Proteinopathy is a broad term used to describe any disease or condition that arises as
a result of aberrant protein behavior. Most often it is used when discussing any of a wide
range of neurodegenerative diseases that tend to result from an abnormal misfolding and
subsequent aggregation of a normal cellular protein. The pathology of each of these diseases
is largely dependent upon the nature of the protein aggregate that is responsible for or
resulting from the disease. When viewed individually each disease seems only vaguely
similar to others, but when a step back is taken to consider the broader aspects of the disease
it begins to show similarities with other diseases, some of which are better studied and
understood. The advances in other proteinopathies can then be experimentally applied to a
specific disease of interest and the results compared to gain better understand the
mechanisms underlying its pathogenesis and progression.
Two examples of such proteinopathies are transmissible spongiform encephalopathies
(TSE) and Parkinson’s disease (PD). TSEs are a subset of prion misfolding diseases,
specifically identified as being transmissible to other individuals in a manner resembling
viral, bacterial, or toxic exposure, that have been studied in animals for decades. While rare
in humans, prion protein misfolding does occur in a handful of different forms. PD on the
other hand is fairly common in older individuals, affecting approximately one million people
in the United States and an estimated 10 million people worldwide. Both conditions share
such notable traits as characteristic protein aggregates, being neurodegenerative, eventually
fatally so, and having a link to the enteric nervous system. Techniques applied to the study of
TSEs have been successfully applied to the study of PD, and inverse has occurred as well,
leading to leap frog effect of advancement for both diseases.
In this thesis, topics of two proteinopathies are covered. A literature review of chronic
wasting disease (CWD) history, study, and further interests leads the paper. This is followed
by a chapter on analysis of feral pig brainstem by RT-QuIC to determine the presence or
absence of aggregated prion protein. The next chapter is dedicated to describing a protocol
for the efficient and reliable production of recombinant human α-synuclein monomeric
protein for use in research. Each of these techniques has been applied to the study of multiple
diseases, but the refinement of each technique for application to the disease or species of
interest is essential to achieving the best results.
","abstract_html":"<p>Proteinopathy is a broad term used to describe any disease or condition that arises as</p> <p>a result of aberrant protein behavior. Most often it is used when discussing any of a wide</p> <p>range of neurodegenerative diseases that tend to result from an abnormal misfolding and</p> <p>subsequent aggregation of a normal cellular protein. The pathology of each of these diseases</p> <p>is largely dependent upon the nature of the protein aggregate that is responsible for or</p> <p>resulting from the disease. When viewed individually each disease seems only vaguely</p> <p>similar to others, but when a step back is taken to consider the broader aspects of the disease</p> <p>it begins to show similarities with other diseases, some of which are better studied and</p> <p>understood. The advances in other proteinopathies can then be experimentally applied to a</p> <p>specific disease of interest and the results compared to gain better understand the</p> <p>mechanisms underlying its pathogenesis and progression.</p> <p>Two examples of such proteinopathies are transmissible spongiform encephalopathies</p> <p>(TSE) and Parkinson’s disease (PD). TSEs are a subset of prion misfolding diseases,</p> <p>specifically identified as being transmissible to other individuals in a manner resembling</p> <p>viral, bacterial, or toxic exposure, that have been studied in animals for decades. While rare</p> <p>in humans, prion protein misfolding does occur in a handful of different forms. PD on the</p> <p>other hand is fairly common in older individuals, affecting approximately one million people</p> <p>in the United States and an estimated 10 million people worldwide. Both conditions share</p> <p>such notable traits as characteristic protein aggregates, being neurodegenerative, eventually</p> <p>fatally so, and having a link to the enteric nervous system. Techniques applied to the study of</p> <p>TSEs have been successfully applied to the study of PD, and inverse has occurred as well,</p> <p>leading to leap frog effect of advancement for both diseases.</p> <p>In this thesis, topics of two proteinopathies are covered. A literature review of chronic</p> <p>wasting disease (CWD) history, study, and further interests leads the paper. This is followed</p> <p>by a chapter on analysis of feral pig brainstem by RT-QuIC to determine the presence or</p> <p>absence of aggregated prion protein. The next chapter is dedicated to describing a protocol</p> <p>for the efficient and reliable production of recombinant human α-synuclein monomeric</p> <p>protein for use in research. Each of these techniques has been applied to the study of multiple</p> <p>diseases, but the refinement of each technique for application to the disease or species of</p> <p>interest is essential to achieving the best results.</p>","abstract_has_math":false,"creators":["Hepker, Monica"],"institution":null,"degree_name":"Master of Science","degree_level":"thesis","degree_discipline":"Biomedical Sciences","degree_department":"Department of Veterinary Microbiology and Preventive Medicine","school":null,"contributors":[],"advisors":["Anumantha Kanthasamy"],"committee_chairs":[],"committee_members":[],"year":2019,"date_issued":"2019-01-01","date_published":"2019-01-01","updated_at":"2026-07-24T02:38:12Z","subjects":[],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["archive/lib.dr.iastate.edu/etd/17202/"],"render_values":[{"text":"archive/lib.dr.iastate.edu/etd/17202/","href":null,"code":true}]}]},"links":{"outbound_url":"https://dr.lib.iastate.edu/handle/20.500.12876/31385","outbound_label":"Repository record","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Anumantha Kanthasamy"]},{"key":"dc:contributor.department","label":"Department","values":["Department of Veterinary Microbiology and Preventive Medicine"]},{"key":"dc:creator","label":"Author","values":["Hepker, Monica"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2019-09-20T04:05:27.000"]},{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2020-06-30T03:16:40Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2020-06-30T03:16:40Z"]},{"key":"dc:date.issued","label":"Date","values":["2019-01-01"]},{"key":"dc:type","label":"Dc Type","values":["thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biomedical Sciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["archive/lib.dr.iastate.edu/etd/17202/"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://dr.lib.iastate.edu/handle/20.500.12876/31385"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Proteinopathy is a broad term used to describe any disease or condition that arises as
a result of aberrant protein behavior. Most often it is used when discussing any of a wide
range of neurodegenerative diseases that tend to result from an abnormal misfolding and
subsequent aggregation of a normal cellular protein. The pathology of each of these diseases
is largely dependent upon the nature of the protein aggregate that is responsible for or
resulting from the disease. When viewed individually each disease seems only vaguely
similar to others, but when a step back is taken to consider the broader aspects of the disease
it begins to show similarities with other diseases, some of which are better studied and
understood. The advances in other proteinopathies can then be experimentally applied to a
specific disease of interest and the results compared to gain better understand the
mechanisms underlying its pathogenesis and progression.
