A novel 45 kDa secretory protein from rat olfactory epithelium: primary structure and localisation

Merkulova, Maria; Andreeva, Svetlana; Shuvaeva, T. M.; Novoselov, Sergey V.; Peshenko, Igor V.; Bystrova, M. F.; Новоселов, В. И.; Фесенко, Е. Е.; Липкин, В. М.

doi:10.1016/s0014-5793(99)00470-6

Cited by 30 publications

(24 citation statements)

References 18 publications

(23 reference statements)

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“…The strong overall sequence homology of hTAP with the 45-kDa secretory protein from rat (AJ132352), which also contains this extension, indicates that both proteins are closely related. The 45-kDa rat secretory protein is present in cells of the olfactory epithelium, the apical region of the trachea, the surface layer of the ciliated bronchial epithelium, and the epidermis (35). Opposite to this, hTAP mRNA is ubiquitous and strongly expressed exclusively in adult tissues.…”

Section: Discussionmentioning

confidence: 99%

A Novel Human Tocopherol-associated Protein

Zimmer

Stocker

Sarbolouki

et al. 2000

Journal of Biological Chemistry

160

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Section: Discussionmentioning

confidence: 99%

A Novel Human Tocopherol-associated Protein

Zimmer

Stocker

Sarbolouki

et al. 2000

Journal of Biological Chemistry

160

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“…This region has 28% identity with cellular retinaldehyde-binding protein and 24% identity with Sec14p, a yeast protein with phosphatidylinositol (PtdIns) 3 transfer activity. A similar Sec14p homology domain is also found in two protein tyrosine phosphatases from Xenopus laevis, PTPX1 and PTPX10 (6), and numerous other proteins (7,8), including many regulators of Rho, Rac, and Ras proteins (9).…”

mentioning

confidence: 85%

Homotypic Secretory Vesicle Fusion Induced by the Protein Tyrosine Phosphatase MEG2 Depends on Polyphosphoinositides in T Cells

Huynh

Wang²,

et al. 2003

The Journal of Immunology

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Sec14p homology domains are found in a large number of proteins from plants, yeast, invertebrates, and higher eukaryotes. We report that the N-terminal Sec14p homology domain of the human protein tyrosine phosphatase PTP-MEG2 binds phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) in vitro and colocalizes with this lipid on secretory vesicle membranes in intact cells. Point mutations that prevented PtdIns(3,4,5)P3 binding abrogated the capacity of PTP-MEG2 to induce homotypic secretory vesicle fusion in cells. Inhibition of cellular PtdIns(3,4,5)P3 synthesis also rapidly reversed the effect of PTP-MEG2 on secretory vesicles. Finally, we show that several different phosphoinositide kinases colocalize with PTP-MEG2, thus allowing for local synthesis of PtdIns(3,4,5)P3 in secretory vesicle membranes. We suggest that PTP-MEG2 through its Sec14p homology domain couples inositide phosphorylation to tyrosine dephosphorylation and the regulation of intracellular traffic of the secretory pathway in T cells.

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“…The relatively large binding pocket of TAPs can accommodate several different ligands that within cells may form a group of lipids competing for the same binding site. Several hydrophobic ligands are bound by the TAP proteins in vitro, such as a-, b-, g-, d-tocopherols and tocotrienols, a-tocopheryl quinone, phosphatidylcholine, phosphatidylserine, and squalene, as well as aTS, phosphatidylinositol and phosphatidylinositol-3,4,5-phosphate [47][48][49][50][56][57][58][59][60][61][62]. Using an isoelectric point mobility shift assay [59], aTP was able to compete in vitro with phosphatidylinositol for binding to recombinant human TAP1 (hTAP1) in a similar manner as aT, suggesting that aT and aTP may influence cellular events via competition for the same binding site.…”

Section: Lipid Transport Proteins With Possible Role In At and Atp Fumentioning

confidence: 99%

α‐Tocopheryl phosphate – An active lipid mediator?

Zingg

Meydani

Azzi

2010

Molecular Nutrition Food Res

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The vitamin E (alpha-tocopherol, alphaT) derivative, alpha-tocopheryl phosphate (alphaTP), is detectable in small amounts in plasma, tissues, and cultured cells. Studies done in vitro and in vivo suggest that alphaT can become phosphorylated and alphaTP dephosphorylated, suggesting the existence of enzyme(s) with alphaT kinase or alphaTP phosphatase activity, respectively. As a supplement in animal studies, alphaTP can reach plasma concentrations similar to alphaT and only a part is dephosphorylated; thus, alphaTP may act both as pro-vitamin E, but also as phosphorylated form of vitamin E with possibly novel regulatory activities. Many effects of alphaTP have been described: in the test tube alphaTP modulates the activity of several enzymes; in cell culture alphaTP affects proliferation, apoptosis, signal transduction, and gene expression; in animal studies alphaTP prevents atherosclerosis, ischemia/reperfusion injury, and induces hippocampal long-term potentiation. At the molecular level, alphaTP may act as a cofactor for enzymes, as an active lipid mediator similar to other phosphorylated lipids, or indirectly by altering membrane characteristics such as lipid rafts, fluidity, and curvature. In this review, the molecular and cellular activities of alphaTP are examined and the possible functions of alphaTP as a natural compound, cofactor and active lipid mediator involved in signal transduction and gene expression discussed.

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A novel 45 kDa secretory protein from rat olfactory epithelium: primary structure and localisation

Cited by 30 publications

References 18 publications

A Novel Human Tocopherol-associated Protein

A Novel Human Tocopherol-associated Protein

Homotypic Secretory Vesicle Fusion Induced by the Protein Tyrosine Phosphatase MEG2 Depends on Polyphosphoinositides in T Cells

α‐Tocopheryl phosphate – An active lipid mediator?

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