id:"swepub:oai:lup.lub.lu.se:9a8c916b-3cad-4b0d-9f9d-65ea8859893d"
Search: id:"swepub:oai:lup.lub.lu.se:9a8c916b-3cad-4b0d-9f9d-65ea8859893d" > Structural determin...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 04110naa a2200385 4500 | |
| 001 | oai:lup.lub.lu.se:9a8c916b-3cad-4b0d-9f9d-65ea8859893d | |
| 003 | SwePub | |
| 008 | 171019s2017 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://lup.lub.lu.se/record/9a8c916b-3cad-4b0d-9f9d-65ea8859893d2 URI |
| 024 | 7 | a https://doi.org/10.1016/j.bbadis.2017.09.0012 DOI |
| 040 | a (SwePub)lu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Del Giudice, Ritau Lund University,Lunds universitet,Medicinsk proteinvetenskap,Forskargrupper vid Lunds universitet,Medical Protein Science,Lund University Research Groups4 aut0 (Swepub:lu)ri8502de |
| 245 | 1 0 | a Structural determinants in ApoA-I amyloidogenic variants explain improved cholesterol metabolism despite low HDL levels |
| 264 | 1 | b Elsevier BV,c 2017 |
| 300 | a 11 s. | |
| 520 | a Twenty Apolipoprotein A-I (ApoA-I) variants are responsible for a systemic hereditary amyloidosis in which protein fibrils can accumulate in different organs, leading to their failure. Several ApoA-I amyloidogenic mutations are also associated with hypoalphalipoproteinemia, low ApoA-I and high-density lipoprotein (HDL)-cholesterol plasma levels; however, subjects affected by ApoA-I-related amyloidosis do not show a higher risk of cardiovascular diseases (CVD). The structural features, the lipid binding properties and the functionality of four ApoA-I amyloidogenic variants were therefore inspected in order to clarify the paradox observed in the clinical phenotype of the affected subjects. Our results show that ApoA-I amyloidogenic variants are characterized by a different oligomerization pattern and that the position of the mutation in the ApoA-I sequence affects the molecular structure of the formed HDL particles. Although lipidation increases ApoA-I proteins stability, all the amyloidogenic variants analyzed show a lower affinity for lipids, both in vitro and in ex vivo mouse serum. Interestingly, the lower efficiency at forming HDL particles is compensated by a higher efficiency at catalysing cholesterol efflux from macrophages. The decreased affinity of ApoA-I amyloidogenic variants for lipids, together with the increased efficiency in the cholesterol efflux process, could explain why, despite the unfavourable lipid profile, patients affected by ApoA-I related amyloidosis do not show a higher CVD risk. | |
| 650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinsk bioteknologi0 (SwePub)3042 hsv//swe |
| 650 | 7 | a MEDICAL AND HEALTH SCIENCESx Medical Biotechnology0 (SwePub)3042 hsv//eng |
| 700 | 1 | a Domingo-Espín, Joanu Lund University,Lunds universitet,Medicinsk proteinvetenskap,Forskargrupper vid Lunds universitet,Medical Protein Science,Lund University Research Groups4 aut0 (Swepub:lu)med-jdg |
| 700 | 1 | a Iacobucci, Ilariau University of Naples Federico II4 aut |
| 700 | 1 | a Nilsson, Oktawiau Lund University,Lunds universitet,Medicinsk proteinvetenskap,Forskargrupper vid Lunds universitet,Medical Protein Science,Lund University Research Groups4 aut0 (Swepub:lu)med-owi |
| 700 | 1 | a Monti, Maria Cristinau University of Naples Federico II4 aut |
| 700 | 1 | a Monti, Daria Mariau University of Naples Federico II4 aut |
| 700 | 1 | a Lagerstedt, Jens Ou Lund University,Lunds universitet,Medicinsk proteinvetenskap,Forskargrupper vid Lunds universitet,Medical Protein Science,Lund University Research Groups4 aut0 (Swepub:lu)med-jls |
| 710 | 2 | a Medicinsk proteinvetenskapb Forskargrupper vid Lunds universitet4 org |
| 773 | 0 | t Biochimica et Biophysica Actad : Elsevier BVg 1863:12, s. 3038-3048q 1863:12<3038-3048x 0006-3002 |
| 773 | 0 | t Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseased : Elsevier BVg 1863:12, s. 3038-3048q 1863:12<3038-3048x 0925-4439 |
| 856 | 4 | u http://dx.doi.org/10.1016/j.bbadis.2017.09.001y FULLTEXT |
| 856 | 4 | u https://doi.org/10.1016/j.bbadis.2017.09.001 |
| 856 | 4 8 | u https://lup.lub.lu.se/record/9a8c916b-3cad-4b0d-9f9d-65ea8859893d |
| 856 | 4 8 | u https://doi.org/10.1016/j.bbadis.2017.09.001 |
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