Two examples of such proteinopathies are transmissible spongiform encephalopathies
(TSE) and Parkinson’s disease (PD). TSEs are a subset of prion misfolding diseases,
specifically identified as being transmissible to other individuals in a manner resembling
viral, bacterial, or toxic exposure, that have been studied in animals for decades. While rare
in humans, prion protein misfolding does occur in a handful of different forms. PD on the
other hand is fairly common in older individuals, affecting approximately one million people
in the United States and an estimated 10 million people worldwide. Both conditions share
such notable traits as characteristic protein aggregates, being neurodegenerative, eventually
fatally so, and having a link to the enteric nervous system. Techniques applied to the study of
TSEs have been successfully applied to the study of PD, and inverse has occurred as well,
leading to leap frog effect of advancement for both diseases.
In this thesis, topics of two proteinopathies are covered. A literature review of chronic
wasting disease (CWD) history, study, and further interests leads the paper. This is followed
by a chapter on analysis of feral pig brainstem by RT-QuIC to determine the presence or
absence of aggregated prion protein. The next chapter is dedicated to describing a protocol
for the efficient and reliable production of recombinant human α-synuclein monomeric
protein for use in research. Each of these techniques has been applied to the study of multiple
diseases, but the refinement of each technique for application to the disease or species of
interest is essential to achieving the best results.
"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Evaluating suspected CWD feral pig brain samples using RT-QuIC and protocol for the purification and quality control of recombinant monomeric proteins for RT-QuIC assay"]}]}],"canonical_facts":{"dc:contributor.advisor":["Anumantha Kanthasamy"],"dc:contributor.department":["Department of Veterinary Microbiology and Preventive Medicine"],"dc:creator":["Hepker, Monica"],"dc:date":["2019-09-20T04:05:27.000"],"dc:date.accessioned":["2020-06-30T03:16:40Z"],"dc:date.available":["2020-06-30T03:16:40Z"],"dc:date.issued":["2019-01-01"],"dc:description.abstract":["Proteinopathy is a broad term used to describe any disease or condition that arises as
a result of aberrant protein behavior. Most often it is used when discussing any of a wide
range of neurodegenerative diseases that tend to result from an abnormal misfolding and
subsequent aggregation of a normal cellular protein. The pathology of each of these diseases
is largely dependent upon the nature of the protein aggregate that is responsible for or
resulting from the disease. When viewed individually each disease seems only vaguely
similar to others, but when a step back is taken to consider the broader aspects of the disease
it begins to show similarities with other diseases, some of which are better studied and
understood. The advances in other proteinopathies can then be experimentally applied to a
specific disease of interest and the results compared to gain better understand the
mechanisms underlying its pathogenesis and progression.
Two examples of such proteinopathies are transmissible spongiform encephalopathies
(TSE) and Parkinson’s disease (PD). TSEs are a subset of prion misfolding diseases,
specifically identified as being transmissible to other individuals in a manner resembling
viral, bacterial, or toxic exposure, that have been studied in animals for decades. While rare
in humans, prion protein misfolding does occur in a handful of different forms. PD on the
other hand is fairly common in older individuals, affecting approximately one million people
in the United States and an estimated 10 million people worldwide. Both conditions share
such notable traits as characteristic protein aggregates, being neurodegenerative, eventually
fatally so, and having a link to the enteric nervous system. Techniques applied to the study of
TSEs have been successfully applied to the study of PD, and inverse has occurred as well,
leading to leap frog effect of advancement for both diseases.
In this thesis, topics of two proteinopathies are covered. A literature review of chronic
wasting disease (CWD) history, study, and further interests leads the paper. This is followed
by a chapter on analysis of feral pig brainstem by RT-QuIC to determine the presence or
absence of aggregated prion protein. The next chapter is dedicated to describing a protocol
for the efficient and reliable production of recombinant human α-synuclein monomeric
protein for use in research. Each of these techniques has been applied to the study of multiple
diseases, but the refinement of each technique for application to the disease or species of
interest is essential to achieving the best results.
"],"dc:format.mimetype":["application/pdf"],"dc:identifier":["archive/lib.dr.iastate.edu/etd/17202/"],"dc:identifier.uri":["https://dr.lib.iastate.edu/handle/20.500.12876/31385"],"dc:language.iso":["en"],"dc:title":["Evaluating suspected CWD feral pig brain samples using RT-QuIC and protocol for the purification and quality control of recombinant monomeric proteins for RT-QuIC assay"],"dc:type":["thesis"],"thesis:degree_discipline":["Biomedical Sciences"],"thesis:degree_level":["thesis"],"thesis:degree_name":["Master of Science"]},"updated_at":"2026-07-24T02:38:12Z"}