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

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...

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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...

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Apolipoprotein A-II and Structure of Human Serum High Density Lipoproteins

In an effort to determine the structural role of human serum apolipoprotein A-II (apo-A-II) in high density lipoproteins (HDL), we have conducted detailed studies on the conditions that influence the in vitro complexation of apo-A-II with mixtures of the polar and nonpolar lipids obtained from the parent HDL. APO-A-II and HDL lipids in different stoichiometric amounts were co-sonicated under di...

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Apolipoprotein A-II and structure of human serum high density lipoproteins. An approach by reassembly techniques.

In an effort to determine the structural role of human serum apolipoprotein A-II (apo-A-II) in high density lipoproteins (HDL), we have conducted detailed studies on the conditions that influence the in vitro complexation of apo-A-II with mixtures of the polar and nonpolar lipids obtained from the parent HDL. APO-A-II and HDL lipids in different stoichiometric amounts were co-sonicated under di...

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Expression of human apolipoprotein A-II and its effect on high density lipoproteins in transgenic mice.

Apolipoproteins A-I and A-II comprise approximately 70 and 20%, respectively, of the total protein content of HDL. Evidence suggests that apoA-I plays a central role in determining the structure and plasma concentration of HDL, while the role of apoA-II is uncertain. To help define the function of apoA-II and determine what effect increasing its plasma concentration has on HDL, transgenic mice ...

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

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منابع مشابه

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

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

Apolipoprotein A-II and Structure of Human Serum High Density Lipoproteins

Apolipoprotein A-II and structure of human serum high density lipoproteins. An approach by reassembly techniques.

Expression of human apolipoprotein A-II and its effect on high density lipoproteins in transgenic mice.

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