Role of clusterin/apolipoprotein J glycosylation in LDL binding and aggregation
Moncunill Copoví, Montserrat
Sánchez Quesada, José Luís, dir. (Institut de Recerca Sant Pau)
Benítez González, Sònia, dir. (Institut de Recerca Sant Pau)
Universitat Autònoma de Barcelona. Facultat de Biociències

Data:	2025
Descripció:	36 pag.
Resum:	Cardiovascular diseases (CVDs) represent the main cause of mortality worldwide, with the atherosclerotic disease being the most common underlying pathology. Atherosclerosis is a chronic inflammatory vascular disease characterized by arterial wall thickening due to cholesterol accumulation, which obstructs blood flux. A wellestablished association exists between low-density lipoproteins (LDL) cholesterol levels, LDL composition and the risk of developing atherosclerotic diseases; particularly linked to the presence of small, dense LDL. Additionally, minor apolipoproteins present in LDL and high-density lipoproteins (HDL) have an influence on their pro-atherogenic or anti-atherogenic properties. Among them, apolipoprotein J (apoJ), also known as clusterin, an extracellular chaperone with a glycosylation domain, is known to exert a protective role in the atherosclerotic disease progression through multiple molecular mechanisms, such as binding to LDL and inhibition of LDL aggregation. Based on this knowledge, our research group aimed to express and purify human recombinant apoJ using HEK293T cells. We sought to investigate the role of the glycosylation moiety of apoJ. To achieve this goal, we used deglycosylases to generate different glycosylation-modified isoforms of apoJ in order to explore for the possible role in the interaction between apoJ and LDL, as well as their capacity to prevent LDL aggregation. Our main findings demonstrated that apoJ had the capacity to prevent LDL aggregation, and this effect was directly proportional to the concentration of apoJ. Furthermore, glycosylation domain played a relevant role in this function, because deglycosylated apoJ partially lost its ability to prevent LDL aggregation. Additionally, this loss of functionality depended on the glycosylation degree. Finally, this posttranslational modification was linked to the interaction between LDL and apoJ, with deglycosylated apoJ binding more efficiently to LDL than the glycosylated form.
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Llengua:	Català
Titulació:	Bioquímica, Biologia Molecular i Biomedicina [4313794]
Pla d'estudis:	Màster Universitari en Bioquímica, Biologia Molecular i Biomedicina [1599]
Document:	Treball de fi de postgrau
Matèria:	Aterosclerosis ; ApoJ ; Glicosilació ; LDL ; Agregació LDL ; Glicosilación ; Agregación LDL ; Atherosclerosis ; Glycosylation ; LDL Aggregation

37 p, 1.6 MB

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