Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
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Rat renin fused at the N-terminus with Sj26, a 26,000 Da glutathione S-transferase of Schistosoma japonicum, was expressed in Escherichia coli. The fusion protein was soluble and easily purified from crude bacterial lysates by affinity chromatography on immobilised glutathione. The fusion protein possessed no detectable renin activity. Antisera raised in rabbits against the fusion protein were specific for renin. These antisera did not bind soluble renin but bound immobilized renin. By immunoblotting, these antisera demonstrated rat renin to migrate on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as two broad bands of 33,000-34,000 and 35,000-37,000 Da. By immunocytochemistry of rat tissues, these antisera stained renin containing cells in the afferent arteriole of the glomerulus of the kidney, the zona glomerulosa of the adrenal and the corpus luteum of the ovary. However, apart from the afferent arteriole of the kidney, no immunoreactive renin was identified in blood vessels of the kidney, adrenal or ovary. These studies demonstrate that a recombinant renin fusion protein is a valuable alternative approach for the preparation of renin-specific antisera.
Mol Cell Endocrinol 1990 Oct 22
PMID:Production of rat renin fusion protein in Escherichia coli and the preparation of renin-specific antisera. 226 96

A Schistosoma mansoni cDNA library was constructed from the mRNA of adult worms in the expression vector lambda gt11 and screened with a rabbit antiserum raised against the 26-kDa S. mansoni glutathione S-transferase isoforms (Sm GST 26). Two clones were selected and the nucleotide sequences deduced. The predicted amino acid sequence, specified by these cDNAs, shows strong homology with a Schistosoma japonicum 26 kDa glutathione S-transferase and a lower level of homology with mammalian glutathione S-transferase class mu isoenzymes (EC 2.5.1.18). No significant homology score was found with a 28-kDa S. mansoni glutathione S-transferase (Sm GST 28). A study of the tissue distribution of the cloned Sm GST 26 by immunoelectron microscopy shows similarities to Sm GST 28 in that they are present in the tegument and in subtegumentary parenchymal cells. However, a major difference exists in the protonephridial region in which Sm GST 26 is present in the cytoplasmic digitations localized in the apical chamber delineated by the flame cell body, suggesting that Sm GST 26 may be actively excreted by adult worms.
Mol Biochem Parasitol 1990 Jun
PMID:Molecular cloning and tissue distribution of a 26-kilodalton Schistosoma mansoni glutathione S-transferase. 238 66

We have characterized actin gene expression in Schistosoma mansoni at the RNA and protein levels. Northern blot analyses showed two size classes of actin mRNA in eggs, cercariae and adult worms of both sexes, approximately 1 900 and 1 400 bases in length. A higher abundance of actin mRNA of both size classes was demonstrated in male worms than in eggs, cercariae, and females. Using a phalloidin-rhodamine conjugate, male worms were observed to contain more actin protein than females. Southern blot-hybridization indicated that the sexual differences in actin mRNA and protein levels were not related to some S. mansoni actin genes being sex linked. In addition, two other trematodes, Schistosoma japonicum and Fasciola hepatica and a cestode, Taenia pisiformis contained two classes of actin mRNA similar in size as those in S. mansoni. In contrast, a turbellarian, Dugesia tigrina contained only a single short actin message size class approximately 1 400 bases in length.
Mol Biochem Parasitol 1985 Dec
PMID:Stage and sex specific differences in actin gene expression in Schistosoma mansoni. 241 16

Constitutively expressed schistosome homologues of heat-shock protein Hsp70 elicit a dominant antibody response in humans infected with either Schistosoma japonicum or Schistosoma mansoni; in each case the parasite antigens are immunologically distinct and noncrossreactive. The antigenic site of the homologues is located near their carboxyl terminus where phylogenetic divergence between Hsp70 proteins is greatest. Nucleotide sequence comparison between these regions predicts very few amino acid differences between the schistosome protein and that of their human host. Thus strikingly limited diversity is sufficient to elicit a discriminatory antibody response to these parasite host-like antigens.
Mol Biochem Parasitol 1988 Jun
PMID:Schistosome heat-shock proteins are immunologically distinct host-like antigens. 245 5

A 43-kDa putative lipoprotein receptor (Sj43) of adult Schistosoma japonicum worms has been identified using ligand blotting techniques. Single and two dimensional electrophoretic analyses showed that Sj43 consisted of a single acidic polypeptide with multiple lipoprotein specificity. The molecule bound 125I-labelled low-density (apo-B), very low-density or high-density (apo-A and/or apo-C) lipoproteins from different mammalian hosts that are permissive to S. japonicum infection, but did not bind mouse apo-A containing lipoprotein. The binding of 125I-labelled lipoprotein to Sj43 could be inhibited by unlabelled human LDL, EDTA or Suramin, or by chemical modification of lipoprotein lysine or arginine residues. Sj43 was localised at the parasite's tegument and gut lining.
Mol Biochem Parasitol 1989 Jun 01
PMID:Identification of a multispecific lipoprotein receptor in adult Schistosoma japonicum by ligand blotting analyses. 254 94

