Expression of phosphatidylethanolamine-binding protein in the male reproductive tract: Immunolocalisation and expression in prepubertal and adult rat testes and epididymides

Frayne, Jan; McMillen, A; Love, Seth; Hall, Len

doi:10.1002/(sici)1098-2795(199804)49:4<454::aid-mrd13>3.0.co;2-u

Cited by 38 publications

(33 citation statements)

References 24 publications

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“…Rat RKIP expression has been found in oligodendrocytes and Schwann cells of the neuronal tissue; spermatids, Leydig cells and epididymal epithelium of the testis; steroidogenic cells of the adrenal gland zona fasciculata; proximal kidney tubule epithelium; enterocytes, goblet cells and plasma cells of the small intestine; plasma cells of the lymph node; plasma cells and megakaryocytes of the spleen; heart; liver; and epididymis [48]. Some expression has also been found in bronchioles of the lung, mesenteric lymph node, oviduct, ovary, lactating mammary glands, uterus and thyroid.…”

Section: Rkip Biologymentioning

confidence: 99%

“…Although RKIP is expressed in multiple tissues of the rat, higher expression levels can be found in the testis, brain oligodendrocytes, Schwann cells, Purkinje cells of the cerebellum, and within cortical and hippocampal layers of the brain [48,[53][54][55][56][57]. In rat medial septal nuclei, RKIP was found to enhance in vitro acetylcholine synthesis by up-regulating choline acetyltransferase and possibly stimulating cholinergic neuronal pathways [57][58][59][60].…”

Section: Rkip Biologymentioning

confidence: 99%

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Metastasis suppressor genes: a role for raf kinase inhibitor protein (RKIP)

Keller

2004

Anti-Cancer Drugs

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The metastatic cascade is a complicated process that involves many steps from gain of the metastatic phenotype in the primary tumor cells through establishment of macroscopic tumor at the distant target organ. A group of genes, termed metastasis suppressor genes (MSG), encode for proteins that inhibit various steps of the metastatic cascade. Accordingly, loss of MSG promotes the metastatic phenotype. Although several MSG have been identified, the mechanisms through which they enhance metastasis are not clearly defined. Gene array analysis of a low metastatic LNCaP prostate cancer cell line compared to its highly metastatic derivative C4-2B prostate cancer cell line revealed decreased expression of raf kinase inhibitor protein (RKIP) in the C4-2B cell line. RKIP blocks the activation of several signaling pathways including MEK, G-proteins and NFkappaB. Immunohistochemical analysis of prostate cancer primary tumors and metastases revealed that RKIP protein expression was decreased in metastases. Restoration of RKIP expression in the C4-2B cell line diminished metastasis in a murine model. These results demonstrate that RKIP is a MSG. Loss of RKIP enhanced both angiogenesis and vascular invasion, and protected against apoptosis. These findings suggest that targeting the RKIP pathway may diminish the metastatic cascade. However, challenges exist as to the best method to target RKIP expression. Restoration of RKIP expression in all cancer cells in vivo is challenging. A plausible strategy is to use small molecules that target proteins in signaling pathways that are dysregulated due to loss of RKIP.

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Section: Rkip Biologymentioning

confidence: 99%

Section: Rkip Biologymentioning

confidence: 99%

Metastasis suppressor genes: a role for raf kinase inhibitor protein (RKIP)

Keller

2004

Anti-Cancer Drugs

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“…Pebp family members have been implicated in membrane biogenesis [10,11], membrane fluidity and the formation of functional domains [6,12], the stimulation of acetylcholine secretion during neuronal development [12,13], and serine protease inhibition in neuronal tissue [14]. Further, pebp-1 (also called raf kinase inhibitory protein [RKIP]) has been identified using a yeast two-hybrid screen as a suppressor of raf-1 kinase activity and mitogen-activated protein (MAP) kinase signaling in fibroblasts through its ability to sequester inactive raf-1 and MEK1 [15,16].…”

