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

Vayda, E. Michael; Londraville, Richard L.; Cashon, E. Robert; Costello, Lori; Sidell, D. Bruce

doi:10.1042/bj3300375

Cited by 37 publications

(30 citation statements)

References 32 publications

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“…Vertebrate heart typically displays only the H-isoform because it imports its fatty acids and induction of A-FABP in heart of hibernating ground squirrels (transcripts were not found in euthermic heart) is a first in the mammalian literature. Its presence could serve two functions : (1) because A-FABP also occurs in the hearts of Antarctic teleost fishes (Vayada et al, 1998), the presence of A-FABP may be important for low-temperature function, or (2) hearts of hibernating ground squirrels maintain substantial intracellular triglyceride lipid droplets (Burlington et al, 1972) that are probably needed to meet the demand for high rates of fatty acid oxidation during arousal that could exceed the capacity for triglyceride delivery via the blood. Hence, expression of A-FABP in hibernator heart provides the organ with access to both intracellular and extracellular lipid reserves for fuel.…”

Section: ( D ) Fatty Acid Binding Proteinsmentioning

confidence: 99%

Metabolic rate depression in animals: transcriptional and translational controls

Storey¹,

Storey²

2004

Biological Reviews

593

525

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Metabolic rate depression is an important survival strategy for many animal species and a common element of hibernation, torpor, aestivation, anaerobiosis, diapause, and anhydrobiosis. Studies of the biochemical mechanisms that regulate reversible transitions to and from hypometabolic states are identifying principles of regulatory control that are conserved across phylogenetic lines and that are broadly applied to the control of multiple cell functions. One such mechanism is reversible protein phosphorylation which is now known to contribute to the regulation of fuel metabolism, to ion channel arrest, and to the suppression of protein synthesis during hypometabolism. The present review focuses on two new areas of research in hypometabolism: (1) the role of differential gene expression in supplying protein products that adjust metabolism or protect cell functions for long-term survival, and (2) the mechanisms of protein life extension in hypometabolism involving inhibitory controls of transcription, translation and protein degradation. Control of translation examines reversible phosphorylation regulation of ribosomal initiation and elongation factors, the dissociation of polysomes and storage of mRNA transcripts during hypometabolism, and control over the translation of different mRNA types by differential sequestering of mRNA into polysome versus monosome fractions. The analysis draws primarily from current research on two animal models, hibernating mammals and anoxia-tolerant molluscs, with selected examples from multiple other sources.

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Section: ( D ) Fatty Acid Binding Proteinsmentioning

confidence: 99%

Metabolic rate depression in animals: transcriptional and translational controls

Storey¹,

Storey²

2004

Biological Reviews

593

525

View full text Add to dashboard Cite

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“…The FABP purified from the liver of the catfish (Rhamdia sapo) was more closely related to the chicken liver FABP than the FABPs of elasmobranchs or mammals (Dipietro et al, 1996). Intracellular FABPs were studied in various species of Antarctic fishes (Londraville and Sidell, 1995) and two distinct types were isolated from heart tissue, one with similarity to mammalian heart-type and the other similar to mammalian adipose tissue-type (Vayada et al, 1998). A muscle FABP with a molecular mass of 14,800 Da that binds fatty acids with 1:1 stoichiometry, and whose concentration is increased by cold acclimation, was isolated from striped bass (Londraville and Sidell, 1996).…”

Section: Absorptionmentioning

confidence: 99%

Metabolism and Functions of Lipids and Fatty Acids in Teleost Fish

Tocher

2003

Reviews in Fisheries Science

2,138

1,718

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Lipids and their constituent fatty acids are, along with proteins, the major organic constituents of fish, and they play major roles as sources of metabolic energy for growth including reproduction, and movement including migration. Furthermore, the fatty acids of fish lipids are rich in ω3 long chain, highly unsaturated fatty acids (n-3 HUFA) that have particularly important roles in animal nutrition, including fish and human nutrition, reflecting their roles in critical physiological processes. Indeed, fish are the most important food source of these vital nutrients for man Thus, the long standing interest in fish lipids stems from their abundance and their uniqueness. This review attempts to summarise our present state of knowledge of various aspects of the basic biochemistry, metabolism and functions of fatty acids, and the lipids they constitute part of, in fish, seeking where possible to relate that understanding as much to fish in their natural environment as to farmed fish. In doing so, it highlights the areas that require to be investigated in greater depth and also the increasing application of molecular technologies in fish lipid metabolism which will fascilitate further advances through molecular biological and genetic techniques including genomics and proteomics.