Three of eleven clones isolated from a genomic expression library of Schistosoma japonicum DNA using chronically infected human sera also react with chronically infected mouse sera. Characterization of these three clones showed that they contain different members of the same gene family. One clone contains two members of the gene family approximately 2 kb apart and in opposite orientation to each other. DNA sequence homologies between pairs of genes range from 98% to 99.5%. Southern hybridization results indicate there are approximately 40 copies of these genes per haploid genome. Sera from mice immunized with purified fusion protein detected immunoreactive products in the central ganglion and ciliated epidermal cells of miracidia.
Mol Biochem Parasitol 1989 Mar 01
PMID:Characterization of a large gene family in Schistosoma japonicum that encodes an immunogenic miracidial antigen. 265 19

A library of randomly sheared Schistosoma japonicum genomic DNA fragments was constructed in the bacteriophage expression vector lambda gt11. A portion of the library was screened with sera collected from rabbits 8 weeks after they were infected with 1000 cercariae. Four clones whose recombinant gene products react with the rabbit sera were purified to homogeneity. Clone SjIR-12A was chosen for detailed study because of its very intense reaction with the rabbit sera. SjIR-12A was found to encode part of a 70 kDa protein (Sj70) that is present in both soluble egg antigen (SEA) and soluble worm antigen preparations (SWAP). Western blot analysis suggests that Sj70 is the only SWAP component that is strongly immunoreactive with the rabbit sera. Rabbit antibodies that react with the SjIR-12A fusion protein were immunoaffinity purified and used to localize immunoreactive product to the nervous tissue of male and female adult worms, the dorsal and lateral tegument of male adult worms, and in eggs to the miracidial tegument and the area between the eggshell and miracidium. Southern hybridization analysis suggests there are approximately four copies of the Sj70 gene per haploid genome.
Mol Biochem Parasitol 1987 Jul
PMID:Cloning of a Schistosoma japonicum gene encoding a major immunogen recognized by hyperinfected rabbits. 304 Dec 13

Isoelectric focusing was used to study the phenol oxidase isozymes in adult female worms of Schistosoma japonicum. More than one form of phenol oxidase has been demonstrated in extracts of female worms when incubated with 3,4-dihydroxyphenylalanine (DOPA), catechol or cresol as substrates. DOPA is the best substrate among all of them. The 5-6 bands of phenol oxidase exhibit pI values in the range of 6.0-7.5, the major band is at pI 6.0.
Mol Biochem Parasitol 1986 Jan
PMID:Isoenzymes of phenol oxidase in adult female Schistosoma japonicum. 308 53

Triton X-114 has been employed to isolate integral membrane proteins from Schistosoma japonicum and Schistosoma mansoni adult worms. Suitable marker molecules and antisera directed or raised against schistosome proteins partitioned by Triton X-114 extraction indicated that the phase separation and purification of integral membrane proteins had been successful and this fraction was free of contamination with aqueous (soluble) or secretory antigens. Two dimensional immunoblots further exemplified differences between antigens in the integral membrane protein extract and those of the aqueous fraction. Seven S. japonicum integral membrane proteins have been identified on immunoblots by serum from a hyperimmune and an infected rabbit and by sera from Philippine patients with a history of schistosomiasis japonica. Integral membrane proteins of S. mansoni and S. japonicum had surprisingly little conformity in the molecular weights and electrophoretic mobilities between the two species.
Mol Biochem Parasitol 1988 May
PMID:Immunoblotting analysis of the major integral membrane protein antigens of Schistosoma japonicum. 313 62

The NH2-terminal amino acid sequence of the Mr 26 000 glutathione S-transferase (EC 2.5.1.18) of Schistosoma japonicum (Sj26) has been deduced by RNA and protein sequence analysis. Using this information, a bacterial plasmid has been constructed that directs the synthesis of the entire Sj26 molecule in Escherichia coli. Recombinant Sj26 exhibits glutathione S-transferase activity and can be readily purified from bacteria in a one-step procedure under non-denaturing conditions. The availability of recombinant Sj26 in essentially unlimited quantities will aid its assessment as a candidate vaccine molecule in schistosomiasis and could eventually lead to the rational design of a drug targetted on schistosome glutathione S-transferases.
Mol Biochem Parasitol 1988 Jan 15
PMID:Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase. 327 28


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