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Article ; Online: Familial Presenilin Mutations and Sporadic Alzheimer's Disease Pathology: Is the Assumption of Biochemical Equivalence Justified?

Roher, Alex E / Maarouf, Chera L / Kokjohn, Tyler A

2016 Volume 50, Issue 3, Page(s) 645–658

Abstract: Studies of presenilin (PSEN) gene mutations producing early onset Alzheimer's disease (AD) have helped elucidate the pathogenic mechanisms of dementia and guided clinical trials of potential therapeutic interventions. Although familial and sporadic forms ...

Abstract	Studies of presenilin (PSEN) gene mutations producing early onset Alzheimer's disease (AD) have helped elucidate the pathogenic mechanisms of dementia and guided clinical trials of potential therapeutic interventions. Although familial and sporadic forms of AD share features, it is unclear if the two are precisely equivalent. In addition, PSEN mutations do not all produce a single phenotype, but exhibit substantial variability in clinical manifestations, which are related to the position and chemical nature of their amino acid substitutions as well as ratios of critical molecules such as Aβ40 and Aβ42. These differences complicate the interpretation of critical clinical trial results and their desired extrapolation to sporadic AD treatment. In this perspective, we examine differences between familial AD and sporadic AD as well as attributes shared by these uniquely arising disturbances in brain biochemical homeostasis that culminate in dementia.
MeSH term(s)	Alzheimer Disease/classification ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Brain/metabolism ; Brain/pathology ; Humans ; Mutation/genetics ; Presenilins/genetics ; Presenilins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Presenilins
Language	English
Publishing date	2016
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-150757
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Article ; Online: Commentary on "Alzheimer's disease drug development and the problem of the blood-brain barrier." Alzheimer's disease drugs: more than one barrier to breach.

Roher, Alex E / Kokjohn, Tyler A

Alzheimer's & dementia : the journal of the Alzheimer's Association

2009 Volume 5, Issue 5, Page(s) 437–438

MeSH term(s)	Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Biological Transport/drug effects ; Biological Transport/physiology ; Blood-Brain Barrier/physiology ; Brain/physiopathology ; Central Nervous System Agents/pharmacokinetics ; Drug Delivery Systems/methods ; Humans
Chemical Substances	Central Nervous System Agents
Language	English
Publishing date	2009-09
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1016/j.jalz.2009.07.037
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Article ; Online: Amyloid precursor protein transgenic mouse models and Alzheimer's disease: understanding the paradigms, limitations, and contributions.

Kokjohn, Tyler A / Roher, Alex E

Alzheimer's & dementia : the journal of the Alzheimer's Association

2009 Volume 5, Issue 4, Page(s) 340–347

Abstract: Transgenic (Tg) mice that overexpress mutant familial Alzheimer's disease (AD) amyloid precursor protein (APP) genes have contributed to an understanding of dementia pathology, and support the amyloid cascade hypothesis. Although many sophisticated mice ... ...

Abstract	Transgenic (Tg) mice that overexpress mutant familial Alzheimer's disease (AD) amyloid precursor protein (APP) genes have contributed to an understanding of dementia pathology, and support the amyloid cascade hypothesis. Although many sophisticated mice APP models exist, none recapitulates AD cellular and behavioral pathology. The morphological resemblance to AD amyloidosis is impressive, but fundamental biophysical and biochemical properties of the APP/Abeta produced in Tg mice differ substantially from those of humans. The greater resilience of Tg mice in the presence of substantial Abeta burdens suggests that levels and forms deleterious to human neurons are not as noxious in these models. Transgenic mice were widely used for testing AD therapeutic agents, and demonstrated promising results. Unfortunately, clinical trials resulted in unforeseen adverse events or negative therapeutic outcomes. The disparity between success and failure is in part attributable to evolutionary divergence between humans and rodents. These observations suggest that the pathogenesis of AD is by far more intricate than can be explained by a straightforward accumulation of Abeta.
MeSH term(s)	Alzheimer Disease/drug therapy ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Brain/metabolism ; Brain/pathology ; Brain/physiopathology ; Clinical Trials as Topic/adverse effects ; Clinical Trials as Topic/methods ; Disease Models, Animal ; Drug Evaluation, Preclinical/methods ; Humans ; Mice ; Mice, Transgenic ; Neurons/metabolism ; Neurons/pathology ; Species Specificity ; Treatment Failure
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
Language	English
Publishing date	2009-03-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1016/j.jalz.2009.03.002
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Article ; Online: Antibody responses, amyloid-beta peptide remnants and clinical effects of AN-1792 immunization in patients with AD in an interrupted trial.

