Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02794 (ferritin)
 17,525 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ultrastructural distribution pattern and site density of alpha-methyldopa immunoglobin G (alpha-MD IgG) on the red cell membrane was observed and compared with that of anti-D IgG, with ferritin-conjugated rabbit anti-human IgG and [125I]anti-D. alpha-MD IgG binds to all common types of human red cells, both Rho (D) positive and negative, to give a random, aperiodic distribution pattern grossly indistinguishable from the red cell D receptor site pattern. alpha-MD IgG inhibits the binding of [125I]anti-D to D-positive red cells when the reaction is controlled with respect to total reaction volume, ionic strength, and the appropriate concentrations of the two IgG reactants. To determine if a alpha-MD IgG binds to the D-antigen receptor, D-positive red cells were sensitized with alpha-MD and [125I]anti-D IgG spearately and with both IgG preparations. The cell-bound radioactivity served to identify what proportion of the total ferritin-labeled IgG sites were due to anti-D. With nonsaturating concentrations of anti-D the number of IgG sites observed was equal to the sum of the sites found when the red cell was sensitized separately with alpha-MD and anti-D IgG. With saturating concentrations of anti-D there was a reduction in the expected number of IgG sites, indicating that alpha-MD IgG was excluded from binding. There was no comparable interaction of alpha-MD IgG and anti-D IgG when D-negative red cells were used. The results obtained indicate that alpha-MD IgG does not bind to the D antigen. The interaction between alpha-MD IgG and anti-D IgG for binding sites on the red cell membrane may be due to the close physical proximity of the two receptors, so as to produce steric hindrance in binding of the two IgG preparations when both are present. The alpha-MD IgG receptor appears to be a part of the Rh antigen complex that occurs in both D-positive and D-negative red cells and probably contains receptors for other types of warm-antibody immune hemolytic anemias.
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PMID:Ultrastructural mapping of methyldopa and anti-D IgG erythrocyte antigen receptors. 80 92

In order to find the immune-relevant factors responsible for the virus resistance in the WSSV-resistant shrimp, a suppression subtractive hybridization method was employed to identify differentially expressed genes and their expression profile in the hepatopancreas of the virus-resistant penaeid shrimp. Thirty five genes were identified from more than 400 clones, of which eight are found for the first time in penaeid shrimp. betaGBP is the most abundant gene in our subtractive library except hemocyanin. Lectin, ferritin, oxygenase and chitinase of the virus-resistant shrimp all showed up-regulation in expression compared with those of normal shrimp. In addition, Ranbp, Rho and Rab were found in the subtractive library. This is the first evidence indicating that small GTPases are involved in the signal transduction in shrimp defense response. Furthermore, a number of genes encoding apoptotic-related proteins and antioxidant enzymes were expressed at a higher level in the virus-resistant shrimp. In short, the high expression of immuno-related genes in response to the virus infection and the involvement of small GTPases in the antiviral response provide a new insight for further study in the crustacean innate immunity.
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PMID:Differential gene expression profile in hepatopancreas of WSSV-resistant shrimp (Penaeus japonicus) by suppression subtractive hybridization. 1545 Jul 50

The purple sea urchin has a complex immune system that is likely mediated by gene expression in coelomocytes (blood cells). A broad array of potential immune receptors and immune response proteins has been deduced from their gene models. Here we use shotgun mass spectrometry to describe 307 proteins with possible immune function in sea urchins including proteins involved in the complement pathway and numerous SRCRs. The relative abundance of dual oxidase 1, ceruloplasmin, ferritin and transferrin suggests the production of reactive oxygen species in coelomocytes and the sequestration of iron. Proteins such as selectin, cadherin, talin, galectin, amassin and the Von Willebrand factor may be involved in generating a strong clotting reaction. Cell signaling proteins include a guanine nucleotide binding protein, the Rho GDP dissociation factor, calcium storage molecules and a variety of lipoproteins. However, based on this dataset, the expression of TLRs, NLRs and fibrinogen domain containing proteins in coelomic fluid and coelomocytes could not be verified.
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PMID:Shotgun proteomics of coelomic fluid from the purple sea urchin, Strongylocentrotus purpuratus. 2335 16