About 20% volume of the mammalian central nervous system comprises of an extracellular matrix that includes proteins, proteoglycans, and glycosaminoglycans (Bignami A et.al 1993). Evolving evidence indicates that the organization and composition of this matrix change throughout the course of normal aging, during neurodegenerative diseases and following central nervous system injury and that these modifications influence a diverse range of cellular behaviors. The central nervous system extracellular matrix was originally believed to play mostly structural roles including tissue integrity. Results from several researches over the past few decades, however, indicate that the central nervous system extracellular matrix is an information wealthy environment that includes signals that influence cell proliferation, differentiation, migration, synapse formation and remodeling, and responses to different injuries.
Decades before the fundamental molecular genetics or biochemical properties were known, Familial (resulting from gene relations) aggregation had been acknowledged as an obvious feature of many neurodegenerative disorders. Often it was the identification of …show more content…
2010). Most cases of prion diseases are sporadic with no apparent onset, but in some rare cases, prion diseases are acquired from faulty genes, by surgical procedures, transfusions, or from contaminated foods. There is currently no cure for prion diseases because of a few reasons. For one, the immune system is unable to recognize misfolded form of the protein as a pathogen to be destroyed; hence the aggregates or amyloid plaques that form from this process go undetected. Prion proteins are also extremely resistant to many chemical reactions, ultra violet light and heat, which are conventional ways of denaturing or destroying proteins (Alper et al.
Decades before the fundamental molecular genetics or biochemical properties were known, Familial (resulting from gene relations) aggregation had been acknowledged as an obvious feature of many neurodegenerative disorders. Often it was the identification of …show more content…
2010). Most cases of prion diseases are sporadic with no apparent onset, but in some rare cases, prion diseases are acquired from faulty genes, by surgical procedures, transfusions, or from contaminated foods. There is currently no cure for prion diseases because of a few reasons. For one, the immune system is unable to recognize misfolded form of the protein as a pathogen to be destroyed; hence the aggregates or amyloid plaques that form from this process go undetected. Prion proteins are also extremely resistant to many chemical reactions, ultra violet light and heat, which are conventional ways of denaturing or destroying proteins (Alper et al.