Phosphatidylethanolamine binding protein is an abundant secretory product of haploid testicular germ cells in the rat

Saunders, Philippa T. K.; McKinnell, Chris; Millar, Michael; Gaughan, J.; Turner, Katie J.; Jégou, Bernard; Syed, Viqar; Sharpe, Richard M.

doi:10.1016/0303-7207(94)03447-2

Cited by 37 publications

(28 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…These experimental data agree with several previous studies that have described the presence of PEBP and HCNP in different biological fluids (i.e. rat haploid testicular germ cell secretions, testicular interstitial fluid (12,13,66), secretion of murine adipocytes (18), and the culture media of transfected Rat-1 fibroblast cells (14)). We have shown here that PEBP is present in bovine serum, although the protein has never been previously detected in human serum, lymph, or plasma probably because of low detection sensitivity (66).…”

Section: Discussionsupporting

confidence: 92%

“…An estimation of the concentration of PEBP in bovine serum was obtained after protein sequencing which indicated a value of 35 nM (Ϯ 5%). Because we have found the PEBP in intragranular matrix and in secretion of chromaffin cells, we further investigated if HCNP, the natural N-terminal peptide derived from PEBP that has been identified in various biological fluids (10,12), is present among the granule constituents and thus may be released upon stress stimulation.…”

Section: Analysis Of the Presence Of Pebp In Granule Membranes-mentioning

confidence: 99%

“…This protein has been found in numerous tissues of many species, including rat testis, liver, kidney, and human platelets (6,9,10), indicating its ubiquitous occurrence. Several reports have also described the presence of PEBP immunoreactivity in biological fluids, including rat haploid testicular germ cell secretions (12), testicular interstitial fluid (13), the culture media of transfected Rat-1 fibroblasts (14), and more recently in the conditioned medium from adult rat hippocampal progenitors (15). PEBP and its N-terminal-derived peptide named hippocampal cholinergic neurostimulating peptide (HCNP), corresponding to the first eleven N-terminal amino acid residues (PEBP [1][2][3][4][5][6][7][8][9][10][11] ), were also found in synaptic vesicles after subcellular fractionation and were detected by immunohistochemistry in nerve cell terminals of neurons in rat brain (10) and small intestine (16).…”

mentioning

confidence: 99%

See 2 more Smart Citations

The Hippocampal Cholinergic Neurostimulating Peptide, the N-terminal Fragment of the Secreted Phosphatidylethanolamine-binding Protein, Possesses a New Biological Activity on Cardiac Physiology

Goumon

Angelone

Schoentgen

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

Phosphatidylethanolamine-binding protein (PEBP), alternatively named Raf-1 kinase inhibitor protein, is the precursor of the hippocampal cholinergic neurostimulating peptide (HCNP) corresponding to its natural N-terminal fragment, previously described to be released by hippocampal neurons. PEBP is a soluble cytoplasmic protein, also associated with plasma and reticulum membranes of numerous cell types. In the present report, using biochemistry and cell biology techniques, we report for the first time the presence of PEBP in bovine chromaffin cell, a well described secretion model. We have examined its presence at the subcellular level and characterized this protein on both secretory granule membranes and intragranular matrix. In addition, its presence in bovine chromaffin cell and platelet exocytotic medium, as well as in serum, was reported showing that it is secreted. Like many other proteins that lack signal sequence, PEBP may be secreted through non-classic signal secretory mechanisms, which could be due to interactions with granule membrane lipids and lipid rafts. By two-dimensional liquid chromatography-tandem mass spectrometry, HCNP was detected among the intragranular matrix components. The observation that PEBP and HCNP were secreted with catecholamines into the circulation prompted us to investigate endocrine effects of this peptide on cardiovascular system. By using as bioassay an isolated and perfused frog (Rana esculenta) heart preparation, we show here that HCNP acts on the cardiac mechanical performance exerting a negative inotropism and counteracting the adrenergic stimulation of isoproterenol. All together, these data suggest that PEBP and HCNP might be considered as new endocrine factors involved in cardiac physiology.Chromaffin cells are derived from the neural crest and constitute the adrenal medulla. In the adrenal medullary chromaffin cell, secretory granules contain a complex mixture of proteins and peptides that are co-released with catecholamines into the circulation in response to splanchnic nerve stimulation (1) . Among the high molecular mass water-soluble proteins, proenkephalin-A and the chromogranins family constitute the major constituents of chromaffin granules with other neuropeptides (neuropeptide Y, vasointestinal peptide, and others). These proteins are actively processed in the intragranular matrix to peptides with various molecular weight (1-3). Recently, using highly sensitive proteomic techniques we have characterized the maturation products of proenkephalin-A (4) and established the presence of other unexpected proteins (5).Phosphatidylethanolamine-binding protein (PEBP) 1 (6, 7)/ Raf-1 kinase inhibitor protein (8) has previously been described in brain and adrenal gland (9, 10). PEBP is a 21-kDa protein initially described as a cytoplasmic protein and later found to be associated with plasma or reticulum membranes (11). This protein has been found in numerous tissues of many species, including rat testis, liver, kidney, and human platelets (6, 9, 10), indicating its ubi...

