Heterologous Expression of Human Cholecystokinin in Saccharomyces cerevisiae

Rourke, Ian J.; Johnsen, Anders H.; Din, Nanni; Petersen, J.; Rehfeld, Jens F.

doi:10.1074/jbc.272.15.9720

Cited by 24 publications

(11 citation statements)

References 47 publications

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“…In the rat and human precursors, a single Lys residue is found upstream the sequence of 26RFa. Although an individual lysine is not regarded as a preferential cleavage site, a few regulatory peptides are actually processed at this site (28,29). The occurrence of an internal dibasic motif (Arg-Lys or Arg-Arg) within the frog, rat, and human 26RFa sequences suggests that the peptide could be further processed to generate the highly conserved C-terminal peptide (Lys)-Gly-Gly-Phe-Ser-Phe-Arg-Phe-NH 2 .…”

Section: Discussionmentioning

confidence: 99%

Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity

Chartrel

Dujardin

Anouar

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

186

308

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A neuropeptide was isolated from a frog brain extract by HPLC purification and characterized by mass spectrometry. This 26-aa neuropeptide, which belongs to the RFamide peptide family, was designated 26RFa, and its primary structure was established as VGTALGSLAEELNGYNRKKGGFSFRF-NH 2. Research in databases revealed the presence of sequences homologous to frog 26RFa in the human genome and in rat ESTs. On the basis of this sequence information, the cDNAs encoding the human and rat 26RFa precursors were cloned. The two preproteins show a similar organization, with the 26RFa sequence located in the C-terminal region of the precursor. Human preprotein (prepro)-26RFa encodes an additional putative RFamide peptide that is not found in the rat precursor. The primary structures of human, rat, and frog 26RFa exhibit Ϸ80% identity, and the C-terminal octapeptide has been fully conserved from amphibians to mammals. In situ hybridization histochemistry revealed that, in the rat brain, the 26RFa gene is exclusively expressed in the ventromedial hypothalamic nucleus and in the lateral hypothalamic area. 26RFa induced a dosedependent stimulation in cAMP production by rat pituitary cells in vitro and markedly increased food intake in mice. The conservation of the primary structure of 26RFa during vertebrate evolution, the discrete localization of the mRNA encoding its precursor in hypothalamic nuclei involved in the control of feeding behavior, and the observation that 26RFa possesses orexigenic properties indicate that this neuropeptide may play important biological functions.

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Section: Discussionmentioning

confidence: 99%

Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity

Chartrel

Dujardin

Anouar

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

186

308

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“…Carboxypeptidase Y and Kex1p were, either of them, involved in the degradation of the C-terminus of hirudin (16) and rLDTI (17). There is also evidence for a lysine-specific, yet uncharacterized endopeptidase, supposed to be involved in cleavage of human pro-CKK (18). In the case of hPTH, strain BJ2168 was chosen as a host because it is mutated in the carboxypeptidase Y gene in addition to defects in the genes encoding proteinase A and B.…”

Section: Aberrant Electrophoretic Mobility Of C-terminally Truncated mentioning

confidence: 99%

High-Level Production of Human Parathyroid Hormone (hPTH) by Induced Expression inSaccharomyces cerevisiae

Vad

Moe

Saga

et al. 1998

Protein Expression and Purification

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“…Trypsin-like, chymotrypsin-like and renin-like activities have been shown to be involved in prohormone processing. Of these, KEX-1 and -2 [56,57], PAM (peptidyl-glycine-h-amidating monooxygenase) [58] and PCE (prohormone processing enzyme) [59] are the most extensively characterized. Cathepsin A is active toward various naturally occurring bioactive peptides in vitro (table 2).…”

Section: Substrate Specificitymentioning

confidence: 99%

Cathepsin A/protective protein: an unusual lysosomal multifunctional protein

Hiraiwa¹

1999

Cellular and Molecular Life Sciences (CMLS)

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Cathepsin A/protective protein [3.4.16.5], carboxypeptidase A, is a lysosomal serine protease with structural homology to yeast (Saccharomyces cerevisiae) carboxypeptidase Y. Cathepsin A is a member of the alpha/beta hydrolase fold family and has been suggested to share a common ancestral relationship with other alpha/beta hydrolase fold enzymes, such as cholinesterases. Several lines of evidence indicate that cathepsin A is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities. Cathepsin A was recently identified in human platelets as deamidase. In vitro, it hydrolyzes a variety of bioactive peptide hormones including tachykinins, suggesting that extralysosomal cathepsin A plays a role in regulation of bioactive peptide functions. Recent reports emphasize the lysosomal protective function of cathepsin A rather than its protease function. The protective function of cathepsin A is distinct from its catalytic function. Human lysosomal beta-galactosidase and neuraminidase exist as a high molecular weight enzyme complex, in which there is a 54-kDa glycoprotein termed 'lysosomal protective protein'. Based on cell culture studies, protective protein was found to protect both beta-galactosidase and neuraminidase from intralysosomal proteolysis by forming a multienzyme complex and was shown to be deficient in patients with galactosialidosis, a combined deficiency of beta-galactosidase and neuraminidase. Molecular cloning and gene expression studies have disclosed that protective protein is cathepsin A. The cathepsin A precursor has the potential to restore both beta-galactosidase and neuraminidase activities in fibroblasts from patients with galactosialidosis. Cathepsin A knockout mice showed a phenotype similar to human galactosialidosis and the deficient phenotype found in the mutant mice was corrected by transplanting erythroid precursor cells overexpressing cathepsin A. Collectively, these findings demonstrate the significance of cathepsin A as a key molecule in the onset of galactosialidosis and also highlight the therapeutic potential of the cathepsin A precursor for patients with galactosialidosis.

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Heterologous Expression of Human Cholecystokinin in Saccharomyces cerevisiae

Abstract: Precursors of the human regulatory peptide cholecystokinin (CCK) have been expressed in

Cited by 24 publications

References 47 publications

Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity

Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity

High-Level Production of Human Parathyroid Hormone (hPTH) by Induced Expression inSaccharomyces cerevisiae

Cathepsin A/protective protein: an unusual lysosomal multifunctional protein

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