Cleavage Without Anchor Addition Accompanies the Processing of a Nascent Protein to Its Glycosylphosphatidylinositol-Anchored Form
Rough microsomal membranes from most mammalian cells, in the presence of a translation system, process nascent proteins with appropriate COOH-terminal signal peptides to their mature glycosylphosphatidylinositol (GPI)-linked forms. The present study, using preprominiplacental alkaline phosphatase as...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-02, Vol.92 (5), p.1550-1554 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 92 |
| creator | Maxwell, Stephen E. Ramalingam, Sandhya Gerber, Louise D. Udenfriend, Sidney |
| description | Rough microsomal membranes from most mammalian cells, in the presence of a translation system, process nascent proteins with appropriate COOH-terminal signal peptides to their mature glycosylphosphatidylinositol (GPI)-linked forms. The present study, using preprominiplacental alkaline phosphatase as substrate, shows that as much as 10% of the mature product is cleaved correctly but is not linked to GPI. Some of the factors that influence the relative proportions of GPI linked to free mini-placental alkaline phosphatase are the amounts of GPI in the cells and the amino acid substituent at the ω site of the nascent protein. A mechanism for explaining cleavage both with and without GPI addition is presented, which supports a transamidase type of enzyme as the catalyst. |
| doi_str_mv | 10.1073/pnas.92.5.1550 |
| format | Article |
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A mechanism for explaining cleavage both with and without GPI addition is presented, which supports a transamidase type of enzyme as the catalyst.</description><subject>Alkaline Phosphatase - metabolism</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Cell lines</subject><subject>Cellular biology</subject><subject>CHO Cells</subject><subject>COS cells</subject><subject>Cricetinae</subject><subject>Enzymes</subject><subject>Epitopes</subject><subject>Gels</subject><subject>Glycosylphosphatidylinositols - metabolism</subject><subject>GPI linked proteins</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>Membranes</subject><subject>Messenger RNA</subject><subject>Microsomes - metabolism</subject><subject>Molecular Weight</subject><subject>Peptides</subject><subject>Placenta - enzymology</subject><subject>Protein Biosynthesis</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Proteins - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkc-L1DAcxYso67h69aQQPHhrTdL8KngZBnddWNSD4jGkaTrNkElqki7O1b_clhmHUTwFvu_zvnlfXlG8RLBCkNfvRq9S1eCKVohS-KhYIdigkpEGPi5WEGJeCoLJ0-JZSjsIYUMFvCquuOACIrEqfm2cUQ9qa8B3m4cwZbD2eggRrLvOZhs8WGsd9qPy1iSQBwO-xKBNStZvQeiBAp9U0sbnZZ6N9SAHcJcTuHUHHdLBjUNI46Cy7Q7O-pBsDq48_mE6cBPi_nnxpFcumRen97r4dvPh6-Zjef_59m6zvi81ESSXPRFcUcoQ77qWYiaIUqTmDWdUQaYUM51mdUs05oY3tG2F6VuttNDYGFF39XXx_rh3nNr9DM-ho3JyjHav4kEGZeXfireD3IYHSTClfLa_Pdlj-DGZlOXezpc7p7wJU5KcI9qwpp7BN_-AuzBFP58mMUQ1FBwv26ojpGNIKZr-nANBuRQrl2JlgyWVS7Gz4fVl-jN-avIi3uL7o579sp-cy-Znvlj0X3DWXx31XcohngFcMyYwrH8DcaTEHQ</recordid><startdate>19950228</startdate><enddate>19950228</enddate><creator>Maxwell, Stephen E.</creator><creator>Ramalingam, Sandhya</creator><creator>Gerber, Louise D.</creator><creator>Udenfriend, Sidney</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950228</creationdate><title>Cleavage Without Anchor Addition Accompanies the Processing of a Nascent Protein to Its Glycosylphosphatidylinositol-Anchored Form</title><author>Maxwell, Stephen E. ; 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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1995-02, Vol.92 (5), p.1550-1554 |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Alkaline Phosphatase - metabolism Amino acids Animals Antibodies Cell lines Cellular biology CHO Cells COS cells Cricetinae Enzymes Epitopes Gels Glycosylphosphatidylinositols - metabolism GPI linked proteins HeLa Cells Humans In Vitro Techniques Membranes Messenger RNA Microsomes - metabolism Molecular Weight Peptides Placenta - enzymology Protein Biosynthesis Protein Processing, Post-Translational Proteins Proteins - metabolism |
| title | Cleavage Without Anchor Addition Accompanies the Processing of a Nascent Protein to Its Glycosylphosphatidylinositol-Anchored Form |
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