Kokjohn, Tyler A / Roher, Alex E

CNS & neurological disorders drug targets

2009 Volume 8, Issue 2, Page(s) 88–97

Abstract: Post mortem examinations of AN-1792-vaccinated humans revealed this therapy produced focal senile plaque disruption. Despite the dispersal of substantial plaque material, vaccination did not constitute even a partial eradication of brain amyloid as water ...

Abstract	Post mortem examinations of AN-1792-vaccinated humans revealed this therapy produced focal senile plaque disruption. Despite the dispersal of substantial plaque material, vaccination did not constitute even a partial eradication of brain amyloid as water soluble amyloid-beta (Abeta) 40/42 increased in the gray matter compared to sporadic Alzheimer's disease (AD) patients and total brain Abeta levels were not decreased. Significant aspects of AD pathology were unaffected by vaccination with both vascular amyloid and hyper-phosphorylated tau deposits appeared refractory to this therapy. In addition, vaccination resulted in the consequential and drastic expansion of the white matter (WM) amyloid pool to levels without precedent in sporadic AD patients. Although vaccination disrupted amyloid plaques, this therapy did not enhance long-term cognitive function or necessarily halt neurodegeneration. The intricate involvement of vascular pathology in AD evolution and the firm recalcitrance of vessel-associated amyloid to antibody-mediated disruption suggest that immunization therapies might be more effective if administered on a prophylactic basis before vascular impairment and well ahead of any clinically evident cognitive decline. Amyloid-beta is viewed as pathological based on the postmortem correlation of senile plaques with an AD diagnosis. It remains uncertain which of the various forms of this peptide is the most toxic and whether Abeta or senile plaques themselves serve any desirable or protective functions. The long-term cognitive effects of chronic immunotherapy producing a steadily accumulating and effectively permanent pool of disrupted Abeta peptides within the human brain are unknown. In addition, the side effects of such therapy provided on a chronic basis could extend far beyond the brain. Eagerly seeking new therapies, critical knowledge gaps should prompt us to take a more wholistic perspective viewing Abeta and the amyloid cascade as aspects of complex and many-faceted physiological processes that sometimes end in AD dementia.
MeSH term(s)	Alzheimer Disease/drug therapy ; Alzheimer Disease/immunology ; Alzheimer Disease/physiopathology ; Amyloid beta-Peptides/administration & dosage ; Amyloid beta-Peptides/adverse effects ; Amyloid beta-Peptides/antagonists & inhibitors ; Amyloid beta-Peptides/metabolism ; Antibodies/blood ; Antibodies/drug effects ; Cerebral Amyloid Angiopathy/drug therapy ; Cerebral Amyloid Angiopathy/immunology ; Cerebral Amyloid Angiopathy/physiopathology ; Clinical Trials as Topic/statistics & numerical data ; Humans ; Immunotherapy, Active/methods ; Immunotherapy, Active/statistics & numerical data ; Plaque, Amyloid/drug effects ; Plaque, Amyloid/immunology ; Plaque, Amyloid/metabolism ; Time ; Treatment Outcome
Chemical Substances	AN-1792 ; Amyloid beta-Peptides ; Antibodies
Language	English
Publishing date	2009-04-07
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2228394-8
ISSN	1996-3181 ; 1871-5273
ISSN (online)	1996-3181
ISSN	1871-5273
DOI	10.2174/187152709787847315
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Article ; Online: Is Alzheimer's disease amyloidosis the result of a repair mechanism gone astray?

