Blink rate and blunted affect among chronic schizophrenic patients.
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Adult↗
Biomedical subjects
A Kahn
Publications and source records attributed to A Kahn.
Nucleotide sequence of a cDNA clone for human aldolase B.
Two specific clones for human aldolase B were isolated from a human liver cDNA library using a rat aldolase B cDNA probe. The clones were identified by positive hybridization-selection and one of them was sequenced. The 127 C-terminal residues of the human protein were deduced from this nucleotide sequence analysis. They showed 92% homology with the corresponding previously published amino-acid sequence of rat liver aldolase B.
Amino Acid Sequence↗
Molecular cloning of cDNA for rat L-type pyruvate kinase and aldolase B.
Two double-stranded cDNA recombinant pBR322 plasmid libraries were constructed starting from high carbohydrate diet rat liver poly(A)+ mRNA, either fractionated by denaturing sucrose gradient centrifugation for the cloning of L-type pyruvate kinase cDNA, or nonfractionated for aldolase B. Both libraries were screened with single-stranded cDNA probes reverse transcribed from fasted or high carbohydrate diet rat liver mRNAs. mRNAs from fasted animals were also fractionated by sucrose gradient centrifugation and mRNAs from the fed animals were, in addition, further purified by high performance liquid gel filtration chromatography. Those clones hybridizing with the "positive" probe (from animals fed the high carbohydrate diet) and not with the "negative" one (from fasted animals) were preselected and their plasmid DNA was purified and analyzed by positive hybridization-selection. Thirty of 4500 bacteria colonies transformed by recombinant plasmids were preselected by differential screening for pyruvate kinase, and 8 of 864 colonies for aldolase B. Twenty-two recombinant plasmids for pyruvate kinase and two for aldolase B were shown to contain specific cDNA inserts by positive hybridization-selection. Plasmids DNAs of some pyruvate kinase and aldolase B clones (whose inserts ranged from 700 to 1050 bases in length) were labeled by nick translation and used as probes for Northern blot hybridization. The pyruvate kinase cDNA probes recognized mainly a 3400-base RNA species which was detected in high carbohydrate diet rat liver, but not in fasted rat liver and in tissues which do not synthesize L-type pyruvate kinase. In addition, some pyruvate kinase probes hybridized with minor RNA species of about 2000 bases in length, only observed after carbohydrate diet. For aldolase B, the recombinant plasmid DNA hybridized with a single RNA species of 1750 bases. This RNA, detected in kidney, small intestine and liver, was induced by a high carbohydrate diet and increased with liver development. The rat probe cross-hybridized with human aldolase B messenger RNA.
Animals↗
[Role of the oncogenes and the protein kinases in carcinogenesis].
The genome of higher animals contains genes called cOnc which are thought to be responsible for cancer when activated. Many oncogenic retroviruses also contain vOnc genes responsible for their transforming properties. cOnc sequences are homologous and result, in fact, from genetic recombinations between retroviruses lacking transforming genes and the animal genome. Onc genes encode transforming proteins which are biological intermediates of their carcinogenic property and may consist of protein kinases active on membrane and cytoskeleton constituents or nuclear proteins probably active on DNA. Modifications of cOnc genes (or oncogenes) due, in particular, to chromosomal rearrangements and occasional mutations have been demonstrated in an increasing number of human cancers.
Animals↗
Induction of glycolytic enzyme synthesis in proliferating fibroblasts. Study of phosphofructokinase, glucose phosphate isomerase and pyruvate kinase.
