Lipoprotein assembly and function in an evolutionary perspective
Circulatory fat transport in animals relies on members of the large lipid transfer protein (LLTP) superfamily, including mammalian apolipoprotein B (apoB) and insect apolipophorin II/I (apoLp-II/I). ApoB and apoLp-II/I, constituting the structural (non-exchangeable) basis for the assembly of various...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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De Gruyter
2010-08-01
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| Series: | Biomolecular Concepts |
| Subjects: | |
| Online Access: | https://doi.org/10.1515/bmc.2010.012 |
| _version_ | 1819135619034513408 |
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| author | Van der Horst Dick J. Rodenburg Kees W. |
| author_facet | Van der Horst Dick J. Rodenburg Kees W. |
| author_sort | Van der Horst Dick J. |
| collection | DOAJ |
| description | Circulatory fat transport in animals relies on members of the large lipid transfer protein (LLTP) superfamily, including mammalian apolipoprotein B (apoB) and insect apolipophorin II/I (apoLp-II/I). ApoB and apoLp-II/I, constituting the structural (non-exchangeable) basis for the assembly of various lipoproteins, acquire lipids through microsomal triglyceride-transfer protein, another LLTP family member, and bind them by means of amphipathic α-helical and β-sheet structural motifs. Comparative research reveals that LLTPs evolved from the earliest animals and highlights the structural adaptations in these lipid-binding proteins. Thus, in contrast to apoB, apoLp-II/I is cleaved post-translationally by a furin, resulting in the appearance of two non-exchangeable apolipoproteins in the single circulatory lipoprotein in insects, high-density lipophorin (HDLp). The remarkable structural similarities between mammalian and insect lipoproteins notwithstanding important functional differences relate to the mechanism of lipid delivery. Whereas in mammals, partial delipidation of apoB-containing lipoproteins eventually results in endocytic uptake of their remnants, mediated by members of the low-density lipoprotein receptor (LDLR) family, and degradation in lysosomes, insect HDLp functions as a reusable lipid shuttle capable of alternate unloading and reloading of lipid. Also, during muscular efforts (flight activity), an HDLp-based lipoprotein shuttle provides for the transport of lipid for energy generation. Although a lipophorin receptor – a homolog of LDLR – was identified that mediates endocytic uptake of HDLp during specific developmental periods, the endocytosed lipoprotein appears to be recycled in a transferrin-like manner. These data highlight that the functional adaptations in the lipoprotein lipid carriers in mammals and insects also emerge with regard to the functioning of their cognate receptors. |
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| format | Article |
| id | doaj.art-a4ac28a16c0946f1a6a00700a7fa8860 |
| institution | Directory Open Access Journal |
| issn | 1868-5021 1868-503X |
| language | English |
| last_indexed | 2024-12-22T10:21:57Z |
| publishDate | 2010-08-01 |
| publisher | De Gruyter |
| record_format | Article |
| series | Biomolecular Concepts |
| spelling | doaj.art-a4ac28a16c0946f1a6a00700a7fa88602022-12-21T18:29:37ZengDe GruyterBiomolecular Concepts1868-50211868-503X2010-08-011216518310.1515/bmc.2010.012Lipoprotein assembly and function in an evolutionary perspectiveVan der Horst Dick J.0Rodenburg Kees W.1Division of Endocrinology and Metabolism, Department of Biology and Institute of Biomembranes, 8 Padualaan, 3584 CH, Utrecht University, Utrecht, The NetherlandsDivision of Endocrinology and Metabolism, Department of Biology and Institute of Biomembranes, 8 Padualaan, 3584 CH, Utrecht University, Utrecht, The NetherlandsCirculatory fat transport in animals relies on members of the large lipid transfer protein (LLTP) superfamily, including mammalian apolipoprotein B (apoB) and insect apolipophorin II/I (apoLp-II/I). ApoB and apoLp-II/I, constituting the structural (non-exchangeable) basis for the assembly of various lipoproteins, acquire lipids through microsomal triglyceride-transfer protein, another LLTP family member, and bind them by means of amphipathic α-helical and β-sheet structural motifs. Comparative research reveals that LLTPs evolved from the earliest animals and highlights the structural adaptations in these lipid-binding proteins. Thus, in contrast to apoB, apoLp-II/I is cleaved post-translationally by a furin, resulting in the appearance of two non-exchangeable apolipoproteins in the single circulatory lipoprotein in insects, high-density lipophorin (HDLp). The remarkable structural similarities between mammalian and insect lipoproteins notwithstanding important functional differences relate to the mechanism of lipid delivery. Whereas in mammals, partial delipidation of apoB-containing lipoproteins eventually results in endocytic uptake of their remnants, mediated by members of the low-density lipoprotein receptor (LDLR) family, and degradation in lysosomes, insect HDLp functions as a reusable lipid shuttle capable of alternate unloading and reloading of lipid. Also, during muscular efforts (flight activity), an HDLp-based lipoprotein shuttle provides for the transport of lipid for energy generation. Although a lipophorin receptor – a homolog of LDLR – was identified that mediates endocytic uptake of HDLp during specific developmental periods, the endocytosed lipoprotein appears to be recycled in a transferrin-like manner. These data highlight that the functional adaptations in the lipoprotein lipid carriers in mammals and insects also emerge with regard to the functioning of their cognate receptors.https://doi.org/10.1515/bmc.2010.012apobapolipophorin iiidiacylglycerolinsect lipophorin receptorlow-density lipophorin (ldlp)ldl receptorlipophorinlipoprotein recyclinglarge lipid transfer (llt) domainmicrosomal triglyceride-transfer protein (mtp) |
| spellingShingle | Van der Horst Dick J. Rodenburg Kees W. Lipoprotein assembly and function in an evolutionary perspective Biomolecular Concepts apob apolipophorin iii diacylglycerol insect lipophorin receptor low-density lipophorin (ldlp) ldl receptor lipophorin lipoprotein recycling large lipid transfer (llt) domain microsomal triglyceride-transfer protein (mtp) |
| title | Lipoprotein assembly and function in an evolutionary perspective |
| title_full | Lipoprotein assembly and function in an evolutionary perspective |
| title_fullStr | Lipoprotein assembly and function in an evolutionary perspective |
| title_full_unstemmed | Lipoprotein assembly and function in an evolutionary perspective |
| title_short | Lipoprotein assembly and function in an evolutionary perspective |
| title_sort | lipoprotein assembly and function in an evolutionary perspective |
| topic | apob apolipophorin iii diacylglycerol insect lipophorin receptor low-density lipophorin (ldlp) ldl receptor lipophorin lipoprotein recycling large lipid transfer (llt) domain microsomal triglyceride-transfer protein (mtp) |
| url | https://doi.org/10.1515/bmc.2010.012 |
| work_keys_str_mv | AT vanderhorstdickj lipoproteinassemblyandfunctioninanevolutionaryperspective AT rodenburgkeesw lipoproteinassemblyandfunctioninanevolutionaryperspective |