Kokjohn, Tyler A / Maarouf, Chera L / Roher, Alex E

Alzheimer's & dementia : the journal of the Alzheimer's Association

2011 Volume 8, Issue 6, Page(s) 574–583

Abstract: Here, we synthesize several lines of evidence supporting the hypothesis that at least one function of amyloid-β is to serve as a part of the acute response to brain hemodynamic disturbances intended to seal vascular leakage. Given the resilient and ... ...

Abstract	Here, we synthesize several lines of evidence supporting the hypothesis that at least one function of amyloid-β is to serve as a part of the acute response to brain hemodynamic disturbances intended to seal vascular leakage. Given the resilient and adhesive physicochemical properties of amyloid, an abluminal hemostatic repair system might be highly advantageous, if deployed on a limited and short-term basis, in young individuals. However, in the aged, inevitable cardiovascular dysfunction combined with brain microvascular lesions may yield global chronic hypoperfusion that may lead to continuous amyloid deposition and consequential negative effects on neuronal viability. A large body of experimental evidence supports the hypothesis of an amyloid-β rescue function gone astray. Preventing or inducing the removal of amyloid in Alzheimer's disease (AD) has been simultaneously successful and disappointing. Amyloid deposits clearly play major roles in AD, but they may not represent the preeminent factor in dementia pathogenesis. Successful application of AD preventative approaches may hinge on an accurate and comprehensive view of comorbidities, including cardiovascular disease, diabetes, and head trauma.
MeSH term(s)	Alzheimer Disease/etiology ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Animals ; Cerebral Amyloid Angiopathy/complications ; Cerebral Amyloid Angiopathy/metabolism ; Cerebral Amyloid Angiopathy/pathology ; Humans
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2011-11-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1016/j.jalz.2011.05.2429
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Article ; Online: APP/Aβ structural diversity and Alzheimer's disease pathogenesis.

Roher, Alex E / Kokjohn, Tyler A / Clarke, Steven G / Sierks, Michael R / Maarouf, Chera L / Serrano, Geidy E / Sabbagh, Marwan S / Beach, Thomas G

Neurochemistry international

2017 Volume 110, Page(s) 1–13

Abstract: The amyloid cascade hypothesis of Alzheimer's disease (AD) proposes amyloid- β (Aβ) is a chief pathological element of dementia. AD therapies have targeted monomeric and oligomeric Aβ 1-40 and 1-42 peptides. However, alternative APP proteolytic ... ...

Abstract	The amyloid cascade hypothesis of Alzheimer's disease (AD) proposes amyloid- β (Aβ) is a chief pathological element of dementia. AD therapies have targeted monomeric and oligomeric Aβ 1-40 and 1-42 peptides. However, alternative APP proteolytic processing produces a complex roster of Aβ species. In addition, Aβ peptides are subject to extensive posttranslational modification (PTM). We propose that amplified production of some APP/Aβ species, perhaps exacerbated by differential gene expression and reduced peptide degradation, creates a diverse spectrum of modified species which disrupt brain homeostasis and accelerate AD neurodegeneration. We surveyed the literature to catalog Aβ PTM including species with isoAsp at positions 7 and 23 which may phenocopy the Tottori and Iowa Aβ mutations that result in early onset AD. We speculate that accumulation of these alterations induce changes in secondary and tertiary structure of Aβ that favor increased toxicity, and seeding and propagation in sporadic AD. Additionally, amyloid-β peptides with a pyroglutamate modification at position 3 and oxidation of Met35 make up a substantial portion of sporadic AD amyloid deposits. The intrinsic physical properties of these species, including resistance to degradation, an enhanced aggregation rate, increased neurotoxicity, and association with behavioral deficits, suggest their emergence is linked to dementia. The generation of specific 3D-molecular conformations of Aβ impart unique biophysical properties and a capacity to seed the prion-like global transmission of amyloid through the brain. The accumulation of rogue Aβ ultimately contributes to the destruction of vascular walls, neurons and glial cells culminating in dementia. A systematic examination of Aβ PTM and the analysis of the toxicity that they induced may help create essential biomarkers to more precisely stage AD pathology, design countermeasures and gauge the impacts of interventions.
MeSH term(s)	Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/etiology ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/analysis ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/analysis ; Amyloid beta-Protein Precursor/chemistry ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Brain/metabolism ; Brain/pathology ; Humans ; Plaque, Amyloid/complications ; Plaque, Amyloid/diagnostic imaging ; Plaque, Amyloid/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
Language	English
Publishing date	2017-08-12
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	283190-9
ISSN	1872-9754 ; 0197-0186
ISSN (online)	1872-9754
ISSN	0197-0186
DOI	10.1016/j.neuint.2017.08.007
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Article: Chemical and neuropathological analyses of an Alzheimer's disease patient treated with solanezumab.