Specific activity of phosphofructokinase is 7-8-fold higher in exponentially growing human fibroblasts than in quiescent cells, but the difference is considerably less pronounced for two other glycolytic enzymes, glucose phosphate isomerase and pyruvate kinase. The ratio of the F-type to L-type phosphofructokinase subunits is essentially the same in growing and resting cells, 4:1. F-type-phosphofructokinase-related antigen concentration is decreased in resting cells as compared with proliferating fibroblasts, but relatively less than the enzyme activity; the ratio of the enzyme activity to the antigen concentration (immunological specific activity) is therefore lower in resting than in growing fibroblasts. Synthesis of phosphofructokinase, as a percentage of the total protein synthesis, is about 30-fold greater during the proliferative phase than in quiescent cells, but this difference is only 3-4-fold for glucose phosphate isomerase and pyruvate kinase. Modulation of the synthesis of phosphofructokinase therefore seems to be responsible for the changes of its specific activity in function of cell proliferation. The appearance of some inactive cross-reacting material in quiescent cells is probably due to post-translational alteration of the pre-synthesized molecules. Compared with other glycolytic enzymes, such as glucose phosphate isomerase and pyruvate kinase, phosphofructokinase seems to be the (or one of the) preferential target of glycolytic induction in proliferating cells.
Cell Division↗
Isolation and characterization of cDNA clones for human skeletal muscle alpha actin.
Two cDNA libraries corresponding to polyA+ RNA from human adult skeletal muscle have been constructed by cloning in the PstI site of pBR322. Skeletal alpha actin cDNA clones have been isolated and characterized. Three of these plasmids have overlapping inserts which together contain the complete 5' non-coding and protein-coding region and part of the 3' untranslated region. Determination of the sequence of the cloned cDNA confirms the complete conservation in human of the amino-acid sequence of skeletal alpha actin compared to the rabbit or rat proteins. The 5' untranslated region, but not the 3' untranslated region, shows good homology with the corresponding one in the rat gene. Analysis of changes at silent sites within the protein-coding region suggests that the divergence of skeletal and cardiac alpha actin took place much earlier than the mammalian radiation. The plasmids described here have been used as probes to detect the homologous gene among the about thirty actin sequences present in the human genome.
Actins↗
Monocyte chemotaxis: stimulation by specific exosite region in thrombin.
Human alpha-thrombin is a potent chemoattractant for human monocytes, with optimum activity occurring at about 10 nanomoles per liter. A variety of thrombins that were chemically modified to alter procoagulant or esterolytic functions showed a similar optimum activity, but complexes of prothrombin or alpha-thrombin with either antithrombin III or hirudin did not. These findings indicate that the regions in thrombin responsible for monocyte chemotaxis are proximate to those involved in certain protein recognition interactions of alpha-thrombin (for example, hirudin binding) but are distinct from the catalytic site and from certain exosites required for clotting.
Binding Sites↗
Protein kinases of rat liver during hepatocarcinogenesis induced by an azo dye.
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Animals↗
Protein kinases in normal human blood cells.
Protein kinases active on basic and acidic artificial substrates were investigated in normal human erythrocytes, platelets, polymorphonuclear and mononuclear cells. These two types of protein kinases were partially purified by affinity chromatography, then assayed for their enzymatic activity using [gamma-32P]ATP or GTP as phosphoryl donor. Partially purified kinases active on acidic substrates were subjected to high-performance liquid chromatography (HPLC). Protein kinases active on basic substrates were analyzed by cellulose acetate electrophoresis of crude cellular extracts and the influence of 3'5' cyclic AMP was studied. Three forms of casein-phosvitin kinases could be distinguished according to their molecular weight (165 K, 38 K, and 31 K). The 165 K species, in contrast to the light species, can use GTP instead of ATP as phosphoryl donor and corresponds to the "so-called" casein kinase 2. This form is very sensitive to proteolysis and, when partial purification is performed without the addition of various antiproteolytic agents, it is degraded into 120-135 K and 105-115 K active species; this artefactual degradative process is especially active in platelet extracts. As many as eight different active bands of histone and protamine kinases can be separated by cellulose acetate electrophoresis, several of them being stimulated by cyclic AMP. Isozymic patterns of protein kinases, levels of activity on the different substrates, and utilization of ATP and GTP were found to be specific for each cell type. These results suggest the possibility of using protein kinases as markers for cell differentiation.
Blood Cells↗
Synchronous tumors in both ureters and left renal pelvis.
A case of bilateral, synchronous ureteral tumors and a tumor in the left renal pelvis is presented. Conservative surgical treatment involved local resection of both ureteral tumors and partial nephrectomy of the left kidney. Multiple urothelial tumors subsequently developed in the bladder which were resected. The patient has had good kidney function and no evidence of disease.
