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Biomedical subjects

T Hunter

Publications and source records attributed to T Hunter.

At least 307 records · Page 17Linked to original sources
PubMed1985

Platelet bound IgG levels in patients with systemic lupus erythematosus.

Platelet bound IgG (PBIgG) measured by antiglobulin consumption assay was compared with indices of clinical and laboratory disease activity in 37 nonthrombocytopenic patients with systemic lupus erythematosus. There was no correlation with clinical disease activity. When patients with a PBIgG level over 50 ng/10(7) platelets were compared to those with normal PBIgG levels (less than 20 ng/10(7) platelets), however, they had a significantly higher DNA binding level (p less than 0.05). In 17 patients there was no correlation between PBIgG levels and circulating immune complexes as measured by the Raji cell assay. Ten patients with PBIgG levels over 50 ng/10(7) platelets were followed for a mean of 23 months (5-26 months). None developed thrombocytopenia.

Adult↗
PubMed1984

Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro.

Enolase, lactate dehydrogenase, and phosphoglycerate mutase have previously been found to contain phosphotyrosine in fibroblasts transformed by Rous sarcoma virus, which encodes a tyrosine-specific protein kinase. However, these phosphorylations are not stoichiometric, and their significance for any aspect of the transformed phenotype is unknown. We show here that enolase and lactate dehydrogenase are each phosphorylated chiefly at a single tyrosine in Rous sarcoma virus-transformed cells. The purified enzymes can also be phosphorylated at the same tyrosine in vitro when incubated with an immunoprecipitated retroviral transforming protein having associated tyrosine protein kinase activity. The phosphorylated tyrosine in lactate dehydrogenase is amino acid 238. The phosphorylated tyrosine in enolase lies in a sequence homologous to that surrounding histidine 43 in yeast enolase. Although the phosphorylated sequence in lactate dehydrogenase shows some homology to those sequences surrounding phosphotyrosines found in retroviral transforming proteins, the phosphorylated sequence in enolase is quite different.

Amino Acid Sequence↗
PubMed1984

C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.

The Ca2+- and phospholipid-dependent protein kinase (C-kinase) binds tightly in the presence of Ca2+ to purified membranes of A431 human epidermoid carcinoma cells. The major membrane substrate for C-kinase is the epidermal growth factor (EGF) receptor. Phosphorylation of the EGF receptor is Ca2+-dependent and occurs at threonine and serine residues. After tryptic digestion of the receptor, three major phosphothreonine-containing peptides were identified. These are identical with three new phosphopeptides present in the EGF receptor isolated from A431 cells treated with either of the tumor promoters 12-O-tetradecanoylphorbol 13-acetate or teleocidin. C-kinase catalyzes phosphorylation at these same sites in purified EGF receptor protein. These results indicate that, in A431 cells exposed to tumor promoters, C-kinase catalyzes phosphorylation of a significant population of EGF receptor molecules. This phosphorylation of EGF receptors results in decreased self-phosphorylation of the EGF receptor at tyrosine residues both in vivo and in vitro and in decreased EGF-stimulated tyrosine kinase activity in vivo.

Animals↗
PubMed1984

Polyoma middle-sized T antigen can be phosphorylated on tyrosine at multiple sites in vitro.

The polyoma middle-sized T antigen (MT antigen) is associated with a protein kinase activity which phosphorylates tyrosine residues in polyoma T antigens in vitro. We have studied the sites of tyrosine phosphorylation of MT antigens phosphorylated in immunoprecipitates or in soluble form after partial purification by immunoaffinity chromatography. By analyzing the amino acid sequences of tryptic peptides of MT antigen, and by analyzing deletion mutant MT antigens, we have identified two major sites of phosphorylation in MT antigen, tyrosines 250 and 315. Additional sites were phosphorylated under some conditions. A synthetic peptide (Glu.Glu.Glu.Glu.Tyr.Met.Pro.Met.Glu), corresponding to the sequence around tyrosine 315, was phosphorylated when added to immunoprecipitates containing MT antigen.

Amino Acid Sequence↗
PubMed1984

Medical politics: decline in the hegemony of the Australian Medical Association?

The last 15 years have seen the emergence of medical associations challenging the long-standing hegemony of the Australian Medical Association (A.M.A.) in medical politics. The article focuses on the two major groups. The General Practitioners' Society in Australia and the Doctors Reform Society. Each represents the right and the left of an ideological spectrum within medical politics. Each has institutionalised longer term division within the profession which were contained within the A.M.A. so long as the basic principles and structure of Australia's voluntaristic health insurance schemes remained intact. Taken together, they represent a wider critique of the entrenched status and political power of the A.M.A. The article examines briefly the ideology, strategy and impact of each group. It concludes that their major significance lies, not in their effectiveness as pressure groups, but as they have affected the public image of the A.M.A. and of the profession as a whole. The future of each depends on secular changes affecting medicine and the profession, on the oversupply of doctors on economic stringencies, and importantly, on the reaction of the A.M.A. to critiques of its representative function.

