Expression of apolipoprotein B epitopes in low density lipoproteins of hemodialyzed patients.

Reade, V; Tailleux, A; Reade, R; Harduin, P; Cachera, C; Tacquet, A; Fruchart, J C; Fievet, C · Kidney Int · 1993

cross_sectional · Level IV

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Abstract

Serum and isolated low-density lipoprotein (LDL) composition abnormalities were investigated in 20 hemodialyzed patients with chronic renal failure and 15 healthy normolipidemic subjects for comparison. LDL apolipoprotein B (apo B) epitope accessibility was determined by the use of seven monoclonal antibodies (Mabs). These Mabs recognize fragments on the N-terminal part of apo B (Mabs B1, B4), on the middle part (Mab BL7), on the C-terminal (Mabs BA11, BL3), and the two remaining Mabs recognize conformational epitopes of apo B (BL5, DA7). Mab BA11 recognizes a fragment of apo B which interacts with the B/E receptor. In hemodialyzed patients, LDL content of triglycerides (P < 0.001) and apo CIII (P < 0.005) was increased, while cholesteryl esters (P < 0.005) were decreased. The accessibility of BL5 epitopes of LDL apo B was enhanced (P < 0.05), while BA11 epitope expression was decreased (P < 0.01). The conformation of patients' LDL (CRF-LDL) was probably abnormal and seemed to be related to some modification of the lipidic environment. It is important to consider a structural modification as it alters the B/E receptor recognition domain of apo B. These results confirm LDL abnormalities in hemodialyzed patients and suggest a possible modification of the recognition of the LDL by cells.

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