Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.10.2 (focal adhesion kinase)
44,029 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ability of Ad40 and Ad41 E1A plus E1B genes to transform BRK cells was considerably lower than that of Ad5 and Ad12 corresponding genes. However, as for Ad5, the E1A genes of enteric adenoviruses could cooperate with an activated ras oncogene for full cell transformation and the Ad41 E1B could be complemented by E1A gene of Ad5 or Ad12 for cell transformation. Complementation studies suggested that the conserved region 1 of Ad41 E1A was responsible for this inefficient transformation. The Ad40- and Ad41-transformed cell lines exhibited a low level of major histocompatibility complex (MHC) class I antigens correlated to the low level of Ad12-transformed cells. Class I MHC antigen amounts expressed at the surface of the cells transformed by the weakly oncogenic Ad3 were between the high level of Ad5- and the low level of Ad12-transformed cells.
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PMID:Cellular transformation by E1 genes of enteric adenoviruses. 182 53

We have previously reported that adenovirus E1a mutants lacking the C-terminal 61 or 67 amino acids were severely defective in immortalization, but cooperated more efficiently (than wt E1a) with activated T24 ras oncogene in transformation of primary rat kidney (BRK) cells (Subramanian et al., 1989; Oncogene, 4:415-420). Here, we show that in contrast to these previous results, transformation of BRK cells in cooperation with the Ad2 E1b region is dependent on the C-terminal region of E1a. Mutational analysis of the C-terminal region has revealed that a region located between residues 266 and 276 may be important for E1a/E1b cooperative transformation. Like E1a/T24 ras cooperative transformation, E1a/E1b cooperative transformation also requires two essential domains involved in the binding of two cellular proteins (300K and 105K) within the N-terminal half of E1a. E1a/E1b cooperative transformation therefore requires an additional E1a activity encoded within the C-terminal region of E1a.
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PMID:Requirement of the C-terminal region of adenovirus E1a for cell transformation in cooperation with E1b. 183 Jun 44

The expression of the junB gene parallels the expression of the MHC class I genes in Adenovirus (Ad) transformed cells. In Ad12E1-transformed primary BRK cells both genes are transcriptionally repressed only when the 13S product of Ad12E1A is present. This indicates that repression of MHC class I and junB genes is a function of conserved region 3 (CR3) of the Ad12E1A protein. In Ad5-transformed BRK cells expression of these genes is unchanged. In established NRK cells, however, introduction of Ad12E1A does not cause repression of the MHC class I and junB genes, but in these cells Ad5E1A increases the expression of both MHC class I and junB. Using mutant Ad5E1A genes, it is shown that this activation is mediated by CR1. Introduction of a functional junB gene under the control of a heterologous promoter in Ad12E1-transformed BRK cells causes no increase in MHC class I expression. This demonstrates that the down-regulation of junB is not directly responsible for class I repression, but rather that both genes are coregulated by the Ad12E1 region.
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PMID:Co-regulated expression of junB and MHC class I genes in adenovirus-transformed cells. 190 58

To determine whether the viral replication functions of the adenovirus E1B 55K protein play a role in its ability to transform cloned rat embryo fibroblast cells in culture, we constructed an extensive series of insertion mutations throughout the 55K gene. The mutations were recombined into infectious virus and characterized for their abilities to produce stable 55K protein in HeLa cells, replicate virus in HeLa cells, express late viral proteins efficiently, and transform CREF cells following infection. Mutant 55K transforming activity in primary baby rat kidney cells was also assayed following DNA transfection. The functions required for viral replication are encoded in several patches of the 55K linear sequence, while the CREF transforming functions are sensitive to all of the insertions. An insertion at amino acid 380 created a mutant virus which was reduced in transforming activity, but was not reduced for viral replication. Therefore, a function required for efficient transformation of CREF cells can be separated from functions required for late gene expression and viral replication. Transformation of BRK cells following DNA transfection was reduced by complete disruption of the 55K protein gene, but was not significantly affected by any of the insertions.
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PMID:Dissection of functional domains in the adenovirus 2 early 1B 55K polypeptide by suppressor-linker insertional mutagenesis. 214 3

