The influence of glycosylation on the fate of renin expressed in <i>Xenopus</i> oocytes

Nakayama, Kazuhisa; Hatsuzawa, Kiyotaka; Kim, Won-Sin; Hashiba, Katsuko; Yoshino, Teruhiko; Hori, Hitoshi; Murakami, Kazuo

doi:10.1111/j.1432-1033.1990.tb19121.x

Cited by 10 publications

(3 citation statements)

References 27 publications

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“…Five potential N-linked glycosylation motifs were found, some of which may be glycosylated, mannose-6-phosphorylated, and may serve as lysosomal targeting signals [14,15].…”

Section: Isolation and Sequence Analysis Of A Full-length Mouse Kapmentioning

confidence: 99%

Molecular cloning of a novel mouse aspartic protease‐like protein that is expressed abundantly in the kidney

Mori¹,

Ogawa²,

Tamura³

et al. 1997

FEBS Letters

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By use of the signal sequence trap method, we isolated a cDNA encoding a novel aspartic protease-like protein from the mouse kidney, and termed it 'kidney-derived aspartic proteaselike protein (KAP).' The protein, a 419-amino-acid polypeptide with a 16-amino-acid signal sequence, had 47% identity with mouse cathepsin D, and its overall structure was closely related to known aspartic proteases. Northern blot analysis revealed that KAP mRNA is expressed at the highest level in the kidney, at a moderate level in the lung, and at low levels in the spleen and adipose tissue. In situ hybridization analysis demonstrated that the mRNA is expressed abundantly in the proximal straight tubule and slightly, but significantly, in the proximal convoluted tubule in the kidney. This intra-renal distribution differs distinctly from those of previously reported proteases such as cathepsins B, D, and H.

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“…Five potential N-linked glycosylation motifs were found, some of which may be glycosylated, mannose-6-phosphorylated, and may serve as lysosomal targeting signals [14,15].…”

Section: Isolation and Sequence Analysis Of A Full-length Mouse Kapmentioning

confidence: 99%

Molecular cloning of a novel mouse aspartic protease‐like protein that is expressed abundantly in the kidney

Mori¹,

Ogawa²,

Tamura³

et al. 1997

FEBS Letters

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“…The precipitates were then analyzed by SDSjPAGE followed by fluorography. When indicated, the precipitates were treated with endoglycosidase F under previously described conditions [42]. For analyses of regulated secretion of renin molecules, after the labeling period, cells were chased for 2 h with unlabeled medium and, finally, incubated for further 2 h in the presence or absence of 5 mM 8-bromoadenosine 3',5'-(cyc1ic)phosphate (Br8 CAMP).…”

Section: Radiolabeling and Immunoprecipitationmentioning

confidence: 99%

Sequence requirements for prohormone processing in mouse pituitary AtT‐20 cells

Nagahama

Nakayama

Murakami

1991

European Journal of Biochemistry

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Although cleavage of peptides at sites marked by paired basic amino acids is a common feature of prohormone processing, little is known about the properties of endoprotease(s) responsible for cleavage of the precursor. To examine the cleavage specificity of a processing endoprotease, we have altered the Lys-Arg cleavage site of human prorenin to Arg-Arg, Lys-Lys and Arg-Lys by site-directed mutagenesis, and expressed the native and mutated precursors in mouse pituitary AtT-20 cells which are known to process foreign prohormones, including prorenin, at paired basic sites during the regulated secretory process. All native and mutated human prorenins were sorted into the regulated secretory pathway. The mutated precursor with Arg-Arg instead of the Lys-Arg native pair was processed at about half the efficiency of the native one, while the Lys-Lys and Arg-Lys mutants were not processed. Rat prorenin, which naturally has a Lys-Lys pair, was not processed in the cells. In addition, mouse Ren2 prorenin, which has a Ser residue next to the Lys-Arg pair, but not mouse Renl prorenin, which has a Pro residue next to the pair, was processed. These results suggest that the Arg residue at the COOH side of the basic pair is essential for cleavage of prorenins by a processing enzyme during the regulated secretory process in AtT-20 cells, although the NH,-side Lys residue also plays a role. The results also demonstrate that the processing enzyme cannot cleave the Arg-Pro peptide bond.In endocrine and neuronal cells, many peptide hormones and neuropeptides are produced from larger, biologically inactive precursors through endoproteolytic cleavage, usually, at paired basic amino acids during intracellular transport [l -41. These cells have two secretory pathways. One is the regulated pathway by which mature hormones are produced by prohormone processing and are selectively targeted to secretory granules where they are stored until release is stimulated. The other is the constitutive pathway by which other proteins are secreted continuously without storage [5 -71. Lines of genetic evidence [8 -121 and studies using synthetic analogs [13 -151 and site-directed mutants [16 -201 of prohormones have suggested that paired basic amino acids are essential for prohormone processing. However, little is known about the specificity of endoprotease responsible for the precursor cleavage; precursor proteins often contain basic pairs which are never cleaved and tissue-specific use of certain pairs is often observed [2,4]. It has been recently reported by surveying various prohormone sequences that there is a hierarchy for the use of certain pairs of basic amino acids at the cleavage sites [17,21] : Lys-Arg (70%); Arg-Arg (1 5 % ) ; Lys-Lys (10%); Arg-Lys (5%). The data suggest that processing enzymes may have a preference for cleavage on the COOH side of Arg residues.Mouse pituitary AtT-20 cells, which endogenously produce adrenocorticotropin, P-endorphin, etc., through cleavage of a precursor, pro-opiomelanocortin, during the regulated secretor...

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“…Many kinds of renin/prorenin receptors have been reported (6)(7)(8). For example, the mannose-6-phosphate receptor, which has been the most extensively studied, mediated only uptake of renin and prorenin in the cell rather than showed other functions on the cell membrane (6).…”

Section: Introductionmentioning

confidence: 99%

Binding properties of rat prorenin and renin to the recombinant rat renin/prorenin receptor prepared by a baculovirus expression system

Nabi

Kageshima²,

Uddin³

et al. 2006

Int J Mol Med

119

144

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The rat recombinant renin/prorenin receptor (AB188298 in DDJB), which conjugated with FLAG epitope in its N-terminus, was expressed in a baculovirus expression system. The recombinant receptor, prepared from the cytoplasmic fraction of the insect cells, was identified by Western blotting using anti-FLAG antibody. Prorenin as well as renin bound to the receptor with different binding affinities. Their K d values were estimated at 8.0 and 20 nM, respectively. The amounts of prorenin and renin bound to the immobilized receptors were 1.0 and 0.2 pmole, respectively. The prorenin bound to the receptor had renin activity and the renin kept the activity at similar level to that before the binding. The K m of their complexes was the same at 3.3 μM when sheep angiotensinogen was used as the substrate. Their V max values were 5.5 and 10 nM•h-1 , respectively. The molecular activities of prorenin and renin bound to the receptor were 1.1 and 10 h-1 , respectively. From these findings, rat prorenin as well as renin was indicated to bind to the recombinant receptor and express the enzymatic activity in vitro.

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The influence of glycosylation on the fate of renin expressed in Xenopus oocytes

Cited by 10 publications

References 27 publications

Molecular cloning of a novel mouse aspartic protease‐like protein that is expressed abundantly in the kidney

Molecular cloning of a novel mouse aspartic protease‐like protein that is expressed abundantly in the kidney

Sequence requirements for prohormone processing in mouse pituitary AtT‐20 cells

Binding properties of rat prorenin and renin to the recombinant rat renin/prorenin receptor prepared by a baculovirus expression system

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