Sub-micellar phospholipid accelerates amyloid formation by apolipoprotein C-II

C-terminal sequence of amyloid-resistant type F apolipoprotein A-II inhibits amyloid fibril formation of apolipoprotein A-II in mice.

In murine senile amyloidosis, misfolded serum apolipoprotein (apo) A-II deposits as amyloid fibrils (AApoAII) in a process associated with aging. Mouse strains carrying type C apoA-II (APOA2C) protein exhibit a high incidence of severe systemic amyloidosis. Previously, we showed that N- and C-terminal sequences of apoA-II protein are critical for polymerization into amyloid fibrils in vitro. He...

Cholesterol Determines and Limits rHDL Formation from Human Plasma Apolipoprotein A-II and Phospholipid Membranes

Apolipoprotein (apo) A-II, the second most abundant protein after apo A-I of human plasma high-density lipoproteins (HDL), is the most lipophilic of the exchangeable apolipoproteins. The rate of microsolubilization of dimyristoylphosphatidylcholine (DMPC) membranes by apo A-I to give rHDL increases as the level of membrane free cholesterol (FC) increases up to 20 mol % when the level of reactio...

Lipids: Apolipoprotein A-1 Apolipoprotein A-II Apolipoprotein B Apolipoprotein C-II Apolipoprotein C-III Apolipoprotein E Cholesterol Direct HDL Cholesterol Direct LDL Cholesterol Lipoprotein (a) sLDL Triglycerides

High density lipoproteins bind Abeta and apolipoprotein C-II amyloid fibrils.

Disease-associated amyloid deposits contain both fibrillar and nonfibrillar components. The majority of these amyloid components originate or coexist in the bloodstream. To understand the nature of the interaction between the nonfibrillar and fibrillar components, we have developed a centrifugation method to isolate fibril binding proteins from human serum. Amyloid fibrils composed of either Ab...

High density lipoproteins bind Ab and apolipoprotein C-II amyloid fibrils

Disease-associated amyloid deposits contain both fibrillar and nonfibrillar components. The majority of these amyloid components originate or coexist in the bloodstream. To understand the nature of the interaction between the nonfibrillar and fibrillar components, we have developed a centrifugation method to isolate fibril binding proteins from human serum. Amyloid fibrils composed of either Ab...