Search for dissertations about: "Cystatin C"
Showing result 1 - 5 of 78 swedish dissertations containing the words Cystatin C.
-
1. L68Q cystatin C: Expression, cellular transport and turnover of the cystatin C variant forming amyloid in patients with Hereditary Cystatin C Amyloid Angiopaty (HCCAA)
Abstract : Hereditary cystatin C amyloid angiopathy (HCCAA) is a disorder characterised by multiple strokes in young adults, resulting in paralysis and dementia. The disease is caused by a mutation in the gene coding for the peptidase inhibitor cystatin C. READ MORE
-
2. L68Q cystatin C. Expression, cellular transport and turnover of the cystatin C variant forming amyloid in patients with Hereditary Cystatin C Amyloid Angiopathy (HCCAA)
Abstract : Hereditary cystatin C amyloid angiopathy (HCCAA) is a disorder characterised by multiple strokes in young adults, resulting in paralysis and dementia. The disease is caused by a mutation in the gene coding for the peptidase inhibitor cystatin C. READ MORE
-
3. Cystatin C in the Eye and in Specific Model Systems
Abstract : It is a necessity of life to make proteins, and it is an equal necessity to degrade those proteins, to eliminate dysfunctional proteins, and leave room for new ones. The processes of protein synthesis and degradation into peptides - proteolysis - have attracted a great interest during the last decades. READ MORE
-
4. Amyloid β-protein, Cystatin C and Cathepsin B as Biomarkers of Alzheimer's Disease
Abstract : It is suggested that Alzheimer’s disease (AD) is caused by an imbalance between production, degradation and clearance of the amyloid-β (Aβ) protein. This imbalance leads to aggregation of Aβ and tau proteins and neurodegeneration in the brain. READ MORE
-
5. Molecular Mechanisms in Amyloid Disorders. Novel Treatment Options in Hereditary Cystatin C Amyloid Angiopathy
Abstract : The pathophysiological process in Alzheimer’s disease and other amyloid disorders usually involves the transformation of a soluble monomeric protein via potentially toxic oligomers into amyloid fibrils. The structure and properties of the intermediary oligomers have been difficult to study due to their instability and dynamic equilibrium with smaller and larger species. READ MORE