Aged↗
Chemotactic response of monocytes to thrombin.
Human alpha-thrombin, the procoagulant activation product of prothrombin, elicits chemotaxis in human peripheral blood monocytes and several macrophagelike continuous cell lines, most notably J-774.2, but not in human peripheral blood granulocytes. alpha-Thrombin is effective in stimulating cell movement at concentrations ranging from 10(-10) to 10(-6) M but is optimally active at 10(-8) M. At the latter concentration, the degree of response is equivalent, on a molar basis, to that observed with the peptide formylmethionylleucylphenylalanine, (FMP). In contrast to thrombin, prothrombin produces a minimal chemotactic response in monocytes and J-774.2. Blockade of alpha-thrombin's active center with diisopropylfluorophosphate (DIP-F) or tryptic proteolysis of the procoagulant exosite (i.e., gamma-thrombin) fails to alter chemotactic activity. On the other hand, addition of equimolar amounts of antithrombin III (AT3) to alpha-thrombin reduces thrombin-mediated chemotaxis by 60%, and increased ratios of AT3 to enzyme completely suppress chemotaxis. We conclude that thrombin is a potent monocyte chemotaxin and that the domains in thrombin involved in stimulating cell movement are distinct from the catalytic site and the fibrin recognition exosite. These chemotactic domains appear to be sequestered in prothrombin and in the thrombin-AT3 complex and, as such, are unavailable to the chemotactic receptor on the monocyte cell membrane.
Binding Sites↗
Absence of functional messenger RNA for glycogen phosphorylase in the muscle of two patients with McArdle's disease.
(1) Two unrelated cases of McArdle's disease (glycogen storage disease type V, deficiency in muscle-type glycogen phosphorylase, EC.2.4.1.1) with no detectable inactive protein, and two heterozygous relatives of one patient, have been investigated for the presence or absence of functional messenger RNA. Methods were developed and scaled down to be compatible with clinical-size biopsies. (2) Total muscle RNA was prepared and translated in a rabbit reticulocyte cell-free system. Neosynthesized products were isolated by immunoaffinity microchromatography. Phosphorylase was compared with control enzymes neosynthesized and purified under the same conditions. (3) No functional mRNA for phosphorylase could be detected in the muscles of the two patients. A decreased amount of messenger for phosphorylase, compared with the control enzymes, was found in the muscles of the two heterozygotes. (4) Exploration of functional messenger RNA in clinical enzymopathies should be readily adaptable to a number of enzymatic diseases.
Adolescent↗
Preoperative chemotherapy for hypopharyngeal carcinoma.
Twenty patients with advanced squamous cell carcinoma of the hypopharynx received two courses of chemotherapy with cisplatinum, vincristine and bleomycin before undergoing surgery. The chemotherapy was well tolerated, with minimal toxicity and no intra or postoperative complications attributable to it. The response to the chemotherapy was dramatic with all but 2 patients exhibiting a greater than 50% tumor shrinkage. Only 3 patients, all with positive surgical margins, received postoperative radiation therapy. Surgical salvage of recurrent lesions was performed on 2 patients who are now free of disease. With a median follow-up of 20 months, 1 patient has died of recurrent disease, 3 have died of other causes, all others remain free of disease.
Antineoplastic Agents↗
Protein ADP-ribosylation in rat liver cytosol.
ADP and poly ADP-ribosylation are post-translational modifications of proteins which have been reported to occur essentially in eucaryotic nuclei. This phenomenon has been shown to interfere with a great variety of biological functions (cell differentiation, DNA repair, malignant transformation...). In this paper, we demonstrate for the first time that ADP-ribosylation occurs also in cytosol (120 000 g supernatant) and that several cytosolic proteins can be ADP-ribosylated in rat liver.
Adenosine Diphosphate Ribose↗
Concerning regulatory peptides and hormones.
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Homeostasis↗
Blood pressure--high and low.
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Dietary Fats↗
Vascular disease.
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Angioplasty, Balloon↗