Factors involved in initiation of haemoglobin synthesis can be phosphorylated in vitro

Traugh, Jolinda A.; Tahara, Stanley M.; Sharp, Sandra B.; Safer, Brian; Merrick, William C.

doi:10.1038/263163a0

Cited by 69 publications

(20 citation statements)

References 19 publications

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“…Both eIF-2a and eIF-2, subunits were phosphorylated in this experiment. The two subunits are phosphorylated by different kinases, and P-subunit phosphorylation is not known to affect eIF-2 activity (25,27). As reported previously (21,23), P1/eIF-2a kinase activity was substantially elevated by 20 h after infection of 293 cells with d1331.…”

Section: Resultssupporting

confidence: 53%

An adenovirus mutant unable to express VAI RNA displays different growth responses and sensitivity to interferon in various host cell lines.

Kitajewski¹,

Schneider²,

Safer³

et al. 1986

Mol. Cell. Biol.

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The VAI RNA of adenovirus is a small, RNA polymerase III-transcribed species required for the efficient translation of host cell and viral mRNAs late after infection. VAI RNA prevented activation of the interferon-induced P1/eIF-2 alpha kinase. In its absence the kinase was activated, eIF-2 alpha was phosphorylated, and translational initiation was inhibited. H5dl331 (dl331), a mutant which cannot express VAI RNA, grew poorly in 293 cells but generated wild-type yields in KB cells. The growth phenotype of the mutant appeared to correlate with the kinetics of kinase induction and activation. Active kinase appeared more rapidly in cell extracts prepared from infected 293 cells, in which dl331 grew poorly, than in extracts of KB cells, in which the mutant grew well. However, when kinase was induced in KB cells by interferon treatment and then activated subsequent to dl331 infection, viral protein synthesis was less severely inhibited than in interferon-treated 293 cells. Thus, activated kinase per se is insufficient to severely inhibit dl331 protein synthesis in KB cells.

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Section: Resultssupporting

confidence: 53%

An adenovirus mutant unable to express VAI RNA displays different growth responses and sensitivity to interferon in various host cell lines.

Kitajewski¹,

Schneider²,

Safer³

et al. 1986

Mol. Cell. Biol.

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“…A decision between these alternative cannot be made presently since the molecular basis for the control of protein synthesis by the phosphorylationdephosphorylation cycle of S6 is unknown [24] . Therefore a causal relationship between the inhibition of protein synthesis [4-81, the disaggregation of polyribosomes, and the appearance of cytoplasmic aggregates probably formed by altered ribosomes [9] observed after GalN treatment and the phosphorylation of S6 cannot be established presently.…”

Section: Discussionmentioning

confidence: 99%

The phosphorylation of liver ribosomal protein S6 during the development of acute hepatic cell injury induced by D‐galactosamine

Gressner

Greiling

1977

FEBS Letters

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“…3, we were CKII is mediated has not yet been identified, we must that there are at least two different sites of action: one in the cytoplasm where it may exert control over the initiation and elongation of protein synthesis [7,8,37, 381 and one in the thesis [13,141. Two of four nucleolar proteins which become phosphorylated by CKII (i,e.…”

Section: Discussionmentioning

confidence: 99%

Casein kinase II is elevated in solid human tumours and rapidly proliferating non‐neoplastic tissue

Münstermann

Fritz

Seitz

et al. 1990

European Journal of Biochemistry

197

106

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Protein kinase CKII (i.e. casein kinase 11, CKII, NII) is expressed at a higher level in rapidly proliferating tissues and in solid human tumours (e. g. colorectal carcinomas) when compared to the corresponding nonneoplastic colorectal mucosa. This could be shown by (a) Western blotting of cellular extracts from solid tumours followed by immunostaining with an anti-CKII polyclonal antibody, (b) immunohistochemical staining of cells from tissue sections and (c) by activity measurements using the CKII-specific synthetic peptide (RRRDDDSDDD). The maximum observed activity in the colorectal carcinomas investigated was up to eightfold higher in the tumour specimens than in the non-neoplastic tissue (i.e. colorectal mucosa). The activity range was between 33 -350 U/ mg protein and in the case of colorectal mucosa 13 -106 U/mg protein. The amount of CKII determined in the individual tumours was in the range 0.4-1.6 nmol/g tissue.Casein kinase I1 (CKII) is found in the cytoplasm and in the nucleus. The latter form has also been called NII, although biochemical and biophysical data suggest that it is the same enzyme. The name is misleading inasmuch as the name casein kinase I1 was coined according to its test substrate which is casein.CKII is a ubiquitous protein kinase which is widely distributed in different eukaryotic cell types [I]. The level of enzyme activity has been shown to be elevated in transformed cells [2], in mitogen-stimulated lymphocytes [3], during mouse embryogenesis [4], during differentiation of 3T3-LI cells [5] and during progesterone-induced maturation of oocytes [6]. All these findings suggest a functional role for CKII in the regulation of cellular growth. In detail, CKII has been thought to play a role in the regulation of protein synthesis 141. By immunohistochemical studies, CKII was shown to be highly concentrated in the nucleolus [15, 161, i.e. in the same cellular compartment where some of its potential physiological substrates (RNA polymerase I, topoisomerases I and 11, and nucleolin) are located. These nucleolar proteins are involved in the first steps of cellular growth and CKII seems to be the key enzyme controlling the very first steps of proliferation at the level of rRNA synthesis. Here we demonstrate that CKII is elevated in human solid tumours when compared to nonneoplastic tissue of the same patient. The results are supported by immunohistochemical studies. In addition, we have shown that CKII is not exclusively elevated in tumour cells but also in normal tissue with high mitotic activity (e. g. colorectal mucosa).Thus the data presented are in good agreement with earlier studies, where elevated CKII activity was detected in tumour cell lines [2] and also in non-neoplastic tissue (e.g. during certain stages of embryogenesis) [4]. A comparison with the proliferation marker Ki67 [I71 also suggests that there may be a potential application for CKII as a marker protein for proliferation. MATERIALS AND METHODS Breast carcinomasA tumour and non-neoplastic tissue from a patient with an i...

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Factors involved in initiation of haemoglobin synthesis can be phosphorylated in vitro

Cited by 69 publications

References 19 publications

An adenovirus mutant unable to express VAI RNA displays different growth responses and sensitivity to interferon in various host cell lines.

An adenovirus mutant unable to express VAI RNA displays different growth responses and sensitivity to interferon in various host cell lines.

The phosphorylation of liver ribosomal protein S6 during the development of acute hepatic cell injury induced by D‐galactosamine

Casein kinase II is elevated in solid human tumours and rapidly proliferating non‐neoplastic tissue

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