affinities of KFABP for longchain fatty acids were 2-to 4-fold higher than those of A FA B P, but the relative affinities for different fatty acids were similar. As for AFA B P, the rate of fatty acid transfer from KFABP to model phospholipid vesicles was increased with acceptor membrane concentration and by inclusion of acidic phospholipids, indicating a similar mechanism of transfer. We conclude KFABP can functionally compensate for the absence of AFA B P, resulting in no major alterations in adipocyte metabolism or fat accumulation in response to short-term feeding of high-fat diets that result in moderate hyperinsulinemia. D i a b e t e s 4 9 :9 0 4-911, 2000

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Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes

Cited by 64 publications

References 50 publications

Two distinct types of fatty acid-binding protein are expressed in heart ventricle of Antarctic teleost fishes

Two distinct types of fatty acid-binding protein are expressed in heart ventricle of Antarctic teleost fishes

Biochemical and biophysical analysis of the intracellular lipid binding proteins of adipocytes

Adipocyte metabolism in adipocyte fatty acid binding protein knockout mice (aP2-/-) after short-term high-fat feeding: functional compensation by the keratinocyte [correction of keritinocyte] fatty acid binding protein.

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