Australia↗
PubMed1984

The 46,000-dalton tyrosine protein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues.

Proteins of molecular mass 46,000 (p46) and 34,000-39,000 (p36) daltons are phosphorylated at tyrosine in Rous sarcoma virus-transformed chicken and mouse fibroblasts. p46 has recently been identified as an isozyme of enolase but the function of p36 is unknown. The expression of these proteins in various mouse and rat tissues has been examined. In most tissues, except muscle, p46 is found at relatively constant levels. In muscle, a more basic, related protein is present. In contrast, the abundance of p36 varies more widely from tissue to tissue, suggesting that it has a function in some but not all differentiated cells. By SDS gel electrophoresis and immunoblotting, high levels of p36 (60-120% of its relative abundance in fibroblasts) were found in small intestine, lung, and thymus, and intermediate levels (20-50%) were found in spleen, lymph nodes, and testes. No p36 was detectable in brain and muscle. Where studied, p36 mRNA expression paralleled protein levels. The cell types within each tissue expressing p36 were identified by immunofluorescence and immunoperoxidase staining. These cell types include all endothelial cells and fibroblastic cells examined, as well as various epithelial cells, cardiac muscle cells, macrophages, and testicular interstitial cells. We were unable to detect p36 in skeletal or smooth muscle cells, erythrocytes, nerve cells, or lymphocytes in any of the examined tissues. p36 appears to be concentrated in the terminal web region of intestinal columnar epithelial cells.

Animals↗
PubMed1984

Diverse mitogenic agents induce the phosphorylation of two related 42,000-dalton proteins on tyrosine in quiescent chick cells.

Incubation of quiescent chicken embryo cells with platelet-derived growth factor, epidermal growth factor, or serum was found to stimulate phosphorylation of two proteins of ca. 42,000 daltons on tyrosine. These proteins are structurally related to each other and to two proteins phosphorylated on tyrosine under similar conditions in mitogen-treated mouse fibroblasts. Three other very different mitogenic agents, the protease trypsin and the chemically unrelated tumor promoters 12-O-tetradecanoyl-phorbol-13-acetate and teleocidin, stimulated phosphorylation of the same proteins. In all cases, phosphotyrosine was detected in these phosphoproteins. Although additional changes in protein phosphorylation were evident, no other proteins were observed by two-dimensional gel electrophoresis which contained increased amounts of phosphotyrosine in mitogen-treated chicken embryo cells. One of these 42,000-dalton proteins was shown previously to be phosphorylated on tyrosine in chicken embryo cells transformed with various retroviruses whose transforming proteins possess tyrosine protein kinase activity. Phosphorylation of the 42,000-dalton proteins could be important in the regulation of cell division.

Animals↗
PubMed1984

Characterization of the protein apparently responsible for the elevated tyrosine protein kinase activity in LSTRA cells.

The LSTRA murine thymoma cell line contains an elevated level of tyrosine protein kinase activity. When a microsomal preparation from these cells is incubated in vitro with ATP, the principal tyrosine protein kinase substrate is a 56,000-dalton protein, p56. We have found that an activity phosphorylating p56 on tyrosine can also be detected at low levels in microsomes from most, but not all, T lymphoma cell lines and from normal thymic tissue. Only 1 of 30 other lymphoma cell lines was found to contain an elevated level of such a tyrosine protein kinase. An activity that phosphorylated p56 in vitro was not detectable in the cells of other hematopoietic lineages. Anti-peptide antibodies reactive with the site of in vitro tyrosine phosphorylation of p56 allowed us to determine that the apparent abundance of the p56 polypeptide parallels closely the level of the tyrosine protein kinase activity in the cell lines examined. This suggests that p56 is the protein kinase responsible for the elevated tyrosine protein kinase activity in LSTRA cells and that the phosphorylation of p56 observed in vitro results from autophosphorylation. Two-dimensional tryptic peptide mapping revealed that p56 is distinct from the proteins encoded by the cellular genes which are the progenitors of retroviral tyrosine protein kinases, src, yes, fgr, abl, fes, and ros. Additionally, none of these proto-oncogenes was found to be transcribed at elevated levels in LSTRA or Thy19 cells. Like the catalytic subunit of the cyclic AMP-dependent protein kinase, the cellular and viral forms of p60src, and the protein phosphatase calcineurin B, p56 contains covalently bound fatty acid.

Adenosine Triphosphate↗
PubMed1984

The effects of antirheumatic drugs on the production of collagenase and tissue inhibitor of metalloproteinases (TIMP) by stimulated rabbit articular chrondrocytes.

