By Novartis Foundation
With the ever-increasing upward push in existence expectancy, there's an pressing have to enhance our knowing of the connection among aging and the pathogenesis of age-related illnesses so that it will establish more desirable technique of prevention, amelioration and administration of such ailments. moreover, there's a have to lessen the social and fiscal effect of the growing old inhabitants. Age-related morbidity and mortality vary dramatically between participants; this e-book focusses on person alterations in susceptibility to age-related problems.
It comprises contributions from prime specialists within the box on issues such as:
age-related pathology within the mind, age-related procedures in stem cells, and age-related results at the immune procedure and in bone, muscle and cardiovascular tissue. For all people with an curiosity within the biology of growing old, this is often obligatory reading.Content:
Read or Download Ageing Vulnerability: Causes and Interventions: Novartis Foundation Symposium 235 PDF
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Extra info for Ageing Vulnerability: Causes and Interventions: Novartis Foundation Symposium 235
Understanding the metalloprotein biochemistry in both diseases may lead to a better understanding of the underlying pathophysiology in both disorders and suggest novel targets for therapeutic agents. 2001 Ageing vulnerability: causes and interventions. Wiley, Chichester (Novartis Foundation Symposium 235) p 26^43 A number of chronic, progressive degenerative disorders are associated with abnormal deposition and accumulation of proteins. Common human diseases as diverse as Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS), prion diseases (including Creutzfeldt-Jakob disease and other spongiform encephalopathies), Parkinson’s disease, age-related cataracts (ARCs) and type 2 diabetes mellitus are all notable for the presence of these pathological protein deposits.
ARC is similar to AD in that both are chronically progressive disorders of ageing, which involve altered protein structure and aggregation (Harding 1972, 1998). Lens protein aggregation leads to the opaci¢cation, which are the sine qua non of cataracts. The major structural protein in the lens protein is a-crystallin, which is composed of two subspecies, aA (173 amino acids; Mr 19 909) and aB (175 amino acids; Mr 20 159), in a molar ratio which is variable among species (Augusteyn & Koretz 1987).
The proteins comprising these deposits rapidly aggregate and frequently result in direct cytotoxicity. Recent evidence suggests that these abnormal protein deposits may directly involve trace quantities of redox-active metals such as copper, iron and manganese (Bush 2000). A large and growing literature now supports the notion that aberrant metal-catalysed protein redox reactions ö those involving local reactions of redox-active metals, oxygen and proteins (Stadtman & Oliver 1991, Stadtman 1993) ö may be a common denominator in the underlying alterations in protein secondary structure which result in protein deposition and accumulation in these diseases.