Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The action of micrococcal nuclease, DNase I and DNase II on mouse TLT hepatoma chromatin revealing the periodicity of its structure as visualized by denaturing and non-denaturing gel electrophoresis, was consistent with the action of these enzymes on other chromatins. Micrococcal nuclease showed a complex subnucleosome fragment pattern based on multiples of 10 base pairs with a prominant couplet at 140/160 base pairs and the absence of the 80 base pair fragment. This couplet of the core and minimal nucleosome fragments was conspicuously present in the mononucleosomes found in the 11S fractions of a glycerol gradient centrifugation. DNase I and II produced a fairly even distribution of a 10 base pair increasing series of fragments to about 180 base pairs, a pattern also repeated in the DNA of nucleosome glycerol-gradient fractions. In limited digestions by these nucleases multinucleosomic DNA fragments are pronounced. These fragment lengths are multiples of an estimated average repeat length of nucleosome DNA of 180 base pairs. The action of the endogenous Mg/Ca-stimulated endonuclease produced only limited cuts in the hepatoma chromatin resulting primarily in multi-nucleosomic DNA fragment lengths and only upon lengthy digestion limited subnucleosomic, 10-base-pair multiple fragments are produced. The putative euchromatin-enriched fractions (50-75S) of the glycerol gradient centrifugation of autodigested chromatin, similarly, contained primarily the multinucleosomic DNA fragment lengths. These results are consistent with our previous electron microscopic demonstration that autodigested chromatin as well as the putative euchromatin-enriched fractions were composed of multi-nucleosomic chromatin segments containing a full complement of histones.
Mol Cell Biochem 1978 Apr 11
PMID:Periodicity and fragment size of DNA from mouse TLT hepatoma chromatin and chromatin fractions using endogenous and exogenous nucleases. 20 20

Rat hepatoma cells infected with mouse mammary tumor virus (MMTV) acquire viral DNA that becomes covalently linked to the cell DNA. Using restriction endonucleases and the DNA transfer procedure of Southern [Southern , E.M. (1975) J. Mol. Biol. 98, 503--517], we have studied the sites in cellular DNA into which MMTV DNA inserts. These experiments indicate that: (i) there are many sites in cell DNA into which MMTV DNA integrates; (ii) the junctions between viral and cellular DNA occur within a limited portion of the viral genome, (iii) clones that contain MMTV DNA do not necessarily produce viral RNA; and (iv) the extent of transcription and glucocorticoid responsiveness of MMTV proviruses may be dependent on the site(s) in cell DNA in which the viral DNA resides.
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PMID:Integration and transcription of mouse mammary tumor virus DNA in rat hepatoma cells. 21 15

The rate of nucleotide substitution (k(nuc)) of 5s RNA was estimated to be (1.8 +/- 0.5) x 10(-10) per site per year by comparing the nucleotide sequences of human and Xenopus 5s RNA and using the geological time elapsed since the separation of mammals and amphibians. Similarly, k(nuc) of 5.8s rRNA was calculated to be 0.93 10(-1u) per site per year from the sequences of rat hepatoma cells and Saccbaromyces cerevisiae. For the comparison of these data with the amino acid substitution rate of known proteins, the k(nuc) values of 5s rRNA and 5.8s rRNA were converted to the rate of amino acid substitution (k(aa')). The k(aa') values in pauling units were 0.4 and 2 0.3, respectively. The average k(aa) of ribosomal proteins was also estimated to be 0.2 0.3 pauling from the N-terminal amino acid sequences of seventeen 30s ribosomal proteins of Bacillus stearothermopbilus and Eschericbia coli. Thus, the evolutionary rates of these ribosomal components studied here are similar to each other; they considerably slower than that of the known cellular proteins. Most, if not all, of the replacements in ribosomal proteins occurred between amino acids of a chemically similar nature.
J Mol Evol 1977 May 13
PMID:The rates of evolution in some ribosomal components. 32 17

The six fractions of rat liver DNA (DNAL) and hepatoma Zaidel DNA (DNAHZ) were obtained by thermal fractionation of these DNAs on a HAP column at equivalent temperature intervals. The percent of two thermolabile fractions obtained at 62--78 degrees is approximately 10% higher for DNAHZ than for DNAL. The reassociation kinetics were carried out till Cot = 5.10(-1). Computer analysis of the kinetics showed considerable difference between the parameters (percent of the sequence and rate constant) only for these thermolabile fractions DNAL and DNAHZ. The two-fold reduction of the reassociation rate for the second thermolabile fraction DNAHZ (63--78 degrees) can be associated with the presence of short uncomplementary pieces in the fast repeating sequences. On the other hand the increase of the rate constant for the initial part of the kinetics reassociation of the first thermolabile fraction (62--73 degrees) of DNAHZ is due to the nicks which are revealed by alkali sucrose centrifugation of the DNAHZ fractions.
Mol Biol (Mosk)
PMID:[Peculiarities of the reassociation kinetics of fast repeating sequences of thermolabile fractions of hepatoma Zaidel DNA]. 46 Jan 94

