Localization of vitellogenin-related protein in the developing oocytes of winter flounder (Pleuronectes americanus) by protein A-gold immunocytochemistry

1993 ◽  
Vol 271 (3) ◽  
pp. 567-570 ◽  
Author(s):  
James J. Nagler ◽  
Faye Murrin ◽  
David R. Idler
Keyword(s):  
Protein A ◽  
Winter Flounder ◽  
Pleuronectes Americanus ◽  
Related Protein

scholarly journals Modulation of Ins(2,4,5)P3-stimulated Ca2+ mobilization by Ins(1,3,4,5)P4: enhancement by activated G-proteins, and evidence for the involvement of a GAP1 protein, a putative Ins(1,3,4,5)P4 receptor

1998 ◽  
Vol 331 (3) ◽  
pp. 947-952 ◽  
Author(s):  
Jefferson W. LOOMIS-HUSSELBEE ◽  
Christopher D. WALKER ◽  
Joanna R. BOTTOMLEY ◽  
Peter J. CULLEN ◽  
Robin F. IRVINE ◽  
...  
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Protein A ◽  
Related Protein ◽  
L1210 Cells ◽  
Putative Receptor ◽  
Specific Enhancement ◽  
Insp3 Receptor

We have previously shown that addition of Ins(1,3,4,5)P4 to permeabilized L1210 cells increases the amount of Ca2+ mobilized by a submaximal concentration of Ins(2,4,5)P3, and we suggested that, in doing this, Ins(1,3,4,5)P4 is not working via an InsP3 receptor but indirectly via an InsP4 receptor [Loomis-Husselbee, Cullen, Dreikhausen, Irvine and Dawson (1996) Biochem. J. 314, 811–816]. Here we have investigated whether this effect might be mediated by GAP1IP4BP, recently identified as a putative receptor for Ins(1,3,4,5)P4. GAP1IP4BP is a protein that interacts with one or more monomeric G-proteins, so we sought evidence for involvement of monomeric G-proteins in the effects of Ins(1,3,4,5)P4 in permeabilized L1210 cells. Guanosine 5´-[γ-thio]triphosphate (GTP[S]) enhanced the effect of Ins(1,3,4,5)P4 on Ins(2,4,5)P3-stimulated Ca2+ mobilization, but had no effect on the action of Ins(2,4,5)P3 alone. A specific enhancement of only the action of Ins(1,3,4,5)P4 was also seen with GTP[S]-loaded R-Ras or Rap1a (two G-proteins known to interact with GAP1IP4BP), whereas H-Ras was inactive at similar concentrations. Guanosine 5´-[β-thio]diphosphate (GDP[S]) did not alter the action of either Ins(2,4,5)P3 or Ins(1,3,4,5)P4. Finally, the addition of exogenous GAP1IP4BP, purified from platelets, markedly enhanced the effect of Ins(1,3,4,5)P4, and again, the amount of Ca2+ mobilized by Ins(2,4,5)P3 alone was unaltered. We conclude that the increase in Ins(2,4,5)P3-stimulated Ca2+ mobilization by Ins(1,3,4,5)P4 may be mediated by GAP1IP4BP or a closely related protein (such as GAP1m), and if so, the action of the GAP1 is not solely to regulate GTP loading of a G-protein, but rather it acts with a G-protein to cause its effect.

Effects of prolonged exercise on agouti-related protein: a pilot study

Endocrine ◽  
2012 ◽  
Vol 42 (2) ◽  
pp. 436-441
Author(s):  
Robert R. Kraemer ◽  
V. Daniel Castracane ◽  
Michelle Francois ◽  
Abbass Ghanbari-Niaki ◽  
Bovorn Sirikul ◽  
...  
Keyword(s):  
Pilot Study ◽  
Prolonged Exercise ◽  
Protein A ◽  
Related Protein ◽  
Agouti Related Protein

scholarly journals Signal Transduction in Human Hematopoietic Cells by Vascular Endothelial Growth Factor Related Protein, a Novel Ligand for the FLT4 Receptor

Blood ◽  
1997 ◽  
Vol 90 (9) ◽  
pp. 3507-3515 ◽  
Author(s):  
Jian-Feng Wang ◽  
Ramesh K. Ganju ◽  
Zhong-Ying Liu ◽  
Hava Avraham ◽  
Shalom Avraham ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Protein A ◽  
Hematopoietic Cells ◽  
Adaptor Protein ◽  
Vascular Endothelial ◽  
Related Protein ◽  
Jnk Pathway ◽  
Endothelial Growth Factor

