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Dyslipidemia
Published in Jahangir Moini, Matthew Adams, Anthony LoGalbo, Complications of Diabetes Mellitus, 2022
Jahangir Moini, Matthew Adams, Anthony LoGalbo
Very low-density lipoproteins (VLDL) are rich in triglycerides, and are produced by the liver. They are similar to chylomicrons in size, also varying based on the amount of triglyceride being carried. With increased triglyceride production in the liver, the secreted VLDL particles are larger. The IDL are VLDL remnants. Removal of triglycerides from VLDL is done by the adipose tissue and muscle tissue. Lipoprotein (α) is an LDL particle with apolipoprotein (α) attached to Apo B-100 with a disulfide bond. The apolipoproteins play a structural role, serve as ligands for lipoprotein receptors, regulate formation of lipoproteins, and are important activators or inhibitors of enzymes involved in lipoprotein metabolism. Insulin resistance and type 2 diabetes mellitus are related to plasma lipid and lipoprotein abnormalities, increasing the risk for cardiovascular disease.
Phytotherapeutic Potential For the Treatment of Alzheimer’s Disease
Published in Atanu Bhattacharjee, Akula Ramakrishna, Magisetty Obulesu, Phytomedicine and Alzheimer’s Disease, 2020
Muhammad Akram, Atanu Bhattacharjee, Naveed Munir, Naheed Akhter, Fozia Anjum, Abida Parveen, Samreen Gul Khan, Muhammad Daniyal, Muhammad Riaz, Fahad Said Khan, Rumaisa Ansari, Umme Laila
Apolipoprotein E is also a causative agent in the development of AD. Different form of apolipoprotein E are present, like apolipoproteins E2, 3, and 4. Glial cells of the brain, which are also called astrocytes, produce these proteins. The risk of developing AD is greater in the presence of higher apolipoprotein E4 concentrations (Aaronson, Van Den Eeden et al. 2017). If the level of this protein increases, then the probability of death is also increased (Harris, Brecht et al. 2003). AD is also associated with E693G mutations in a gene encoding an amyloid precursor protein (Nilsberth, Westlind-Danielsson et al. 2001). Furthermore, AD is caused by oxidative stress because, in this situation, demand by the brain for oxygen is increased (Butterfield and Lauderback 2002). AD is also associated with some pathogens like Chlamydia pneumoniae, which enter the brain tissue and damage brain cells (Harris, Brecht et al. 2003). AD is more common in females, smokers, obese people, patients with high blood pressure or a high level of cholesterol, whereas previous trauma, changes in sleep pattern, and Down syndrome can all increase the risk of AD (Simonson 2018).
Serum Amyloid a Gene Regulation
Published in Andrzej Mackiewicz, Irving Kushner, Heinz Baumann, Acute Phase Proteins, 2020
Patricia Woo, Mark R. Edbrooke, Jonathan Betts, Glenda Watson, Phillippa Francis
Serum amyloid A (SAA) is a group of closely related proteins coded for by a multigene family in many species, e.g., mice,1 Syrian hamster,2 mink,3 and dog4 as well as humans.5 Most of these proteins are apolipoproteins carried by the high density lipoprotein (HDL) fraction of plasma and are acute phase reactants. They respond to conditioned medium from stimulated monocytes or from recombinant cytokines such as interleukin 1 (IL-1), interleukin 6 (IL-6), and tumor necrosis factor-α (TNFα).
Amyloid nomenclature 2022: update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee
Published in Amyloid, 2022
Joel N. Buxbaum, Angela Dispenzieri, David S. Eisenberg, Marcus Fändrich, Giampaolo Merlini, Maria J. M. Saraiva, Yoshiki Sekijima, Per Westermark
Amyloid deposits not only contain the main amyloid fibril proteins but may also have components that appear to be present in most deposits. The most well studied are serum amyloid P-component (SAP) and heparan sulphate proteoglycans (HSPG), both of which seem to be important both for the stability of the fibrils and, at least for HSPG, in their genesis. There are other proteins regularly found attached to the fibril by uncertain mechanisms. They include among others, apolipoprotein A-IV and apolipoprotein E; with other components under continuing investigation. The presence of these proteins has been used in mass spectrometry as additional proof that the tissue extracted material contains amyloid. Therefore, these components have been designated as ‘amyloid signature proteins’ [6].
Low-density lipoprotein nanomedicines: mechanisms of targeting, biology, and theranostic potential
Published in Drug Delivery, 2021
Although lipid and protein contents of lipoproteins can be variable depending on species (e.g. human, animal), disease state, nutrition, and genetics (John Chapman, 1986; Levy et al., 2000; German et al., 2006; Hegele, 2009; Dron & Hegele, 2016), apolipoproteins are functionally classified as either water insoluble and non-exchangeable (ApoB family) or water soluble and exchangeable (ApoA, ApoC, and ApoE families) (Babin et al., 1997; Curtiss et al., 2006; Phillips, 2013). Whereas non-exchangeable apolipoproteins remain on the same lipoprotein particle from biosynthesis to degradation, exchangeable apolipoproteins (ApoA, ApoC and ApoE families of lipoproteins) are able to interact with a number of lipid-bearing structures and molecules (e.g. vesicles, membranes, and other lipoproteins) (Jonas & Phillips, 2008). Apolipoproteins also play a role in the synthesis of LDL and HDL, as their carrier proteins (ApoB and ApoA-I, respectively) are released from the liver in a complex with nascent vLDL or from the liver and intestine as lipid-free ApoA-1, respectively. ApoB and ApoA-I subsequently recruit lipids, triglycerides, and cholesterol, which are transported between peripheral tissues and the liver as part of the functional processes called forward and reverse cholesterol transport (Tall, 1998; Huang, Elvington, et al., 2015).
Novel emerging therapies in atherosclerosis targeting lipid metabolism
Published in Expert Opinion on Investigational Drugs, 2020
Manasvi Gupta, Colin Blumenthal, Subhankar Chatterjee, Dhrubajyoti Bandyopadhyay, Vardhmaan Jain, Carl J Lavie, Salim S. Virani, Kausik K Ray, Wilbert S Aronow, Raktim K Ghosh
Following an acute MI, the risk of secondary cardiovascular events remains high despite treatment, which is in part attributable to a sustained low levels of HDL levels despite reduced LDL-C levels. Studies have indicated that increasing the ability of HDL particles to remove cholesterol, defined in terms of CEC, is more beneficial than increasing the sheer level of HDL [67]. Human plasma-derived apolipoprotein A-I (ApoA1), which is a key component of HDL particles and responsible for the CEC, was first evaluated in the AEGIS-I (ApoA-I Event Reducing in Ischemic Syndromes I) trial. This dose-ranging phase 2b trial was designed to confirm the renal and hepatic safety in addition to efficacy in enhancing CEC [68]. The population was expanded in a subsequent trial to include patients with decreased renal function (eGFR <60 mL/min/1.73 m2) that were excluded in the AEGIS-I trial [69]. Neither study demonstrated significant safety concerns and CEC was increased 2.45-fold in the higher 6 g dose group. Though cardiovascular mortality was technically higher in the 6 g group, it is difficult to draw any conclusions from this finding as only 89 of the 1,258 patients completed follow-up through 1 year and the statistical power for MACE was very low. The drug is presently being investigated in the phase 3 AEGIS-II (ApoA-I Event Reducing in Ischemic Syndromes II) trial with the goal of recruiting over 17,000 participants to evaluate the endpoint of MACE in adults with history of acute MI. The trial is expected to conclude in 2022 and would provide a more definitive idea of use of this drug in atherosclerosis prevention.