A serum-albumin-alprenolol conjugate was used to isolate beta-adrenergic receptors from the human A431 cell lysates. Three monoclonal antibodies were obtained from BALB/c mice immunized with these receptors. These antibodies: BRK-1, BRK-2, BRK-3, were respectively of the IgM, IgG2a and IgG3 classes. All three antibodies recognized photoaffinity-labelled receptors, immunoprecipitated ligand-binding activity and identified the 65-kDa and 55-kDa polypeptides corresponding to the beta 2-adrenergic receptors of A431 cells. BRK-2 and BRK-3 recognized both beta 1 and beta 2-adrenergic receptors of several mammalian cells. All three antibodies visualized, by immunofluorescence, the beta 2-adrenergic receptors at the surface of A431 cells. The monoclonal antibodies are directed against the protein portion of the beta-adrenergic receptors since partial or complete removal of the carbohydrate moieties by treatment with endoglycosidase such as endo-F (endo-beta-N-acetylglucosaminidase F) and periodate oxidation did not affect the immunoreactivity. These antibodies will be of value to immunopurify the beta-adrenergic receptors.
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PMID:Monoclonal antibodies directed against the human A431 beta 2-adrenergic receptor recognize two major polypeptide chains. 282 Jul 27

The present study investigates the innervation of the embryonic chick ovary with regard to (i) development and compartmentalization of catecholaminergic nerves, and (ii) presence of adrenoceptors on steroidogenic target cells of catecholaminergic nerve terminals. Catecholaminergic nerve fibers visualized by glyoxylic acid-induced histofluorescence first appeared at embryonic day (E) 13. From E15 through E21 the density of fluorescent aminergic nerves increased markedly in parallel with the concentration of catecholamines and numbers of nerve bundles and single axons seen at the electron-microscopic level. Catecholaminergic nerves were confined to the ovarian medulla and closely associated with interstitial cells. Nerve terminals approached interstitial cells up to a distance of 20 nm and, in their majority, exhibited uptake of the false adrenergic transmitter 5-hydroxydopamine. Although adrenaline amounted to 14% of the total catecholamine content at E21, adrenaline immunoreactivity was only detected in adrenal chromaffin cells, but not in nerve fibers or cell bodies within the ovary. Interstitial cells structurally matured between E15 and E21 as documented by an increase of smooth endoplasmic reticulum and tubular mitochondria. Monoclonal antibodies mAB 120 and BRK 2 raised against avian beta 1- and mammalian beta 2-adrenergic receptors revealed the presence of beta 2-adrenoceptor-like immunoreactivity on the surface of interstitial cells, but not on any other cell type. The results are consistent with the notion of a dense adrenergic innervation of the embryonic chick ovarian medulla and its steroidogenic interstitial cells, and suggest the chick ovary as an excellent model for elucidating the functional role of a neural input to steroidogenic cells during development.
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PMID:Catecholaminergic nerves in the embryonic chick ovary: co-localization with beta 2-adrenoceptor-bearing steroidogenic cells. 284 26

We have analyzed the cell cycle effects that different domains of the adenovirus E1A proteins have on quiescent primary BRK cells. Studies with deletion mutants that in combination removed all but the N-terminal 85 amino acids common to both the 12S and 13S proteins suggest that this region may be sufficient for the induction of synthesis of proliferating cell nuclear antigen and the stimulation of DNA synthesis. A second domain also common to the N-terminal exon of the 12S and 13S proteins was required for the induction of mitosis and stimulation of proliferation of primary BRK cells. A virus containing a mutation in this region was still able to stimulate DNA synthesis efficiently. A third domain, unique to the 13S protein, was required for the accelerated activation of the cellular thymidylate synthase gene in a manner similar to the 13S-dependent stimulation of adenovirus early region genes.
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PMID:Different functional domains of the adenovirus E1A gene are involved in regulation of host cell cycle products. 288 Nov 97