A comparative study of the position specificity of tRNA-methylases from normal and tumour tissues was performed on yeast tRNA1Val as the substrates using partially purified enzyme preparations from rat kidney and carcinoma RA. As in the case of rat liver and Novikoff hepatoma, two methylated compounds are formed in yeast tRNA1Val under the action of rat kidney and carcinoma enzyme preparations: m5C is formed in the sequence C49--C52 located in the extra loop and A59 in the Tpsi-loop is is converted into m1A. The activity of m5C-methylase [S-Ado-Met-tRNA-(cytosine-5)methyltransferase] (E. C. 2.1.1.29) is approximately equal in both tissues, whereas the activity of m1A-methylase [S-Ado-Met-tRNA-(adenine-1)methyltransferase] (E. C. 2.1.1.36) in carcinoma is twice as high as in the kidney. The two enzymes do not differ in their position specificity.
Mol Biol (Mosk)
PMID:[Comparative study of the tRNA-methylases of normal and tumor tissues. II. Positional specificity of renal and carcinoma RA methylases]. 61 46

Transplantable rat liver tumors 5123 t.c., 7288 ct.c., 5123 t.c.(H) and the Novikoff hepatoma have active mixed function oxidase systems capable of metabolizing a variety of drug and polycyclic hydrocarbon substrates. The tumor drug metabolism systems are at best 20% as active as rat liver. The tumor drug metabolism activities are induced by pretreatment with phenobarbital or beta-naphthoflavone and can be inhibited with specific inhibitors such as carbon monoxide or 7,8-benzoflavone. Tumor drug metabolism systems appear to consist of cytochrome P-450 and cytochrome P-450 reductase. The properties of the two protein components from tumors are highly similar to the corresponding components of the liver drug metabolism system. Cytochrome P-450 reductase has been at least partially purified from the Novikoff hepatoma and hepatoma 5123 t.c.(H). The kinetic and physical properties of the tumor reductases are similar to those of the liver reductase except that the Km of hepatoma 5123 t.c.(H) reductase, but not of the Novikoff hepatoma reductase for NADPH, is elevated an order of magnitude over the Km of the liver reductase. The mechanism for the interaction of electron donor and electron acceptor with liver or tumor reductases seems to be a sequential reaction mechanism. Experiments on the NADP-inhibition of the interaction of NADPH and cytochrome c with liver reductase indicate that NADP is competitive with NADPH and noncompetitive with cytochrome c. This result is consistent with the postulate of a sequential reaction for NADPH-cytochrome P-450 reductases of liver and tumors. These data support the conclusions that an active drug metabolism system is present in liver tumors and that the tumor systems are constituted like the liver system.
Mol Cell Biochem 1978 Dec 22
PMID:The drug metabolism systems of liver and liver tumors: a comparison of activities and characteristics. 74 99

Chromatin from TLT hepatoma cells, mouse liver cells, and mouse brain cells was fractionated by differential centrifugation into a pellet, enriched with heterochromatin, and a supernatant, enriched with euchromatin. The pellet was found to contain more than twice as much of a particular species of chromatin-associated RNA per milligram chromatin DNA as did the supernatant. This chromatin-associated RNA was also found to be associated with the transcriptionally inactive chromatin of mature avian erythrocytes. Bull sperm, whose genome is known to be completely inactive, was used as the source in the preparation of sperm heads. Bull sperm head RNA appeared to consist of a single, low molecular weight species which migrated on polyacrylamide gels at a rate just slightly slower than the aforementioned chromatin-associated RNA. The results are interpreted as indicating that this chromatin-associated RNA is more prevalently associated with the heterochromatic fraction of chromatin. It is postulated that this chromatin-associated RNA might constitute a structural component of heterochromatin.
Mol Cell Biochem 1975 Oct 31
PMID:Chromatin-associated RNA content of heterochromatin and euchromatin. 118 64

