A novel endozepine-like peptide (ELP) is exclusively expressed in male germ cells

Pusch, Wolfgang; Balvers, Marga; Hunt, Nicholas H.; Ivell, Richard

doi:10.1016/0303-7207(96)03874-9

Cited by 25 publications

(2 citation statements)

References 18 publications

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“…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]. The highest concentration of ACBP is found in liver, where it is evenly distributed in all hepatocytes [133].…”

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

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

625

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

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

625

477

View full text Add to dashboard Cite

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Proteomic markers of low and high fertility bovine spermatozoa separated by Percoll gradient

D’Amours

Calvo

Bourassa

et al. 2019

Molecular Reproduction Devel

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In the context of artificial insemination, male fertility is defined as the ability to produce functional spermatozoa able to withstand cryopreservation. We hypothesized that interindividual variations in fertility depend on the proportion of the fully functional sperm population contained in the insemination dose. The objective of this study was to identify protein markers of the fully functional sperm subpopulation. Insemination doses from four high‐fertility (HF) and four low‐fertility (LF) bulls with comparable post‐thaw quality parameters were selected for proteomic analysis using iTRAQ technology. Thawed semen was centrifuged through a Percoll gradient to segregate the motile (high density [HD]) from the immotile (low density [LD]) sperm populations. Sperm proteins were extracted with sodium deoxycholate and four groups were compared: LD and HD spermatozoa from LF and HF bulls. A total of 498 unique proteins were identified and quantified. Comparison of HD spermatozoa from HF and LF bulls revealed that five proteins were significantly more abundant in the HF group (AK8, TPI1, TSPAN8, OAT, and DBIL5) whereas five proteins were more abundant in the LF group (RGS22, ATP5J, CLU, LOC616319, and CCT5). Comparison of LD spermatozoa from HF and LF bulls revealed that four proteins were significantly more abundant in the HF group (IL4I1, CYLC2, OAT, and ARMC3) whereas 15 proteins were significantly more abundant in the LF group (HADHA, HSP90AA1, DNASE1L3, SLC25A20, GPX5, TCP1, HIP1, CLU, G5E622, LOC616319, HSPA2, NUP155, DPY19L2, SPERT, and SERPINE2). DBIL5, TSPAN8, and TPI1 showed potential as putative markers of the fully functional sperm subpopulation.

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Structure and Function of Normal and Transformed Murine Acyl-CoA Binding Proteins

Gossett

Edmondson

Jolly

et al. 1998

Archives of Biochemistry and Biophysics

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A novel endozepine-like peptide (ELP) is exclusively expressed in male germ cells

Cited by 25 publications

References 18 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

Proteomic markers of low and high fertility bovine spermatozoa separated by Percoll gradient

Structure and Function of Normal and Transformed Murine Acyl-CoA Binding Proteins

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