Synthesis and secretion of active alpha sub(1)-antichymotrypsin by murine primary astrocytes

Activated astrocytes have been identified as the main source of the serine protease inhibitor alpha sub(1)-antichymotrypsin (ACT), an acute phase protein that is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain. We analyzed the synthe...

Full description

Saved in:
Bibliographic Details
Published in:Neurobiology of aging 1996-01, Vol.17 (5), p.767-771
Main Authors: Kanemaru, K, Meckelein, B, Marshall, DCL, Sipe, J D, Abraham, C R
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Activated astrocytes have been identified as the main source of the serine protease inhibitor alpha sub(1)-antichymotrypsin (ACT), an acute phase protein that is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain. We analyzed the synthesis of ACT by cultured murine astrocytes in vitro. The murine astrocytes expressed an ACT-like antigen that crossreacted with antibodies to human ACT. The murine ACT-like protein is secreted by the astrocytes and is able to form an SDS-resistant complex with the serine protease cathepsin G, indicating that the secreted ACT is biologically active. We conclude that cultured primary astrocytes synthesize and secrete murine ACT in an active form. We, therefore, suggest that the ACT present within AD plaques is locally derived from plaque-associated activated astrocytes as a part of a glia-mediated local inflammatory response that is associated with the neurodegeneration seen in AD.
ISSN:0197-4580