To distinguish the individual roles of the 13S, 12S, and 9S adenovirus E1A gene products, we isolated the corresponding cDNA clones and recombined them into both plasmids and viruses. Only the expected E1A mRNA products were made from the corresponding 12S and 13S viruses. The 9S mRNA was detected when the 9S virus was coinfected with the 13S virus but not when either virus was infected alone. The 13S virus formed plaques equally well in 293 cells, HeLa cells, and A549 cells, a human lung oat cell carcinoma line. Plaque titers of the 12S virus were much reduced in HeLa and A549 cells compared with 293 cells, although the 12S virus is multiplicity-dependent leaky in both HeLa and A549 cells. A549 cells were significantly more permissive than HeLa cells for growth of the 12S virus. In A549 cells even at low multiplicities of infection the final yield of 12S virus eventually approached the maximum yield from 293 cells. Expression from the adenovirus early region 2 and early region 3 promoters in HeLa cells was activated in the presence of a 13S cDNA E1A region but not in the presence of a 12S E1A cDNA region. Although defective for lytic growth in HeLa cells, the 12S virus immortalized BRK cells at very high efficiency, whereas infection of these cells with 13S virus, as with wild-type E1A virus, resulted mainly in cell death. The 13S product does have an immortalization function, however, revealed in the absence of adenovirus lytic functions when a plasmid containing the E1A 13S cDNA region was transfected into BRK cells. The 9S virus failed to immortalize infected BRK cells or to interfere with focus formation when coinfected with the 12S virus.
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PMID:Lytic and transforming functions of individual products of the adenovirus E1A gene. 293 98

Tumour necrosis factor alpha (ref. 1), synthesized primarily by monocytes in response to various invasive agents, induces a wide variety of biological effects relevant to regulating cell growth and differentiation, including the selective killing of some tumour cells and the growth stimulation of some normal fibroblasts. As tumour necrosis factor (TNF) appears to kill tumour cells preferentially, we asked whether TNF sensitivity correlates with the expression of specific oncogene(s). If so, by examining the cellular target(s) of the oncogene product, it might be possible to identify specific factor(s) which mediate TNF action. By using an in vitro cytotoxicity assay with NIH 3T3 and Fisher BRK-derived cells expressing exogenously introduced oncogenes, we found that adenovirus E1A proteins induce susceptibility to TNF killing.
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PMID:Induction by E1A oncogene expression of cellular susceptibility to lysis by TNF. 296 Sep 1

The human adenovirus type 12 (H12) E1A region encodes two early proteins of 266 amino acid residues (266R) and 235R whilst the H12 E1B promoter directs the synthesis of two major proteins of 163R and 482R. To determine the functions of E1A and E1B in lytic infection and oncogenic transformation we have isolated and characterized a series of H12 E1 mutants. Mutant H12 hr 700 contains a point mutation in exon 1 that alters a single amino acid common to both the 266 and 235R proteins. This mutant synthesized reduced levels of E1 and structural proteins at delayed times in HEK cells, transformed BRK cells, and induced tumors in newborn rats at reduced efficiency compared to wild-type virus. The mutation in H12 in 600 truncates the 266R protein in its unique sequences but this mutant synthesized the 235R, E1B, and structural proteins at delayed times in HEK cells. H12 in 600 was nontransforming but induced rare tumors in newborn rats. A third E1A mutant H12 in 601 synthesized no E1A proteins, reduced levels of E1B and structural proteins at delayed times in lytic infections, and was not a transforming or oncogenic virus. Three E1B mutants were studied in detail. Both H12 hr 703 and H12 in 602 encode N-terminal truncated 482R proteins whereas H12 del 620 encodes an in-frame internally deleted 482R protein. All three synthesized reduced amounts of E1A proteins and the E1B 163R protein, identifying a regulatory function for the 482R protein. None of the E1B mutants could transform and only H12 del 620 could induce rare tumors in newborn rats. These results show that H12 oncogenesis requires the coordinated expression of the E1 proteins.
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PMID:Host range mutants of adenovirus type 12 E1 defective for lytic infection, transformation, and oncogenicity. 296 53


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