Results 11 to 20 of about 15,232 (136)

Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase of rabbit reticulocytes: homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2 alpha kinase. [PDF]

Proceedings of the National Academy of Sciences, 1991
We have cloned the cDNA of the heme-regulated eIF-2 alpha kinase (HRI) of rabbit reticulocytes. In vitro translation of mRNA transcribed from the HRI cDNA yields a 90-kDa polypeptide that exhibits eIF-2 alpha kinase activity and is recognized by a monoclonal antibody directed against authentic HRI.
J J, Chen, M S, Throop, L, Gehrke, I, Kuo, J K, Pal, M, Brodsky, I M, London   +6 more
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Effects of Dietary Crude Protein Levels and Cysteamine Supplementation on Protein Synthetic and Degradative Signaling in Skeletal Muscle of Finishing Pigs. [PDF]

PLoS ONE, 2015
Dietary protein levels and cysteamine (CS) supplementation can affect growth performance and protein metabolism of pigs. However, the influence of dietary protein intake on the growth response of CS-treated pigs is unclear, and the mechanisms involved in
Ping Zhou, Lin Zhang, Jiaolong Li, Yiqiu Luo, Bolin Zhang, Shen Xing, Yuping Zhu, Hui Sun, Feng Gao, Guanghong Zhou   +9 more
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Histidyl-tRNA Synthetase-related Sequences in GCN2 Protein Kinase Regulate in Vitro Phosphorylation of eIF-2 [PDF]

Journal of Biological Chemistry, 1996
In yeast, starvation for amino acids stimulates GCN2 phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2). Phosphorylation of eIF-2alpha induces the translational expression of GCN4, a transcriptional activator of the general amino acid control pathway.
S, Zhu, A Y, Sobolev, R C, Wek
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Erythroid Expression of the Heme-Regulated eIF-2α Kinase [PDF]

Molecular and Cellular Biology, 1994
The role of heme-regulated eIF-2 alpha kinase (HRI) in the regulation of protein synthesis in rabbit reticulocytes is well documented. Inhibitors of protein synthesis with properties similar to those of HRI have been described in some nonerythroid cell types, but it has not yet been determined whether these eIF-2 alpha kinase activities are mediated by
J S, Crosby, K, Lee, I M, London, J J, Chen   +3 more
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Posttranscriptional Suppression of Lipopolysaccharide-Stimulated Inflammatory Responses by Macrophages in Middle-Aged Mice: A Possible Role for Eukaryotic Initiation Factor 2α

International Journal of Inflammation, 2014
The intensities of macrophage inflammatory responses to bacterial components gradually decrease with age. Given that a reduced rate of protein synthesis is a common age-related biochemical change, which is partially mediated by increased phosphorylation ...
Ken Shirato, Kazuhiko Imaizumi
doaj   +1 more source

Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 α-subunit

Journal of Biological Chemistry, 1989
We have reported previously that a 67-kDa polypeptide (p67) present in reticulocyte lysates protects the alpha-subunit of reticulocyte eukaryotic peptide chain initiation factor 2 (eIF-2) from phosphorylation by an eIF-2 kinase, heme-regulated protein synthesis inhibitor (Datta, B., Chakrabarti, D., Roy, A.L., and Gupta, N. K. (1988) Proc. Natl.
B, Datta, M K, Ray, D, Chakrabarti, D E, Wylie, N K, Gupta   +4 more
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Differential regulation of protein synthesis in skeletal muscle and liver of neonatal pigs by leucine through an mTORC1-dependent pathway

Journal of Animal Science and Biotechnology, 2012
Neonatal growth is characterized by a high protein synthesis rate that is largely due to an enhanced sensitivity to the postprandial rise in insulin and amino acids, especially leucine. The mechanism of leucine's action in vivo is not well understood. In
Suryawan Agus, Nguyen Hanh V, Almonaci Rosemarie D, Davis Teresa A   +3 more
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Disulfide Bond Formation in the Regulation of eIF-2 α Kinase by Heme

Journal of Biological Chemistry, 1989
Abstract The inhibition of the autophosphorylation of the heme-regulated eukaryotic initiation factor (eIF)-2 alpha kinase (HRI) by hemin is very similar to that produced by thiol oxidation by diamide. The results obtained from the analysis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis of unphosphorylated and phosphorylated HRI under ...
J J Chen, J M Yang, R Petryshyn, N Kosower, I M London   +4 more
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Induction of Apoptosis Coupled to Endoplasmic Reticulum Stress through Regulation of CHOP and JNK in Bone Marrow Mesenchymal Stem Cells from Patients with Systemic Lupus Erythematosus

Journal of Immunology Research, 2015
Previous studies indicated that bone marrow mesenchymal stem cells (BM-MSCs) from patients with systemic lupus erythematosus (SLE) exhibited the phenomenon of apoptosis.
Genkai Guo, Yan Meng, Wei Tan, Yunfei Xia, Chun Cheng, Xiaolan Chen, Zhifeng Gu   +6 more
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Phospholipid‐sensitive Ca²⁺‐dependent protein kinase phosphorylates the β subunit of eukaryotic initiation factor 2 (eIF‐2) [PDF]

FEBS Letters, 1983
The ability of homogeneous phospholipid‐sensitive Ca2+‐dependent protein kinase (PL‐Ca‐PK) from pig spleen to phosphorylate eukaryotic initiation factor 2 (eIF‐2) was examined. PL‐Ca‐PK phosphorylated the β‐subunit of eIF‐2, whereas myosin light chain kinase (MLCK) and cyclic AMP‐ and cyclic GMP‐dependent protein kinases (cA‐PK and cG‐PK) did not.
Schatzman, Randall C., Grifo, Jamie A., Merrick, William C., Kuo, J.F.   +3 more
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