scholarly journals IL-10 is crucial for the transition from acute to chronic disease state during infection of mice with Schistosoma mansoni

2003 ◽  
Vol 33 (4) ◽  
pp. 880-888 ◽  
Author(s):  
Clare H. Sadler ◽  
Laura I. Rutitzky ◽  
Miguel J. Stadecker ◽  
R. Alan Wilson
Keyword(s):  
Chronic Disease ◽  
Schistosoma Mansoni ◽  
Disease State ◽  
Chronic Disease State

scholarly journals A Chronic Disease State Simulation in an Ambulatory Care Elective Course

2015 ◽  
Vol 79 (9) ◽  
pp. 133 ◽  
Author(s):  
Diana Isaacs ◽  
Cindy Leslie A. Roberson ◽  
Lalita Prasad-Reddy
Keyword(s):  
Chronic Disease ◽  
Ambulatory Care ◽  
Disease State ◽  
Elective Course ◽  
Chronic Disease State

scholarly journals Signaling, Polyubiquitination, Trafficking, and Inclusions: Sequestosome 1/p62's Role in Neurodegenerative Disease

2006 ◽  
Vol 2006 ◽  
pp. 1-12 ◽  
Author(s):  
Marie W. Wooten ◽  
Xiao Hu ◽  
J. Ramesh Babu ◽  
M. Lamar Seibenhener ◽  
Thangiah Geetha ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Chronic Disease ◽  
Neurodegenerative Diseases ◽  
Inclusion Formation ◽  
Disease Biomarker ◽  
Sequestosome 1 ◽  
Uba Domain ◽  
Chronic Disease State

Aggregated misfolded proteins are hallmarks of most neurodegenerative diseases. In a chronic disease state, including pathologic situations of oxidative stress, these proteins are sequestered into inclusions. Accumulation of aggregated proteins can be prevented by chaperones, or by targeting their degradation to the UPS. If the accumulation of these proteins exceeds their degradation, they may impair the function of the proteasome. Alternatively, the function of the proteasome may be preserved by directing aggregated proteins to the autophagy-lysosome pathway for degradation. Sequestosome 1/p62 has recently been shown to interact with polyubiquitinated proteins through its UBA domain and may direct proteins to either the UPS or autophagosome. P62 is present in neuronal inclusions of individuals with Alzheimer's disease and other neurodegenerative diseases. Herein, we review p62's role in signaling, aggregation, and inclusion formation, and specifically as a possible contributor to Alzheimer's disease. The use of p62 as a potential target for the development of therapeutics and as a disease biomarker is also discussed.

Sign in / Sign up

Export Citation Format

Share Document