Amino acid sequence of acyl-CoA-binding protein from cow liver

Mikkelsen, J; Højrup, Peter; Nielsen, Peter; Roepstorff, Peter; Knudsen, Jens

doi:10.1042/bj2450857

Cited by 72 publications

(38 citation statements)

References 9 publications

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“…However, the identification of a novel cytoplasmic high-affinity ACBP [110][111][112][113][114] has added a new dimension to our understanding of the regulation of metabolism and transport of long-chain acyl-CoA esters and their role as second messengers in signal transduction and gene regulation.…”

Section: Intracellular Acyl-coa Binding Proteins (Acbps)mentioning

confidence: 99%

“…Sources : human-1 [171], human-2 [172], rat [112], mouse [173], bovine [113], pig [174], dog, tortoise, duck, chicken, Arabidopsis thaliana [130], frog [175], Manduca sexta [130], Drosophila melanogaster [135], yeast-1, yeast-2 [140], Brassica napus [176], cotton [177] and endozepine-like peptide (ELP) [134].…”

Section: Figure 2 Comparison Of Amino Acid Sequences Of Acbps From 16mentioning

confidence: 99%

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Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling

Færgeman¹,

Knudsen²

1997

Biochemical Journal

629

477

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The intracellular concentration of free unbound acyl-CoA esters is tightly controlled by feedback inhibition of the acyl-CoA synthetase and is buffered by specific acyl-CoA binding proteins. Excessive increases in the concentration are expected to be prevented by conversion into acylcarnitines or by hydrolysis by acyl-CoA hydrolases. Under normal physiological conditions the free cytosolic concentration of acyl-CoA esters will be in the low nanomolar range, and it is unlikely to exceed 200 nM under the most extreme conditions. The fact that acetyl-CoA carboxylase is active during fatty acid synthesis (Ki for acyl-CoA is 5 nM) indicates strongly that the free cytosolic acyl-CoA concentration is below 5 nM under these conditions. Only a limited number of the reported experiments on the effects of acyl-CoA on cellular functions and enzymes have been carried out at low physiological concentrations in the presence of the appropriate acyl-CoA-buffering binding proteins. Re-evaluation of many of the reported effects is therefore urgently required. However, the observations that the ryanodine-senstitive Ca2+-release channel is regulated by long-chain acyl-CoA esters in the presence of a molar excess of acyl-CoA binding protein and that acetyl-CoA carboxylase, the AMP kinase kinase and the Escherichia coli transcription factor FadR are affected by low nanomolar concentrations of acyl-CoA indicate that long-chain acyl-CoA esters can act as regulatory molecules in vivo. This view is further supported by the observation that fatty acids do not repress expression of acetyl-CoA carboxylase or Δ9-desaturase in yeast deficient in acyl-CoA synthetase.

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Section: Intracellular Acyl-coa Binding Proteins (Acbps)mentioning

confidence: 99%

Section: Figure 2 Comparison Of Amino Acid Sequences Of Acbps From 16mentioning

confidence: 99%

Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling

Færgeman¹,

Knudsen²

1997

Biochemical Journal

629

477

View full text Add to dashboard Cite

show abstract

“…The validity of the method is being demonstrated for a number of secondary structure amides in one globular protein, the four a-helix bundle acyl-coenzyme A binding protein, ACBP (Mikkelsen et al, 1987;. The rate constants of segmental opening and closing provide a timetable for the lifetimes of local opening events occumng in the native state protein, and they permit mapping of the events that lead to opening of both exterior and interior hydrogen bonds in the protein.…”

mentioning

confidence: 99%

Mapping the lifetimes of local opening events in a native state protein

Kragelund¹,

Heinemann²,

Knudsen³

et al. 1998

Protein Science

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The rate constants for the processes that lead to local opening and closing of the structures around hydrogen bonds in native proteins have been determined for most of the secondary structure hydrogen bonds in the four-helix protein acyl coenzyme A binding protein. In an analysis that combines these results with the energies of activation of the opening processes and the stability of the local structures, three groups of residues in the protein structure have been identified. In one group, the structures around the hydrogen bonds have frequent openings, every 600 to 1,500 s, and long lifetimes in the open state, around 1 s. In another group of local structures, the local opening is a very rare event that takes place only every 15 to 60 h. For these the lifetime in the open state is also around 1 s. The majority of local structures have lifetimes between 2,000 and 20,000 s and relatively short lifetimes of the open state in the range between 30 and 400 ms. Mapping of these groups of amides to the tertiary structure shows that the openings of the local structures are not cooperative at native conditions, and they rarely if ever lead to global unfolding. The results suggest a mechanism of hydrogen exchange by progressive local openings.