Conditioned medium from human peripheral blood mononuclear cells stimulated with concanavalin A (50 micrograms/ml) was used to induce rabbit articular chondrocytes to produce collagenase. In passaged chondrocyte cultures sodium aurothiomalate (GSTM) (either 5 micrograms/ml or 100 micrograms/ml). D-penicillamine (100 micrograms/ml) and dexamethasone (either 100 nM or 200 nM) did not reduce collagenase levels. Chloroquine (0.5 micrograms/ml) had a variable effect. Dexamethasone increased tissue inhibitor of metalloproteinases levels and also reduced collagenase levels in primary chondrocyte and cartilage fragment cultures. When the drugs were added to the mononuclear cells in culture, dexamethasone (10 nM), D-penicillamine (100 micrograms/ml), D-penicillamine (100 micrograms/ml) and copper sulphate (2 micrograms/ml) and chloroquine (5 micrograms/ml) reduced the activity of the conditioned medium when tested onchondrocytes. GSTM (100 micrograms/ml) and chloroquine (0.5 micrograms/ml) had no effect.

Anti-Inflammatory Agents↗
PubMed1983

Multiple proteins and subgenomic mRNAs may be derived from a single open reading frame on tobacco mosaic virus RNA.

It has previously been shown that messenger activity for a protein of Mr = ca. 30k exists in RNA fractions extracted from particles of either native or alkali stripped U1 TMV, or from cowpea strain TMV, that are smaller than full genomic length. Analysis of sucrose gradient fractions containing this activity reveals a number of slightly smaller template activities directing synthesis of proteins between 18.5k and 29k in size. All of these messenger activities, including that for the 30k protein, respond to cap analogues in anomalous ways. Discrete RNA species that include active mRNAs for these proteins can be demonstrated in the same fractions by labelling with preparations of vaccinia capping enzyme and [alpha-32P] GTP without prior beta-elimination. Detailed analysis of three of these proteins (of Mr's ca. 30k, 29k and 23k) by peptide mapping and translation of purified vaccinia-labelled RNA demonstrates that all three are unrelated to the large early TMV proteins, but are related to each other in such a way as to form a nested set with staggered N termini and identical C termini. mRNAs of chain lengths ca. 1900 and 1500 bases direct synthesis of the 30k and 23k proteins respectively, an mRNA of about 1850 bases directs both 29k and (perhaps because of cross-contamination) 30k synthesis. Initiation codons for the 29k and 23k proteins have been mapped at positions 4960-4962 and 5191-5193 respectively on TMV RNA. Since all three encapsidated templates have similar properties we conclude that either there is a family of 30k-related proteins with unusual mRNAs, or that none of these in vitro translation products are directed by physiological templates.

Amino Acid Sequence↗
PubMed1983

Identification and characterization of cellular targets for tyrosine protein kinases.

Protein kinases associated with the transforming proteins of a number of retroviruses are specific for tyrosine. Several proteins in cells transformed by these viruses are phosphorylated at tyrosine. We have now identified three unrelated abundant nonphosphorylated cellular proteins of 46,000, 39,000 and 28,000 daltons in chick embryo cells, which are the unphosphorylated forms of phosphotyrosine-containing proteins and thus are substrates for tyrosine protein kinases. By two-dimensional gel analysis, we have found that the 46,000-dalton protein exists in two unphosphorylated forms of which the more acidic is a minor species. This latter form is phosphorylated, chiefly at serine, in both normal and transformed cells, generating a yet more acidic species. In transformed but not normal cells, the major form is phosphorylated at tyrosine and serine, yielding a fourth isoelectric variant. The 46,000-dalton unphosphorylated protein has been partially purified, and antiserum to it recognizes all four isoelectric variants of the protein. The 39,000-dalton protein has two unphosphorylated forms of which the more acidic is a minor species. The major form is phosphorylated at tyrosine and serine in transformed cells only. The 39,000-dalton unphosphorylated protein has been partially purified, and antiserum raised to it recognizes all three isoelectric variants. The 28,000-dalton protein has a single phosphorylated form which contains serine in normal cells, but both serine and tyrosine in transformed cells.

Animals↗
PubMed1983

Spinal fractures complicating ankylosing spondylitis. A long-term followup study.

Twenty-two spinal fractures in 20 patients with chronic ankylosing spondylitis are reported. Nineteen fractures occurred in the cervical region. Fourteen of the fractures were caused by minor falls, 3 by falls down steps, 4 by motor vehicle accidents, and 1 by cardiopulmonary resuscitation. Long-term followup (mean 3.2 years) of 9 fractures diagnosed early and managed conservatively showed bony union of all fractures. No patient deteriorated neurologically and 3 patients made major recovery. Long-term followup is also reported on 6 patients in whom the diagnosis was delayed. The difficulties in diagnosis and management are discussed.

Aged↗