Nuclei of MPC 11 mouse myeloma cells contain several species of small RNAs related to those found in other mammalian cells. These include U1 RNA, about 190 nucleotides in length and U2 RNA, about 170 nucleotides long. The 5'-termini of 32P-labelled U1 and U2 RNAs have been investigated by a fingerprinting technique involving digestion with T2-ribonuclease. The RNAs were found to have modified 5'-terminal structures of the form m3G(5')ppp (5')AmpUmpAp for U1 RNA and m3G(5')ppp(5')AmpUmpCmpCp for U2 RNA, where m3G is N2, N27-trimethyl guanosine and Am and Um are 2'-O-methyl nucleosides. These 5'-terminal sequences are the same as those proposed for rat hepatoma U1 and U2 RNAs (Ro-Choi et al., Fed. Proc. 33, 1548, 1974) but with triphosphate rather than diphosphate links.
Mol Biol Rep 1975 Dec
PMID:Modified 5'-termini in small nuclear RNAs of mouse myeloma cells. 121 81

Transforming growth factor-beta (TGF beta) has been implicated in the regulation of hepatocyte function. We have examined TGF beta 1 regulation of albumin and alpha-fetoprotein (AFP) mRNA levels in a well differentiated mouse hepatoma cell line (BWTG3). TGF beta 1 reversibly decreased steady state mRNA levels of both albumin and AFP. By nuclear run-on assays, we found that TGF beta 1 caused no significant change in transcription rates for albumin or AFP. Pretreatment with actinomycin-D prevented the TGF beta 1-induced decrease in albumin and AFP mRNA levels. Also, if cells were treated with actinomycin-D after a 12-h exposure to TGF beta 1, actinomycin-D abrogated the further decrease in albumin and AFP mRNA levels that occurred after treatment with TGF beta 1 alone. Cycloheximide pretreatment blocked the TGF beta 1-induced decrease in albumin and AFP mRNA levels. TGF beta 1 altered neither the rate of BWTG3 cell growth nor the levels of mRNA for the growth-associated protooncogene c-myc. These data suggest that TGF beta 1 has regulatory effects on specific hepatocyte functions that are independent of growth regulatory effects. The decrease in albumin and AFP mRNAs caused by TGF beta 1 is posttranscriptional and dependent upon de novo RNA and protein synthesis.
Mol Endocrinol 1992 Nov
PMID:Posttranscriptional regulation of albumin and alpha-fetoprotein messenger RNA by transforming growth factor-beta 1 requires de novo RNA and protein synthesis. 128 69

Insulin-like growth factor-binding protein-1 (IGFBP-1) can inhibit or potentiate IGF action. The biological activity of IGFBP-1 is determined by many factors, including its abundance in tissues and plasma, posttranslational modifications, and localization. IGFBP-1 levels in human plasma are highly regulated. They are increased after acute fasting and in diabetes, and are rapidly reversed by refeeding and insulin treatment, respectively. Similarly, IGFBP-1 mRNA is increased in the liver of severely diabetic and ketotic rats and decreased after 4 days of insulin treatment. Insulin rapidly decreases IGFBP-1 mRNA and IGFBP-1 transcription in rat hepatoma cells. The present study asks whether the increase in IGFBP-1 mRNA in diabetic rat liver reflects increased gene transcription, whether insulin decreases IGFBP-1 mRNA through a transcriptional or posttranscriptional mechanism, and whether this decrease is sufficiently rapid to account for the dynamic fluctuations in plasma IGFBP-1. Rats were injected ip with 100 mg/kg streptozotocin and used 7 days later when they were hyperglycemic and failed to gain weight, but were not ketotic. Hepatic IGFBP-1 mRNA levels were 13.6 +/- 5.3-fold greater in diabetic than control liver and decreased to the low levels in nondiabetic controls within 1 h after insulin treatment. In run-on transcription assays, IGFBP-1 transcription was 12.6 +/- 1.5-fold greater in nuclei from diabetic than control liver and decreased to low control levels by 1 h after insulin injection. Normalization of hepatic IGFBP-1 mRNA in insulin-treated diabetic animals did not require restoration of euglycemia. IGFBP-1 mRNA and IGFBP-1 gene transcription also were increased in the kidney of diabetic ketotic rats. We propose that the dynamic regulation of IGFBP-1 gene transcription in diabetes and after insulin treatment, by determining the availability of IGFBP-1 in tissues and plasma, may be a critical factor in the modulation of IGF action.
Mol Endocrinol 1992 Dec
PMID:Insulin rapidly decreases insulin-like growth factor-binding protein-1 gene transcription in streptozotocin-diabetic rats. 128 42


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