Document Detail

The NH2-terminal proregion of peptidylglycine alpha-amidating monooxygenase facilitates the secretion of soluble proteins.
MedLine Citation:
PMID:  7760848     Owner:  NLM     Status:  MEDLINE    
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.
R E Mains; S L Milgram; H T Keutmann; B A Eipper
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular endocrinology (Baltimore, Md.)     Volume:  9     ISSN:  0888-8809     ISO Abbreviation:  Mol. Endocrinol.     Publication Date:  1995 Jan 
Date Detail:
Created Date:  1995-06-26     Completed Date:  1995-06-26     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8801431     Medline TA:  Mol Endocrinol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  3-13     Citation Subset:  IM    
Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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MeSH Terms
Amino Acid Sequence
Biological Transport
Cell Line
Cytoplasmic Granules / enzymology
Endoplasmic Reticulum / metabolism
Enzyme Precursors / chemistry,  metabolism*
Kidney / embryology
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
Subtilisins / chemistry,  metabolism
Tumor Cells, Cultured
Grant Support
Reg. No./Substance:
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 monooxygenase; EC 3.4.21.-/Subtilisins; EC Convertase 2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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