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“…Recently, the structures of the yeast (Saccharomyces cerevisiae) ACBP/DBI gene (61) and tobacco hornworm (Manduca sexta) DBI cDNA have been described (70). Protein sequences have been reported for human (43), rat (34), bovine (43,44), pig (14), and duck (74) DBI. Recently genomic sequences of the rat DBI functional gene and five processed pseudogenes have been reported (36,41).…”

mentioning

confidence: 99%

“…More recently DBI has also been purified from several peripheral organs such as pig intestine (14) and from bovine and rat liver (34,44,47). DBI has been shown to be expressed in several rat tissues (3, 9).…”

mentioning

confidence: 99%

Tissue-specific expression of the diazepam-binding inhibitor in Drosophila melanogaster: cloning, structure, and localization of the gene.

Kolmer¹,

Roos²,

Tirronen³

et al. 1994

Mol. Cell. Biol.

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The diazepam-binding inhibitor (DBI; also called acyl coenzyme A-binding protein or endozepine) is a 10-kDa polypeptide found in organisms ranging from yeasts to mammals. It has been shown that DBI and its processing products are involved in various specific biological processes such as GABAA/benzodiazepine receptor modulation, acyl coenzyme A metabolism, steroidogenesis, and insulin secretion. We have cloned and sequenced the Drosophila melanogaster gene and cDNA encoding DBI. The Drosophila DBI gene encodes a protein of 86 amino acids that shows 51 to 56% identity with previously known DBI proteins. The gene is composed of one noncoding 5' and two coding exons and is localized on the chromosomal map at position 65E. Several transcription initiation sites were detected by RNase protection and primer extension experiments.Computer analysis of the promoter region revealed features typical of housekeeping genes, such as the lack of TATA and CCAAT elements. However, in its low GC content and lack of a CpG island, the region resembles promoters of tissue-specific genes. Northern (RNA) analysis revealed that the expression of the DBI gene occurred from the larval stage onwards throughout the adult stage. In adult flies, DBI mRNA and immunoreactivity were detected in the cardia, part of the Malpighian tubules, the fat body, and gametes of both sexes. Developmentally regulated expression, disappearing during metamorphosis, was detected in the larval and pupal brains. No expression was detected in the adult nervous system. On the basis of the expression of DBI in some but not all tissues with high energy consumption, we propose that in D. melanogaster, DBI is involved in energy metabolism in a manner that depends on the substrate used for energy production.The diazepam-binding inhibitor (DBI) is a 10-kDa polypeptide that was first purified from rat brain on the basis of its ability to displace diazepam from the -y-aminobutyric acid receptor type A (GABAA)/benzodiazepine receptor (24). More recently DBI has also been purified from several peripheral organs such as pig intestine (14) and from bovine and rat liver (34,44,47). DBI has been shown to be expressed in several rat tissues (3, 9). The highest expression has been observed in the adrenal gland, liver, and somatic tissue of the testes, while the lowest levels have been detected in spleen, lung, and muscle (34,45,68). Nevertheless, DBI expression is restricted to certain cell types. In the rat brain, DBI is localized in selected neuronal populations, ependymal and glial cells (2, 3). DBIlike peptides have also been found in the central nervous systems of trout (Salmo gairdneri) (39) and frogs (Rana ridibunda) (40). In the adrenal gland, DBI is expressed in cortical cells, whereas chromaffin cells of the medulla are immunonegative (9). DBI and its metabolites octadecaneuropeptide (DBI33_50) and triakontatetraneuropeptide (DBI17-50) are involved in the regulation of multiple biological processes. In rats, intracerebroventricular injection of DBI or one of its metabolit...

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Amino acid sequence of acyl-CoA-binding protein from cow liver

Cited by 72 publications

References 9 publications

Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling

Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling

Mapping the lifetimes of local opening events in a native state protein

Tissue-specific expression of the diazepam-binding inhibitor in Drosophila melanogaster: cloning, structure, and localization of the gene.

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