Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.23.15 (renin)
 35,795 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat gene for renin-binding protein (RnBP) was shown to be expressed in the kidney, adrenal gland, brain, lung, spleen, ovary, testis, and heart. On sodium depletion and captopril administration, the rat showed a marked increase in the adrenal RnBP mRNA level and a slight decrease in the kidney RnBP mRNA level. In two-kidney, one clip hypertensive rats, the RnBP mRNA levels of the clipped and contralateral kidneys were unchanged and also its adrenal mRNA level was maintained at the control level. The recombinant rat RnBP was synthesized in Escherichia coli cells and purified to apparent homogeneity. The RnBP existed as a homodimer and formed a heterodimer with rat renin to inhibit renin activity extensively. Intravenous injection of the RnBP into rats resulted in a rapid and strong inhibition of plasma renin activity, which persisted at least for 2 h. These results suggest that the expression of RnBP gene in the kidney and adrenal gland is regulated independently, and the function of RnBP is related to electrolyte homeostasis, probably through the interaction with renin.
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PMID:Tissue-specific regulation of renin-binding protein gene expression in rats. 140 Feb 60

To investigate the role of renin-binding protein (RnBP) in renin metabolism, RnBP expression plasmid, which was constructed to express human RnBP under the control of mouse mammary tumor virus long terminal repeat, was transfected into mouse pituitary AtT-20 cells together with the expression plasmid encoding human renin. The transfectant secreted prorenin and active renin, whereas RnBP was expressed only in the presence of dexamethasone and without secretion into the medium. The secretion of active renin was stimulated by forskolin, and the stimulation was repressed by dexamethasone. The secretion of prorenin, however, was insensitive to forskolin irrespective of the presence or absence of dexamethasone. Moreover, the forskolin-stimulated release of active renin was hardly repressed by dexamethasone in AtT-20 cells transfected with the renin expression plasmid and a selectable plasmid pMAMneo. Coexistence of RnBP and renin mRNAs in human Wilms' tumor G-401 cells was shown by means of polymerase chain reaction of respective cDNAs from the cells. These results suggest that RnBP modulates the release of active renin in renin-producing cells.
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PMID:Modulation of active renin secretion by renin-binding protein (RnBP) in mouse pituitary AtT-20 cells transfected with human renin and RnBP cDNAs. 158 5

The presence of a leucine zipper motif was recognized in the deduced amino acid sequences of human and rat renin-binding proteins (RnBPs) on cloning and sequence analysis of the RnBP cDNAs. The in vitro synthesized RnBPs, with the respective cDNAs, formed heterodimers with porcine renin and homodimers. On comparison of these properties with those of porcine RnBP, the leucine zipper motif was suggested to be a functional domain common to animal RnBPs. In addition to the motif, a hydrophobic domain adjacent to the motif and 10 cysteine residues were also well conserved in the three RnBPs. Moreover, about 85% of their amino acid sequences were identical. The RnBP mRNAs were expressed in the kidneys as the same size of 1.5-kb and the genes are suggested to exist as single copies in the genomes. Despite the high similarities in genetic and molecular properties, the molecular weights of human and rat RnBPs were 43,000, which is 1,000 larger than that of porcine RnBP. The immunoreactivities of human and rat RnBPs toward anti-porcine RnBP antiserum were 88 and 8% that of porcine RnBP, respectively, and the affinities of the two RnBPs for porcine renin were remarkably less than that of porcine RnBP. Moreover, the human and rat RnBP homodimers were partly dissociated under the conditions under which porcine RnBP existed as a dimer. These results indicate distinct differences in the molecular properties among the three RnBPs, in spite of their being highly similar structurally and functionally.
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PMID:Genetic and molecular properties of human and rat renin-binding proteins with reference to the function of the leucine zipper motif. 172 10

An apparent leucine zipper motif was recognized in the predicted amino acid sequence of porcine kidney renin-binding protein (RnBP) by analysis of the nucleotide sequence of a cDNA encoding the protein (Inoue, H., Fukui, K., Takahashi, S., and Miyake, Y. (1990) J. Biol. Chem. 265, 6556-6561). To evaluate the role of this motif in the formation of an RnBP-renin heterodimer and an RnBP homodimer, a porcine mutant cDNA involving Leu185----Asp and Leu192----Asp substitutions was constructed and expressed in vitro and in Xenopus oocytes. The mutant protein neither binds to renin nor forms the homodimer. The results strongly suggest that the leucine zipper motif in the RnBP molecule mediates the formation of both the RnBP-renin heterodimer and the RnBP homodimer observed previously. The existence of the motif should facilitate elucidation of the role of RnBP in renin metabolism.
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PMID:Leucine zipper motif in porcine renin-binding protein (RnBP) and its relationship to the formation of an RnBP-renin heterodimer and an RnBP homodimer. 205 Jun 86

A complementary DNA encoding a renin-binding protein (RnBP) has been isolated from a porcine kidney cDNA library by immunological screening of in vitro translation products from the cDNAs. Analysis of the nucleotide sequence of the clone revealed a 1,342-nucleotide sequence with a 5'-terminal untranslated region of 52 nucleotides, an open reading frame of 1,206 nucleotides that encodes 402 amino acids, and a 3'-terminal untranslated region of 84 nucleotides that contains the polyadenylation signal sequence, AATAAA. The predicted amino acid sequence contains no hydrophobic amino-terminal sequence and does not show significant homology to those of other identified proteins. The in vitro translated RnBP was found to have the same molecular weight, 42,000, as that of the purified RnBP from porcine kidney on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and it formed a complex with renin purified from porcine kidney, which indicates that the cDNA encodes a functional RnBP without a propeptide sequence. The RnBP cDNA probe hybridized to a 1.5-kilobase mRNA in kidney, liver, adrenal, and pituitary glands, the amount being much greater in kidney than in the other tissues. Southern blot analysis showed the presence of a unique gene for RnBP in the porcine genome.
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PMID:Molecular cloning and sequence analysis of a cDNA encoding a porcine kidney renin-binding protein. 218 20

