Acyl-CoA-binding protein from cow. Binding characteristics and cellular and tissue distribution

Mikkelsen, J; Knudsen, Jens

doi:10.1042/bj2480709

Cited by 97 publications

(41 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In view of the fact that DBI is released from nerve terminals and its fragments can be found in liquor and peripheral blood [33], such peptides may represent novel neuroendocrine mediators linking the central nervous system to the immune system. Moreover, inasmuch as DBI or a protein with an identical amino acid sequence, previously named acyl-CoA binding protein, is also widely distributed in many peripheral organs such as gut and endocrine cells of the pancreatic islets [5,34], liver, kidney [35], adrenals [36], adipose tissue, heart, muscles, and mammary gland [37] of different species, and in circulating mononuclear cells [38], in red blood cells [39], and even in neoplastic cell lines [40], it cannot be excluded that high concentrations of DBI and/or of its processing products may occur locally as the result of leakage from damaged cells during tissue injury. DBI-derived peptides may thus also add to the multiple agents constituting the local microenvironment in inflamed tissues.…”

Section: Discussionmentioning

confidence: 99%

Diazepam-binding inhibitor-derived peptides induce intracellular calcium changes and modulate human neutrophil function

Cosentino

Marino

Cattaneo

et al. 2000

Journal of Leukocyte Biology

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Diazepam-binding inhibitor-derived peptides induce intracellular calcium changes and modulate human neutrophil function

Cosentino

Marino

Cattaneo

et al. 2000

Journal of Leukocyte Biology

View full text Add to dashboard Cite

“…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%

“…ACBP is a widely distributed cytosolic protein of molecular mass 10 kDa that has been found in all eukaryotes tested, from plants to humans [130], and has been identified in liver, adipose tissue, kidney, heart, brain, intestine, skeletal muscle, mammary gland [111], erythrocytes [131] duodenum, testis, adrenal gland, ovary, lung and spleen [132,133]. Recently an ACBP isoform (endozepine-like peptide) was identified in mouse testes [134].…”

Section: Role Of Acbp In Acyl-coa Metabolism and Acyl-coa-mediated Cementioning

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

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.

show abstract

“…It has also been shown that DBI and TTN exhibit high affinity for the peripheral-type benzodiazepine receptors (PBR) (Slobodyansky et al 1989, Berkovitch et al 1990, Bovolin et al 1990). In addition, DBI acts as an acyl-CoAbinding protein (Knudsen et al 1989), suggesting that it may exert a physiological role as a lipid-transport protein (Mikkelsen & Knudsen 1987). Recent studies conducted in rat astrocytes indicated that endozepines may also activate a membrane receptor positively coupled to a phospholipase C through a pertussis toxin-sensitive G protein (Patte et al 1995, Lamacz et al 1996, Gandolfo et al 1997.…”

Section: Introductionmentioning

confidence: 99%

Effect of the triakontatetraneuropeptide (TTN) on corticosteroid secretion by the frog adrenal gland

Lesouhaitier

Feuilloley²,

Vaudry³

1998

Journal of Molecular Endocrinology

View full text Add to dashboard Cite

Diazepam-binding inhibitor (DBI) was initially isolated from the rat brain as a result of its ability to compete with benzodiazepines for their receptors. Immunohistochemical studies have recently shown the presence of peripheral-type benzodiazepine receptor (PBR)-and DBI-like immunoreactivity in the frog adrenal gland. The aim of the present study was to investigate the effect of two biologically active DBI-derived peptides, the triakontatetraneuropeptide [TTN; ] and the octadecaneuropeptide [ODN; DBI(33-50)], on corticosteroid secretion by frog adrenocortical cells. Exposure of frog adrenal explants to graded concentrations of TTN (3·16 10 8 to 3·16 10 6 M) induced a dose-related increase in corticosterone and aldosterone secretion. In contrast, ODN did not modify corticosteroid output. When repeated pulses of TTN (10 6 M) were administered at 2-h intervals, the response of the adrenal explants to the second dose of TTN was markedly reduced, suggesting the existence of a desensitization phenomenon. Exposure of dispersed adrenal cells to TTN also induced a marked stimulation of corticosteroid secretion, indicating that TTN acts directly on adrenocortical cells. The central-type benzodiazepine receptor (CBR) agonist, clonazepam, did not stimulate corticosteroid secretion and the CBR antagonist, flumazenil, did not block the stimulatory action of TTN. Similarly, the PBR agonist, Ro5-4864, did not mimic the stimulatory effect of TTN and the PBR antagonist, flunitrazepam, did not affect the stimulatory action of TTN. The present study provides the first evidence for a stimulatory effect of TTN on intact adrenocortical cells. The receptor mediating the corticotropic action of TTN is not related to central-or peripheral-type benzodiazepine receptors. Our data suggest that TTN, released by chromaffin cells, may act as a paracrine factor regulating the activity of adrenocortical cells.

show abstract

Acyl-CoA-binding protein from cow. Binding characteristics and cellular and tissue distribution

Cited by 97 publications

References 18 publications

Diazepam-binding inhibitor-derived peptides induce intracellular calcium changes and modulate human neutrophil function

Diazepam-binding inhibitor-derived peptides induce intracellular calcium changes and modulate human neutrophil function

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

Effect of the triakontatetraneuropeptide (TTN) on corticosteroid secretion by the frog adrenal gland

Contact Info

Product

Resources

About