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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
31
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pubmed:dateCreated |
1995-9-7
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pubmed:abstractText |
Polypeptide hormones and neuropeptides are initially synthesized as precursors possessing one or several domains that constitute the propeptide. Previous work from our laboratory demonstrated that expression of anglerfish prosomatostatin-I (proSRIF-I) in rat anterior pituitary GH3 cells resulted in efficient and accurate cleavage of the prohormone to generate the mature 14-amino acid peptide, SRIF-I. We also implicated the propeptide in mediating intracellular sorting to the trans Golgi network where proteolytic processing is initiated. In contrast, expression of a second form of the precursor, proSRIF-II in GH3 cells resulted in its intracellular degradation in an acidic, post-trans Golgi network compartment, most probably lysosomes. To further investigate the positive sorting signal present in proSRIF-I, we constructed a chimera comprising the signal peptide and proregion of SRIF-I fused to proSRIF-II and expressed the cDNA in GH3 cells. Here we demonstrate that the propeptide of SRIF-I rescued proSRIF-II from intracellular degradation quantitatively and diverted it to secretory vesicles. Furthermore, the chimera was processed to SRIF-28, an amino-terminally extended form of the hormone that is the physiological cleavage product of proSRIF-II processing in vivo. Most significantly, the SRIF-I propeptide functioned only in cis as part of the fusion protein and not in trans when expressed as a separate polypeptide. These data suggest that the SRIF-I propeptide may possess a sorting signal for sequestration into the secretory pathway rather than functioning as an intramolecular chaperone to promote protein folding.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Somatostatin,
http://linkedlifedata.com/resource/pubmed/chemical/prosomatostatin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18598-605
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7629190-Amino Acid Sequence,
pubmed-meshheading:7629190-Animals,
pubmed-meshheading:7629190-Base Sequence,
pubmed-meshheading:7629190-Chromatography, High Pressure Liquid,
pubmed-meshheading:7629190-Fishes,
pubmed-meshheading:7629190-Fluorescent Antibody Technique,
pubmed-meshheading:7629190-Hydrogen-Ion Concentration,
pubmed-meshheading:7629190-Molecular Sequence Data,
pubmed-meshheading:7629190-Peptide Fragments,
pubmed-meshheading:7629190-Precipitin Tests,
pubmed-meshheading:7629190-Protein Precursors,
pubmed-meshheading:7629190-Protein Processing, Post-Translational,
pubmed-meshheading:7629190-Protein Sorting Signals,
pubmed-meshheading:7629190-Recombinant Fusion Proteins,
pubmed-meshheading:7629190-Sequence Analysis,
pubmed-meshheading:7629190-Somatostatin
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pubmed:year |
1995
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pubmed:articleTitle |
The propeptide of anglerfish preprosomatostatin-I rescues prosomatostatin-II from intracellular degradation.
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pubmed:affiliation |
Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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