Synthesis, transport, and processing of apolipoproteins of high density lipoproteins
Cell biology methods have greatly influenced the elucidation of the biosynthetic pathways of apolipoproteins. In vitro and tissue culture systems allow the study, to a large extent, of the process of synthesis, intracellular processing, secretion, and extracellular processing of the major high densi...
| Main Author: | |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
1984-12-01
|
| Series: | Journal of Lipid Research |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S0022227520344369 |
| _version_ | 1818671898961117184 |
|---|---|
| author | W Stoffel |
| author_facet | W Stoffel |
| author_sort | W Stoffel |
| collection | DOAJ |
| description | Cell biology methods have greatly influenced the elucidation of the biosynthetic pathways of apolipoproteins. In vitro and tissue culture systems allow the study, to a large extent, of the process of synthesis, intracellular processing, secretion, and extracellular processing of the major high density lipoprotein apoproteins apoA-I and A-II and also of a minor component, apoA-IV. Whereas the latter apoprotein is equipped only with a signal sequence, the primary translation products of apoA-I and apoA-II carry N-terminal extensions of preprosequence of 24 amino acids for apoA-I and 23 amino acid residues for apoA-II. The pro-form of apoA-I characterized by a hexapeptide extension is completely stable intracellularly and is secreted as such. The pro-form is further processed by a serum protease specific for an unusual -Gln-Gln-Asp-Glu-sequence site. Pro-apoA-II, a pentapeptide sequence, is partially processed intracellularly to its mature form and secreted together with the residual pro-form. The cleavage site of pro-apoA-II is characterized by two basic amino acid residues Arg-Arg, present also in other known pro-proteins. The biological function of the N-terminal pro-sequences and details of their final processing by the serum protease(s) have yet to be established. |
| first_indexed | 2024-12-17T07:31:19Z |
| format | Article |
| id | doaj.art-f1ac39a22d204b2f8a66d5288005f7ed |
| institution | Directory Open Access Journal |
| issn | 0022-2275 |
| language | English |
| last_indexed | 2024-12-17T07:31:19Z |
| publishDate | 1984-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Lipid Research |
| spelling | doaj.art-f1ac39a22d204b2f8a66d5288005f7ed2022-12-21T21:58:29ZengElsevierJournal of Lipid Research0022-22751984-12-01251315861592Synthesis, transport, and processing of apolipoproteins of high density lipoproteinsW StoffelCell biology methods have greatly influenced the elucidation of the biosynthetic pathways of apolipoproteins. In vitro and tissue culture systems allow the study, to a large extent, of the process of synthesis, intracellular processing, secretion, and extracellular processing of the major high density lipoprotein apoproteins apoA-I and A-II and also of a minor component, apoA-IV. Whereas the latter apoprotein is equipped only with a signal sequence, the primary translation products of apoA-I and apoA-II carry N-terminal extensions of preprosequence of 24 amino acids for apoA-I and 23 amino acid residues for apoA-II. The pro-form of apoA-I characterized by a hexapeptide extension is completely stable intracellularly and is secreted as such. The pro-form is further processed by a serum protease specific for an unusual -Gln-Gln-Asp-Glu-sequence site. Pro-apoA-II, a pentapeptide sequence, is partially processed intracellularly to its mature form and secreted together with the residual pro-form. The cleavage site of pro-apoA-II is characterized by two basic amino acid residues Arg-Arg, present also in other known pro-proteins. The biological function of the N-terminal pro-sequences and details of their final processing by the serum protease(s) have yet to be established.http://www.sciencedirect.com/science/article/pii/S0022227520344369 |
| spellingShingle | W Stoffel Synthesis, transport, and processing of apolipoproteins of high density lipoproteins Journal of Lipid Research |
| title | Synthesis, transport, and processing of apolipoproteins of high density lipoproteins |
| title_full | Synthesis, transport, and processing of apolipoproteins of high density lipoproteins |
| title_fullStr | Synthesis, transport, and processing of apolipoproteins of high density lipoproteins |
| title_full_unstemmed | Synthesis, transport, and processing of apolipoproteins of high density lipoproteins |
| title_short | Synthesis, transport, and processing of apolipoproteins of high density lipoproteins |
| title_sort | synthesis transport and processing of apolipoproteins of high density lipoproteins |
| url | http://www.sciencedirect.com/science/article/pii/S0022227520344369 |
| work_keys_str_mv | AT wstoffel synthesistransportandprocessingofapolipoproteinsofhighdensitylipoproteins |