| The NH2-terminal proregion of peptidylglycine alpha-amidating monooxygenase facilitates the secretion of soluble proteins. | |
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MedLine Citation:
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PMID: 7760848 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A highly conserved ten amino acid proregion separates the peptidylglycine alpha-hydroxylating monooxygenase (PHM) domain of the bifunctional peptidylglycine alpha-amidating monooxygenase (PAM) protein from the NH2-terminal signal peptide; propeptides with amino acid sequences similar to the PAM proregion have been identified in other secreted proteins. In AtT-20 cells, but not in human embryonic kidney (hEK)-293 cells, an endogenous endoprotease acting at a site distal to the trans-Golgi network efficiently removes the propeptide from stably transfected monofunctional PHM (PHMs). We constructed a mutant PHM protein (delta ProPHMs) in which the proregion was deleted and the signal peptide joined directly to the monooxygenase domain. Newly synthesized, enzymatically active delta ProPHMs was secreted from both AtT-20 cells and hEK-293 cells more slowly than PHMs. In endocrine cells, the proregion was not required for storage in regulated secretory granules. We transferred the PAM proregion to prohormone convertase 2 (PC2), another soluble constituent of secretory granules, to determine whether the effect of the proregion were transferrable. In both AtT-20 cells and hEK-293 cells, the PAM/PC2 fusion molecule was able to exit the endoplasmic reticulum more rapidly than PC2. |
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Authors:
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R E Mains; S L Milgram; H T Keutmann; B A Eipper |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Molecular endocrinology (Baltimore, Md.) Volume: 9 ISSN: 0888-8809 ISO Abbreviation: Mol. Endocrinol. Publication Date: 1995 Jan |
Date Detail:
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Created Date: 1995-06-26 Completed Date: 1995-06-26 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 8801431 Medline TA: Mol Endocrinol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 3-13 Citation Subset: IM |
Affiliation:
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Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Biological Transport Cell Line Cytoplasmic Granules / enzymology Endoplasmic Reticulum / metabolism Enzyme Precursors / chemistry, metabolism* Humans Kidney / embryology Mice Mixed Function Oxygenases / chemistry, physiology* Molecular Sequence Data Multienzyme Complexes* Pituitary Neoplasms / pathology Pro-Opiomelanocortin / chemistry, metabolism Proprotein Convertase 2 Protein Processing, Post-Translational Protein Sorting Signals / chemistry Proteins / secretion* Recombinant Fusion Proteins / chemistry, metabolism Solubility Subtilisins / chemistry, metabolism Transfection Tumor Cells, Cultured |
| Grant Support | |
ID/Acronym/Agency:
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DK-32948/DK/NIDDK NIH HHS; GM-15293/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Enzyme Precursors; 0/Multienzyme Complexes; 0/Protein Sorting Signals; 0/Proteins; 0/Recombinant Fusion Proteins; 66796-54-1/Pro-Opiomelanocortin; EC 1.-/Mixed Function Oxygenases; EC 1.14.17.3/peptidylglycine monooxygenase; EC 3.4.21.-/Subtilisins; EC 3.4.21.94/Proprotein Convertase 2 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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