show abstract

Section: Discussionsupporting

confidence: 92%

Section: Analysis Of the Presence Of Pebp In Granule Membranes-mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

The Hippocampal Cholinergic Neurostimulating Peptide, the N-terminal Fragment of the Secreted Phosphatidylethanolamine-binding Protein, Possesses a New Biological Activity on Cardiac Physiology

Goumon

Angelone

Schoentgen

et al. 2004

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…These include the mouse antigen MEP-9, a protein found in elongated spermatids in the testis and in the principal cells of the epididymal epithelium , and B109, a protein isolated from the rat epididymis (Pryor et al 1994). However, other investigations have reported that PEBP is secreted from isolated round and elongating rat spermatids (Saunders et al 1995), is secreted into the epididymal luminal fluid and is associated with the surface of mature rodent spermatozoa (e.g. rat: Jones & Hall 1991).…”

Section: Discussionmentioning

confidence: 97%

A mouse sperm decapacitation factor receptor is phosphatidylethanolamine-binding protein 1

Gibbons¹,

Adeoya-Osiguwa²,

Fraser³

2005

Reproduction

View full text Add to dashboard Cite

Capacitation is a pivotal event for mammalian spermatozoa, involving the loss of surface proteins known as decapacitation factors (DF) and consequent acquisition of fertilizing ability. Earlier studies showed that a mouse sperm DF binds to a receptor, DF-R, whose attachment to the sperm plasma membrane appears to involve a glycosylphosphatidylinositol (GPI) anchor. In the present study, purification and subsequent sequencing of DF-R has identified this , 23 kDa protein as phosphatidylethanolamine-binding protein 1 (PEBP 1). To obtain functional evidence that supports sequence homology data, purified recombinant PEBP 1 and PEBP 2 were evaluated for biological activity. While PEBP 1 was able to remove DF activity in solution at concentrations above , 1 nmol/l, PEBP 2 was ineffective, even at 600 nmol/l; this confirmed that DF-R is PEBP 1. Anti-PEBP 1 antiserum recognized recombinant PEBP 1 and a ,23 kDa protein in both mouse and human sperm lysates. Immunolocalization studies revealed that DF-R/PEBP 1 is located on the acrosomal cap, the post-acrosomal region and the flagellum of both mouse and human spermatozoa, with epitope accessibility being capacitation state-dependent and reversible. Treatment of cells with a phospholipase able to cleave GPI anchors essentially abolished immunostaining, thus confirming the extracellular location of DF-R/PEBP 1. We suggest that DF-R/PEBP 1 plays its fundamental role in capacitation by causing alterations in the sperm plasma membrane in both head and flagellum, with functional consequences for membrane-associated proteins. Obtaining more detail about DF $ DF-R interactions could lead to useful applications in both fertility treatments and new contraceptive approaches.

show abstract

“…It was found that PEBP was an abundant secretory product of testicular germ cells [22]. Also, rodents possess an RKIP isoform, PEBP-2, whose expression appears to be testis-specific [23].…”

Section: Rkipmentioning

confidence: 99%

Modulation of the MAP kinase signaling cascade by Raf kinase inhibitory protein

Trakul

Rosner

2005

Cell Res

View full text Add to dashboard Cite

Proteins like Raf kinase inhibitory protein (RKIP) that serve as modulators of signaling pathways, either by promoting or inhibiting the formation of productive signaling complexes through protein-protein interactions, have been demonstrated to play an increasingly important role in a number of cell types and organisms. These proteins have been implicated in development as well as the progression of cancer. RKIP is a particularly interesting regulator, as it is a highly conserved, ubiquitously expressed protein that has been shown to play a role in growth and differentiation in a number of organisms and can regulate multiple signaling pathways. RKIP is also the first MAP kinase signaling modulator to be identified as playing a role in cancer metastasis, and identification of the mechanism by which it regulates Raf-1 activation provides new targets for therapeutic intervention.

show abstract

Phosphatidylethanolamine binding protein is an abundant secretory product of haploid testicular germ cells in the rat

Cited by 37 publications

References 43 publications

The Hippocampal Cholinergic Neurostimulating Peptide, the N-terminal Fragment of the Secreted Phosphatidylethanolamine-binding Protein, Possesses a New Biological Activity on Cardiac Physiology

The Hippocampal Cholinergic Neurostimulating Peptide, the N-terminal Fragment of the Secreted Phosphatidylethanolamine-binding Protein, Possesses a New Biological Activity on Cardiac Physiology

A mouse sperm decapacitation factor receptor is phosphatidylethanolamine-binding protein 1

Modulation of the MAP kinase signaling cascade by Raf kinase inhibitory protein

Contact Info

Product

Resources

About