HUMAN APO A-I AND ITS NATURAL VARIANTS INDUCE DIFFERENT ENDOTHELIAL CHONDROITIN/ DERMATAN SULFATE PROTEOGLYCAN PROFILE. PROBABLE ROLE IN SETTLEMENT OF AMYLOIDOSIS.

FUNEZ, F; M. A. TRICERRI; BIROCCO, AM; CALABRESE, GRACIELA C.; EIGUREN, AC; ROSU, S. A

Mar del Plata

Encuentro; SAIC.SAI.SAFIS 2018; 2018

SAIC. SAI.SAFIS

Amyloidosis constitutes a heterogeneous group of diseases involving protein misfolding and deposition of fibrils. Natural variants or fragments of Apolipoprotein A-I (apo A-I), the main protein of plasma high-density lipoproteins, elicit their propensity to suffer misfolding or aggregation. Our previous reports suggest that specific interactions of ApoA-I with glycosaminoglycans could elicit its retention and/or aggregation. Furthermore, recent studies indicate that protein cores of proteoglycans (PGs) may influence the type and modification patterns of the subsequently attached glycosaminoglycan chains. We hypothesize that mutations in human Apo A-I may affect the core protein pattern expression of vascular chondroitin/dermatan sulfate PGs, modulating chemical changes in the glycosylation pattern which elicit extracellular ApoA-I aggregation.