Increased KPI containing amyloid precursor protein in experimental autoimmune encephalomyelitis brains.

Abstract

Amyloid precursor protein can be translated from three alternatively spliced mRNAs. We measured levels of amyloid precursor protein isoforms containing the Kunitz protease inhibitor domain (KPIAPP), and amyloid precursor protein without the Kunitz protease inhibitor domain (KPIAPP) in brain homogenates of acute experimental autoimmune encephalomyelitis mice. At the preclinical phase of the disease, both KPIAPP and KPIAPP levels were significantly higher in homogenates from brains of autoimmune encephalomyelitis mice, whereas at the acute phase of the disease only KPIAPP remained significantly elevated compared with controls. At the recovery phase, no differences were observed between the groups. The early and isoform-specific elevation of KPIAPP in autoimmune encephalomyelitis mice suggests a possible role for amyloid precursor protein in the immune response mediating the disease.

• Authors: Orit Beilin, Dimitrios M Karussis, Amos D Korczyn, David Gurwitz, Ramona Aronovich, Rachel Mizrachi-Kol, Joab Chapman
• Journal: Neuroreport (Neuroreport) Vol. 18 Issue 6 Pg. 581-4 (Apr 16 2007) ISSN: 0959-4965 [Print] England
• PMID: 17413661 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amyloid beta-Protein Precursor
• Aprotinin

Topics

• Acute Disease
• Amyloid beta-Protein Precursor (chemistry, immunology, metabolism)
• Animals
• Aprotinin (chemistry, immunology, metabolism)
• Encephalomyelitis, Autoimmune, Experimental (immunology, metabolism)
• Female
• Isomerism
• Mice
• Mice, Inbred Strains
• Prosencephalon (immunology, metabolism)
• Protein Structure, Tertiary