Pancreatic polypeptide immunoreactivity in medullary carcinoma of the thyroid: identification and characterisation by radioimmunoassay, immunocytochemistry and high performance liquid chromatography

Pancreatic polypeptide immunoreactivity has been identified in primary medullary carcinoma of thyroid using radioimmunoassay and immunocytochemistry and subsequently characterised by HPLC. Two region-specific PP antisera were used in the study; one C-terminal and one non-C-terminal. These antisera demonstrate variable cross-reactivity with the molecular species of PP identified in the tumours. The immunoreactive material in the tumours corresponded to human PP and not PYY or NPY on the basis of immunoreactivity and HPLC behaviour. It was identified in all patients with familial-type disease but not in the two sporadic cases examined. We propose that estimation of the PP content of medullary carcinoma of thyroid may be a useful means of differentiating familial and sporadic types.     

Activation of hypoxanthine/guanine phosphoribosyltransferase from yeast by divalent zinc and nickel ions

We have observed previously that the reactions catalyzed by hypoxanthine/guanine phosphoribosyltransferase (HGPRTase) are activated by Mg(II), Mn(II), and Co(II), and we have defined the mechanism by which these activations proceed [Biochemistry 22, 3419-3424 (1983)]. A more extensive survey of the kinds of metal ions that will activate the HGPRTase catalysis now has been completed through the use of an HPLC assay procedure. Although Fe(II) and Ca(II) are unable to activate this reaction, a significant activation was achieved with the addition of spectroscopically pure Zn(II) to the assay solution. In addition some IMP synthesis resulted from the addition of Ni(II) to the assay mixture. Both the Zn(II) and Ni(II) kinetic effects on HGPRTase over a limited metal ion concentration range have been analyzed through the use of curve-fitting exercises. These results, in addition to the similar pH profiles for the activations by Mg(II), Mn(II), Co(II), and Zn(II), suggest that all of these metal ions activate the HGPRTase-catalyzed synthesis of IMP by way of the same mechanism [model II as defined by London and Steck, Biochemistry 8, 1767-1779 (1969)], during which two divalent ions bind to the HGPRTase active site per molecule of PRibPP.     

Plasmid-encoded lysostaphin endopeptidase gene of Staphylococcus simulans biovar staphylolyticus

A 12.2-kilobase (kb) BclI fragment containing the lysostaphin endopeptidase gene was cloned from Staphylococcus simulans biovar staphylolyticus into Escherichia coli. The gene was expressed in E. coli and the gene product apparently was secreted into the periplasmic space. The gene was localized to a 3.3-kb region of the cloned fragment and this region was shown to contain a staphylococcal promoter for the endopeptidase gene. By hybridization analysis, the endopeptidase gene was shown to reside on the largest of five plasmids in S. simulans biovar staphylolyticus. No additional copies of this gene were detected in the genome.     

Extensive loss of translational genes in the structurally dynamic mitochondrial genome of the angiosperm <Emphasis Type="Italic">Silene latifolia</Emphasis>

Background  

Mitochondrial gene loss and functional transfer to the nucleus is an ongoing process in many lineages of plants, resulting in substantial variation across species in mitochondrial gene content. The Caryophyllaceae represents one lineage that has experienced a particularly high rate of mitochondrial gene loss relative to other angiosperms.     

Non-canonical autophagy drives alternative ATG8 conjugation to phosphatidylserine

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Induction of HLA class II molecules on human T cells: relationship to immunoregulation and the pathogenesis of AIDS.

Human T cells express HLA class II molecules upon activation. The factors that regulate the induction of expression of these molecules are for the most part unknown. Here we report preliminary results indicating that tumor necrosis factor-alpha (TNF-alpha) regulates the induction of cell-surface HLA-DR, DO, and DP molecules in human T cells stimulated with PHA. In contrast, recombinant interferon-gamma (rIFN-gamma), recombinant interleukin-1 alpha (rIL-1 alpha), or rIL-4 appear to have no effect on class II expression. The role of class II molecules on activated T cells is discussed in relationship to immunoregulation and the progression of HIV infection. Three non-mutually exclusive hypotheses are discussed. In the first hypothesis, we consider the role of these class II molecules in antigen presentation of endogenously synthesized HIV envelope by CD4+ cells. The second is a clonal inactivation of virus-specific helper T cells that might occur as a consequence of a direct T cell to T cell interaction and a bypass of the "accessory signal" normally delivered by antigen-presenting cells such as macrophages. The third is a molecular mimicry between HIV envelope proteins and HLA class II molecules, which may lead to the development of autoimmunity against CD4+ T-cell-expressing class II molecules.     

Construction of a sequenced Clostridium perfringens-Escherichia coli shuttle plasmid.

A new Clostridium perfringens-Escherichia coli shuttle plasmid has been constructed and its complete DNA sequence compiled. The vector, pJIR418, contains the replication regions from the C. perfringens replicon pIP404 and the E. coli vector pUC18. The multiple cloning site and lacZ' gene from pUC18 are also present, which means that X-gal screening can be used to select recombinants in E. coli. Both chloramphenicol and erythromycin resistance can be selected in C. perfringens and E. coli since pJIR418 carries the C. perfringens catP and ermBP genes. Insertional inactivation of either the catP or ermBP genes can also be used to directly screen recombinants in both organisms. The versatility of pJIR418 and its applicability for the cloning of toxin genes from C. perfringens have been demonstrated by the manipulation of a cloned gene encoding the production of phospholipase C.     

The Escherichia coli SRP Receptor Forms a Homodimer at the Membrane

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