Abstract We have recently identified a novel ligand of the vascular endothelial growth factor (VEGF) family termed VEGF-related protein (VRP), which specifically binds to the FLT4 receptor. To characterize the signaling events after VRP engagement of its cognate receptor in hematopoietic cells, a population of human erythroleukemia (HEL) cells, termed HEL-JW, expressing high levels of FLT4 receptor was isolated. Stimulation of HEL-JW cells with VRP alone and in combination with the c-kit ligand/stem cell factor increased cell growth. VRP induced tyrosine phosphorylation of various proteins, including the FLT4 receptor. Further characterization of these tyrosine phosphorylated molecules revealed that Shc, Grb2, and SOS form a complex with the activated FLT4 receptor. HEL-JW cells also expressed RAFTK, a recently identified member of the focal adhesion kinase family. RAFTK was phosphorylated and activated upon VRP treatment, and there was an enhanced association of this kinase with the adaptor protein Grb2. Furthermore, the c-Jun NH2-terminal kinase (JNK), involved in growth activation and shown to mediate RAFTK signaling in other cell types, was activated by VRP stimulation. We also observed that VRP treatment of HEL-JW cells resulted in the phosphorylation of the cytoskeletal protein paxillin. This treatment resulted in an increased association of paxillin with RAFTK, which was mediated by the C-terminal region of RAFTK. These studies indicate that VRP stimulation induced the formation of a signaling complex at its activated receptor as well as activation of RAFTK. VRP-mediated activation of RAFTK may facilitate signal transduction to the cytoskeleton and downstream to the JNK pathway in FLT4-expressing blood cells.

Induced Cytochrome P4501A in Winter Flounder, Pleuronectes americanus, from Offshore and Coastal Sites

1994 ◽  
Vol 51 (4) ◽  
pp. 933-941 ◽  
Author(s):  
Emily Monosson ◽  
John J. Stegeman
Keyword(s):  
East Coast ◽  
Dry Weight ◽  
Winter Flounder ◽  
Boston Harbor ◽  
Pleuronectes Americanus ◽  
Georges Bank ◽  
Urban Centers ◽  
Cytochrome P4501a ◽  
Passamaquoddy Bay ◽  
Specific Activities

Cytochrome P4501A (CYP1A), Aroclor 1254 (A1254), and 3,3′,4,4′-tetrachlorobiphenyl (TCB) were measured in liver of winter flounder, Pleuronectes americanus, from Boston Harbor, Mass., Hempsted Harbor, N.Y., Niantic, Conn., and an offshore site, Georges Bank. We also measured CYP1A content and activity in flounder from Passamaquoddy Bay, N.B. Concentrations of A1254 and TCB were the least in fish from Georges Bank (0.46 and 0.002 μg∙g dry weight−1, respectively); concentrations in fish from Boston, Niantic, and Hempsted ranged from 7.6 to 11.3 μg∙g−1 and from 0.013 to 0.024 μg∙g−1. Immunodetected microsomal CYP1A contents (expressed as scup P450E equivalents) were 0.17 and 0.19 nmol∙mg−1 in fish from Georges Bank and Passamaquoddy and 0.25–0.41 nmol∙mg−1 in fish from Boston, Niantic, and Hempsted. Ethoxyresorufin-O-deethylase specific activities likewise were greater in fish from Boston, Niantic, and Hempsted (1.7–2.4 nmol∙min−1∙mg−1) than in fish from Georges Bank or Passamaquoddy (0.83 and 0.61 nmol∙min−1∙mg−1). CYP1A content and activity were correlated with hepatic concentrations of A1254 and TCB. These data, together with data reported in previous studies, indicate that strong induction of CYP1A protein occurs in winter flounder populations along most of the industrialized east coast and that induction of CYP1A is common, but less strong, at sites distant from the urban centers of the Northeast.

Chemical contaminants and hepatic lesions in winter flounder (Pleuronectes americanus) from the northeast coast of the United States

1993 ◽  
Vol 27 (13) ◽  
pp. 2759-2771 ◽  
Author(s):  
Lyndal L. Johnson ◽  
Carla M. Stehr ◽  
O. Paul Olson ◽  
Mark S. Myers ◽  
Susan M. Pierce ◽  
...  
Keyword(s):  
United States ◽  
The United States ◽  
Winter Flounder ◽  
Pleuronectes Americanus ◽  
Chemical Contaminants ◽  
Hepatic Lesions ◽  
Northeast Coast
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