Complete amino acid sequence and maturation of the mouse submaxillary gland renin precursor

Panthier, Jean‐Jacques; Foote, Simon J.; Chambraud, Béatrice; Strosberg, A. Donny; Corvol, Pierre; Rougeon, François

doi:10.1038/298090a0

Cited by 187 publications

(101 citation statements)

References 23 publications

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“…cDNA cloning of SMG preprorenin-2 has been described [3]. The cDNA fragment was cloned into the PstI site of M13mp9 and the 5'poly(G) tail was deleted by in vitro mutagenesis.…”

Section: Site-directed Mutagenesis and Plusmid Constructionsmentioning

confidence: 99%

N‐linked glycosylation affects the processing of mouse submaxillary gland prorenin in transfected AtT20 cells

Ladenheim

Seidah

Rougeon

1991

European Journal of Biochemistry

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Paris, FranceMost mouse inbred strains carry two renin genes, Ren-I and Ren-2. Renin-2, the product of the Ren-2 gene, is highly expressed in the submaxillary gland. It is a renin isoenzyme 96% similar to kidney renin-1, but unglycosylated. In order to investigate if glycosylation of prorenin affects its processing and/or secretion we have introduced two potential N-linked glycosylation sites into preprorenin-2 cDNA using site-directed mutagenesis. Expression plasmids were derived from wild-type and mutant renin-2 cDNA and were transfected into AtT20 cells. Both transfected cells, expressing glycosylated or unglycosylated forms, secreted prorenin and renin by the constitutive and regulated pathways, respectively. Prorenin was correctly processed to active renin but the second maturation site was not cleaved in AtT20 cells. The comparison of glycosylated and unglycosylated renin expression showed a diminished secretion of glycosylated active renin. Prevention of glycosylation with tunicamycin resulted in an improved secretion of active renin. Moreover, the efficiency of the trypsin activation in vitro was reduced for glycosylated prorenin and it was restored when the activation was performed on mutant renin secreted from tunicamycin-treated cells. It is proposed that the bulky carbohydrates attached to prorenin constitute a steric hindrance to proteolysis by maturation enzymes.

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“…cDNA cloning of SMG preprorenin-2 has been described [3]. The cDNA fragment was cloned into the PstI site of M13mp9 and the 5'poly(G) tail was deleted by in vitro mutagenesis.…”

Section: Site-directed Mutagenesis and Plusmid Constructionsmentioning

confidence: 99%

N‐linked glycosylation affects the processing of mouse submaxillary gland prorenin in transfected AtT20 cells

Ladenheim

Seidah

Rougeon

1991

European Journal of Biochemistry

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show abstract

“…However, close inspection of the data in Fig. 4 revealed that the molecular weight of {he plasmid-encoded renin precursor (Mr== 40,000) is lower than the expected value (Mr == 43,000} from the sequence results of analysis 9 ) and the pulse-chase experiments. 13 ,14) There is a possibility that the renin precursor synthesized in E. coli might have undergone proteolytic breakdown.…”

Section: Construction and Expression Of The Preprorenin Genementioning

confidence: 99%

Synthesis of Enzymatically Active Mouse Submandibular Gland Renin inEscherichia coli

Masuda¹,

Nakano²,

Hirose³

et al. 1986

Agricultural and Biological Chemistry

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“…The messenger (m) RNA of the renin gene is translated into a protein preprorenin consisting of 401 amino acid residues (Imai et al 1983;Pratt et al 1983). In the endoplasmic reticulum a 20-amino-acid signal peptide is cleaved from preprorenin, leaving prorenin a glycosylated protein of 381 amino acids (Panthier et al 1982;Cantanzaro et al 1983;Galen et al 1984). Prorenin, which is enzymatically inactive, is packed into secretory granules at the Golgi apparatus; where it is further processed into active renin by the cleavage of a 46-amino-acid peptide from the N-terminus of the molecule.…”

Section: Processing Of Renin In Juxtaglomerular Cellsmentioning

confidence: 99%

“…The presence of renin has been demonstrated in a variety of tissues, including kidney, salivary glands, placenta, blood vessels, and various endocrine glands (Campbell 1987). Although renin obtained from these tissues, in particular from the submaxillary gland, has been important for the elucitation of the structure and intracellular processing of renin (Panthier et al 1982;Cantazaro et al 1983), so far only renal renin has proved important in the regulation of the RAAS. Therefore, unless otherwise indicated, only renal renin is considered in this review.…”

Section: Introductionmentioning

confidence: 99%

Cellular control of renin secretion

Kurtz

Wagner

Reviews of Physiology, Biochemistry and Pharmacology

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Complete amino acid sequence and maturation of the mouse submaxillary gland renin precursor

Cited by 187 publications

References 23 publications

N‐linked glycosylation affects the processing of mouse submaxillary gland prorenin in transfected AtT20 cells

N‐linked glycosylation affects the processing of mouse submaxillary gland prorenin in transfected AtT20 cells

Synthesis of Enzymatically Active Mouse Submandibular Gland Renin inEscherichia coli

Cellular control of renin secretion

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