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  • 1
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    Toxicant-disease-environment interactions associated with suppression of immune system, growth, and reproduction (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-06-01
    Description: The effects of marginal malnourishment , infections, and environmental chemicals on growth and reproductive success in Swiss-Webster white mice and wild deer mice were studied with fractional factorial designs. Interaction effects were discovered. For example, malnourished mice were more sensitive to virus exposure and environmental chemicals (a plant growth regulator or polychlorinated biphenyls). Since several commercial plant growth regulators also appear to suppress the immune system, these results cast doubt on the adequacy of current toxicity testing procedures in which factors are studied individually and not in combination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Porter, W P -- Hinsdill, R -- Fairbrother, A -- Olson, L J -- Jaeger, J -- Yuill, T -- Bisgaard, S -- Hunter, W G -- Nolan, K -- 5-T32-ES07015/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1984 Jun 1;224(4652):1014-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6426058" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Wild ; Chlormequat/adverse effects ; Cyclophosphamide/adverse effects ; Encephalomyelitis, Venezuelan Equine/physiopathology ; Environmental Exposure ; Female ; Food Supply ; Growth/*drug effects ; Humans ; Immunity/*drug effects ; Mice ; Nutrition Disorders/physiopathology ; Peromyscus ; Polychlorinated Biphenyls/adverse effects ; Pregnancy ; Reproduction/*drug effects ; Water Supply
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Identification of a fourth mannose 6-phosphate binding site in the cation-independent mannose 6-phosphate receptor (2015)
    Oxford University Press
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    Publication Date: 2015-04-28
    Description: The 300 kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays an essential role in lysosome biogenesis by targeting ~60 different phosphomannosyl-containing acid hydrolases to the lysosome. This type I membrane glycoprotein has a large extracellular region comprised of 15 homologous domains. Two mannose 6-phosphate (M6P) binding sites have been mapped to domains 3 and 9, whereas domain 5 binds preferentially to the phosphodiester, M6P- N -acetylglucosamine (GlcNAc). A structure-based sequence alignment predicts that the C-terminal domain 15 contains three out of the four conserved residues identified as essential for carbohydrate recognition by domains 3, 5 and 9 of the CI-MPR, but lacks two cysteine residues that are predicted to form a disulfide bond. To determine whether domain 15 of the CI-MPR has lectin activity and to probe its carbohydrate-binding specificity, truncated forms of the CI-MPR were tested for binding to acid hydrolases with defined N -glycans in surface plasmon resonance analyses, and used to interrogate a phosphorylated glycan microarray. The results show that a construct encoding domains 14–15 binds both M6P and M6P-GlcNAc with similar affinity ( K d = 13 and 17 μM, respectively). Site-directed mutagenesis studies demonstrate the essential role of the conserved Tyr residue in domain 15 for phosphomannosyl binding. A structural model of domain 15 was generated that predicted an Arg residue to be in the binding pocket and mutagenesis studies confirmed its important role in carbohydrate binding. Together, these results show that the CI-MPR contains a fourth carbohydrate-recognition site capable of binding both phosphomonoesters and phosphodiesters.
    Print ISSN: 0959-6658
    Electronic ISSN: 1460-2423
    Topics: Biology , Medicine
    Published by Oxford University Press
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  • 3
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    The glycan-binding properties of the cation-independent mannose 6-phosphate receptor are evolutionary conserved in vertebrates (2012)
    Oxford University Press
    Details
    Publication Date: 2012-05-19
    Description: The 300-kDa cation-independent mannose 6-phosphate receptor (CI-MPR) plays an essential role in the biogenesis of lysosomes by delivering newly synthesized lysosomal enzymes from the trans Golgi network to the endosomal system. The CI-MPR is expressed in most eukaryotes, with Saccharomyces cerevisiae and Caenorhabditis elegans being notable exceptions. Although the repertoire of glycans recognized by the bovine receptor has been studied extensively, little is known concerning the ligand-binding properties of the CI-MPR from non-mammalian species. To assess the evolutionary conservation of the CI-MPR, surface plasmon resonance analyses using lysosomal enzymes with defined N -glycans were carried out to probe the glycan-binding specificity of the Danio rerio CI-MPR. The results demonstrate that the D. rerio CI-MPR harbors three glycan-binding sites that, like the bovine CI-MPR, map to domains 3, 5 and 9 of its 15-domain-containing extracytoplasmic region. Analyses on a phosphorylated glycan microarray further demonstrated the unique binding properties of each of the three sites and showed that, similar to the bovine CI-MPR, only domain 5 of the D. rerio CI-MPR is capable of recognizing Man-P-GlcNAc-containing glycans.
    Print ISSN: 0959-6658
    Electronic ISSN: 1460-2423
    Topics: Biology , Medicine
    Published by Oxford University Press
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  • 4
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    Strategies for carbohydrate recognition by the mannose 6-phosphate receptors (2008)
    Oxford University Press
    Details
    Publication Date: 2008-06-25
    Print ISSN: 0959-6658
    Electronic ISSN: 1460-2423
    Topics: Biology , Medicine
    Published by Oxford University Press
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