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confidence: 99%

“…Thus, these two proteins are hypothesized to have distinct physiological functions. A-and HFABP were found in cardiac muscle cell in Antarctic Teleost fish and in different cell types of bovine mammary gland, suggesting further that the two proteins have specialized functions in the metabolism of fatty acids (20,21).The potential role of FABPs in FA trafficking has been investigated in vitro using fluorescent anthroyloxy-labeled fatty acid (AOFA) and a resonance energy transfer assay (22-25). AOFA transfer from both A-and HFABP to membranes appears to occur through a collisional process.…”

mentioning

confidence: 99%

Role of the Helical Domain in Fatty Acid Transfer from Adipocyte and Heart Fatty Acid-binding Proteins to Membranes

Liou¹,

Kahn²,

Storch³

2002

Journal of Biological Chemistry

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The adipocyte and heart fatty acid-binding proteins (Aand HFABP) are members of a lipid-binding protein family with a ␤-barrel body capped by a small helix-turn-helix motif. Both proteins are hypothesized to transport fatty acid (FA) to phospholipid membranes through a collisional process. Previously, we suggested that the helical domain is particularly important for the electrostatic interactions involved in this transfer mechanism (Herr, Despite their using qualitatively similar FA transfer mechanisms, differences in absolute transfer rates as well as regulation of transfer from AFABP versus HFABP, prompted us to consider the structural determinants that underlie these functional disparities. To determine the specific elements underlying the functional differences between AFABP and HFABP in FA transfer, two pairs of chimeric proteins were generated. The first and second pairs had the entire helical domain and the first ␣-helix exchanged between A-and HFABP, respectively. The transfer rates of anthroyloxy-labeled fatty acid from proteins to small unilamellar vesicles were compared with the wild type AFABP and HFABP. The results suggest that the ␣II-helix is important in determining the absolute FA transfer rates. Furthermore, the ␣I-helix appears to be particularly important in regulating protein sensitivity to the negative charge of membranes. The ␣I-helix of HFABP and the ␣II-helix of AFABP increased the sensitivity to anionic vesicles; the ␣I-helix of AFABP and ␣II-helix of HFABP decreased the sensitivity. The differential sensitivities to negative charge, as well as differential absolute rates of FA transfer, may help these two proteins to function uniquely in their respective cell types.FFatty acids (FA) 1 are major substrates for the synthesis of complex lipids and for energy production. Due to their limited solubility, specific carriers, known as fatty acid-binding proteins (FABP), are expressed in various tissues that use FA. Structural analyses of several FABPs have revealed markedly similar three-dimensional folds consisting of ten antiparallel ␤-strands that form a ␤-barrel, which is capped by two short ␣-helices arranged as a helix-turn-helix segment (1-4). It is believed this ␣-helical domain, along with the ␤ C-D and D-E turns, functions as a "dynamic portal" that regulates FA entry and exit from the internal ligand binding cavity (5-7).Heart FABP (HFABP) and adipocyte FABP (AFABP) are homologous proteins sharing Ͼ60% amino acid sequence identity (8). Both proteins bind one FA in the binding pocket (1, 2), although x-ray crystallographic studies show that the FA adopts an entirely different conformation in their respective binding sites (9, 10). AFABP has generally lower binding affinities for FA than HFABP (11), and it appears that HFABP shows greater affinity for saturated versus unsaturated fatty acids, whereas AFABP does not show such a preference (9). Aand HFABP also exhibit unique patterns of tissue distribution. AFABP is found in adipose tissue and monocytes/macrophages (12, 13), whereas ...

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

Cited by 37 publications

References 32 publications

Metabolic rate depression in animals: transcriptional and translational controls

Metabolic rate depression in animals: transcriptional and translational controls

Metabolism and Functions of Lipids and Fatty Acids in Teleost Fish

Role of the Helical Domain in Fatty Acid Transfer from Adipocyte and Heart Fatty Acid-binding Proteins to Membranes

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