Section: Introductionmentioning

confidence: 99%

Identification of a Novel Testis-Specific Member of the Phosphatidylethanolamine Binding Protein Family, pebp-21

Hickox¹,

Gibbs²,

Morrison³

et al. 2002

Biology of Reproduction

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The phosphatidylethanolamine binding proteins (pebps) are an evolutionarily conserved family of proteins recently implicated in mitogen-activated protein (MAP) kinase pathway regulation, where they are called raf kinase inhibitory proteins. Here, we describe the cloning, cellular localization, and partial characterization of a new member, pebp-2, with potential roles in male fertility. Expression data show that pebp-2 is a testis-specific 21-kDa protein found within late meiotic and haploid germ cells in a stage-specific pattern that is temporally distinct from that of pebp-1. Sequence analyses suggest that pebp-2 forms a distinct subset of the pebp family within mammals. Database analyses revealed the existence of a third subset. Analysis suggests that the specificity/regulation of the distinct pebps subsets is likely to be determined by the amino terminal 40 amino acids or the 3' untranslated region, where the majority of sequence differences occur. Protein homology modeling suggests that pebp-2 protein is, however, topologically similar to other pebps and composed of Greek key fold motifs, a dominant beta-sheet formed from five anti-parallel beta strands forming a shallow groove associated with a putative phosphatidylethanolamine binding site. The pebp-2 gene is intronless and data suggest that it is a retrogene derived from pebp-1. Further, pebp-2 colocalizes with members of the MAP kinase pathway in late spermatocytes and spermatids and on the midpiece of epididymal sperm. These data raise the possibility that pebp-2 is a novel participant in the MAP kinase signaling pathway, with a role in spermatogenesis or posttesticular sperm maturation.

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“…In neuronal tissue, PEBP has been localised to oligodendrocytes (Moore et al 1996;Roussel et al 1988) and Schwann cells (Moore et al 1996) and, in the testis, to elongating spermatids (Perry et al 1994;Frayne et al 1998), leading the authors to postulate a possible role for this protein in membrane biogenesis or lipid transfer. However, the distribution of PEBP throughout the cytoplasm, together with its localisation to the plasma membrane, has led Schoentgen and co-workers (1993) to suggest a possible role in signalling mechanisms between the membrane and cytoplasm of cells.…”

Section: Introductionmentioning

confidence: 99%

Localisation of phosphatidylethanolamine-binding protein in the brain and other tissues of the rat

Frayne¹,

Ingram²,

Love³

et al. 1999

Cell and Tissue Research

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Phosphatidylethanolamine-binding protein (PEBP) is a highly-conserved 21- to 23-kDa basic protein that shows preferential affinity in vitro for phosphatidylethanolamine. Previous studies have focussed on PEBP in the brain and male reproductive tract where it has been proposed to play a role in membrane biogenesis. In the present more comprehensive study, rat PEBP transcripts and protein have been found to be expressed in all tissues examined, although the levels vary considerably between tissues. However, at the cellular level, PEBP expression is enigmatic, being restricted to a diverse range of highly specialised neuronal and non-neuronal cell types. The nature of this diversity, ranging from oligodendrocytes to plasma cells, whilst not precluding a role for PEBP in membrane biogenesis in some cell types, would imply that this is not the major function in others.

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Expression of phosphatidylethanolamine-binding protein in the male reproductive tract: Immunolocalisation and expression in prepubertal and adult rat testes and epididymides

Cited by 38 publications

References 24 publications

Metastasis suppressor genes: a role for raf kinase inhibitor protein (RKIP)

Metastasis suppressor genes: a role for raf kinase inhibitor protein (RKIP)

Identification of a Novel Testis-Specific Member of the Phosphatidylethanolamine Binding Protein Family, pebp-21

Localisation of phosphatidylethanolamine-binding protein in the brain and other tissues of the rat

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