A high-molecular-weight renin (HMWR) was detected in the plasma (molecular weight 50,600) and renal cortical homogenate (molecular weight 57,000) of 25-week-old male stroke-prone spontaneously hypertensive rats (SHRSP), in contrast to the renin with a molecular weight of 38,000 in normotensive Wistar Kyoto rats (WKY) and 5-week-old SHRSP. However, renin granules contained only the renin with a molecular weight of 38,000, indicating that the renal HMWR is not a native form but is probably a renin/renin-binding protein complex. Such HMWR was not produced when the renal cortex was homogenized with an equal amount of renal cortex of WKY. Further, the HMWR of the aged SHRSP was converted into the 38,000-dalton renin, when incubated with the extract of renal cortex of WKY. Thus, the existence of a renal cortical substance that converts the renal HMWR into the 38,000-dalton renin was evidenced. This substance was fractionated with DEAE-cellulose and was characterized as a putative SH enzyme. We conclude that a deficiency in the HMWR-converting substance may be attributed to the unusual formation of HMWR in the aged SHRSP.
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PMID:Renal high-molecular-weight renin: unusual formation in the aged stroke-prone spontaneously hypertensive rats. 352 65

Hog renal renin-binding protein could bind homologous and non-homologous renin but could not bind human renal renin. Renin-binding protein was only detected in the kidney and pituitary in which renin is found in relatively high concentration. The renal binding protein had no interaction with renal acid proteases nor with extrarenal renins obtained from pituitary and submaxillary glands, indicating that the binding is specific for renal renin. Subcellular localization of the binding protein was studied using rat kidney by differential and density gradient centrifugation. Most renin-binding protein was recovered in the cytosol fraction and was not associated with sedimentable subcellular organelles. A renin-secreting tumor (Juxtaglomerular cell tumor) in human kidney produced not only renin but also renin-binding protein in a very large quantity.
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PMID:Properties of renin-binding protein. 675 82

1. A completely inactive renin was isolated from hog kidney extract by affinity chromatography on pepstatin-aminohexyl-Sepharose and on an Affi-Gel Blue column. 2. This inactive renin had a molecular weight of 43 000 +/- 1500 as determined by gel filtration on Ultrogel AcA 44. Upon activation with trypsin, its molecular weight fell to 41 000 +/- 1400. 3. The inactive renin lacked the ability to bind renin-binding substance whereas trypsin-activated renin was able to bind the renin-binding protein and to form high-molecular-weight renin. 4. Chymotrypsin as well as trypsin could activate the inactive renin although less effectively. 5. The active renins generated from the inactive renin by the action of different proteolytic enzymes differed in their net charge, reflecting the specificities of the proteases used; the isoelectric points of the native, the trypsin-activated and the chymotrypsin-activated forms of renin occurred at pH 5.3, 5.1 and 4.8 respectively.
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PMID:Renin precursor and its activation mechanism in hog kidney. 700 24

Renin-binding protein (RBP) in hog kidney was characterized and identified as a renin inhibitor. The molecular weight (Mr) of rBP is 56,000 when estimated by gel filtration. Its isoelectric point is 4.9. Upon binding to renin, it forms a renin.RBP complex with Mr = 113,000 as revealed by sedimentation equilibrium using an air-driven ultracentrifuge (Airfuge). The renin.RBP complex, formed by incubating hog kidney extract at 37 degrees C, is inactive when assayed with little dilution. On extensive dilution, however, this complex dissociates and acquires renin activity. The equilibrium between renin and renin.RBP complex and the equilibration rate were also studied by high performance liquid chromatographic gel filtration. The equilibrium was shifted to the complex, suggesting that RBP is present in an excess of renin in the kidney. The complex was shown to dissociate during the gel filtration due to rapid equilibration. Therefore, the elution position of the complex varied depending on flow rates, thereby making it difficult to determine the Mr of the complex by gel filtration. The renin.RBP complex is unlikely to occur in the normal kidney because renin and RBP are localized in the granule and cytosol fractions, respectively. RBP may provide security against accidental rupture of renin granules under abnormal circumstances.
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PMID:A 56,000-dalton renin-binding protein in hog kidney is an endogenous renin inhibitor. 702 49

A high-performance liquid chromatograph equipped with the newly developed gel, TSK G3000SW, was used to study the interaction between renin and renin-binding protein (RBP). Previously, the interaction could only be demonstrated after overnight gel chromatography in the presence of a non-physiological sulfhydryl reagent. However, this new high-speed gel chromatography provided a clear separation of renin and renin--RBP complex within 40 min. It also demonstrated that the renin--RBP complex was formed at 37 degrees C in the absence of sulfhydryl reagent. Theses results indicate that the binding protein may play an important role in blood pressure regulation.
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PMID:Demonstration of the formation of renin and renin-binding protein complex using high-performance liquid chromatography. 702 69


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