Roher, Alex E / Maarouf, Chera L / Kokjohn, Tyler A / Belden, Christine / Serrano, Geidy / Sabbagh, Marwan S / Beach, Thomas G

American journal of neurodegenerative disease

2016 Volume 5, Issue 4, Page(s) 158–170

Abstract: Introduction: Based on the amyloid cascade hypothesis of Alzheimer's disease (AD) pathogenesis, a series of clinical trials involving immunotherapies have been undertaken including infusion with the IgG1 monoclonal anti-Aβ antibody solanezumab directed ... ...

Abstract	Introduction: Based on the amyloid cascade hypothesis of Alzheimer's disease (AD) pathogenesis, a series of clinical trials involving immunotherapies have been undertaken including infusion with the IgG1 monoclonal anti-Aβ antibody solanezumab directed against the middle of the soluble Aβ peptide. In this report, we give an account of the clinical history, psychometric testing, gross and microscopic neuropathology as well as immunochemical quantitation of soluble and insoluble Aβ peptides and other proteins of interest related to AD pathophysiology in a patient treated with solanezumab. Materials and methods: The solanezumab-treated AD case (SOLA-AD) was compared to non-demented control (NDC, n = 5) and non-immunized AD (NI-AD, n = 5) subjects. Brain sections were stained with H&E, Thioflavine-S, Campbell-Switzer and Gallyas methods. ELISA and Western blots were used for quantification of proteins of interest. Results: The SOLA-AD subject's neuropathology and biochemistry differed sharply from the NDC and NI-AD groups. The SOLA-AD case had copious numbers of amyloid laden blood vessels in all areas of the cerebral cortex, from leptomeningeal perforating arteries to arteriolar deposits which attained the cerebral amyloid angiopathy (CAA) maximum score of 12. In contrast, the maximum CAA for the NI-AD cases averaged a total of 3.6, while the NDC cases only reached 0.75. The SOLA-AD subject had 4.4-fold more soluble Aβ40 and 5.6-fold more insoluble Aβ40 in the frontal lobe compared to NI-AD cases. In the temporal lobe of the SOLA-AD case, the soluble Aβ40 was 80-fold increased, and the insoluble Aβ40 was 13-fold more abundant compared to the non-immunized AD cases. Both soluble and insoluble Aβ42 levels were not dramatically different between the SOLA-AD and NI-AD cohort. Discussion: Solanezumab immunotherapy provided no apparent relief in the clinical evolution of dementia in this particular AD patient, since there was a continuous cognitive deterioration and full expression of amyloid deposition and neuropathology.
Language	English
Publishing date	2016-08-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	2695563-5
ISSN	2165-591X
ISSN	2165-591X
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Article: Of mice and men: The relevance of transgenic mice Abeta immunizations to Alzheimer's disease.

Roher, Alex E / Kokjohn, Tyler A

Journal of Alzheimer's disease : JAD

2002 Volume 4, Issue 5, Page(s) 431–434

MeSH term(s)	Alzheimer Disease/immunology ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/administration & dosage ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Antibodies/immunology ; Humans ; Immunization ; Mice ; Mice, Transgenic
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Antibodies
Language	English
Publishing date	2002-11-25
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/jad-2002-4509
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Article: An association with great implications: vascular pathology and Alzheimer disease.

Roher, Alex E / Kokjohn, Tyler A / Beach, Thomas G

Alzheimer disease and associated disorders

2006 Volume 20, Issue 1, Page(s) 73–75

MeSH term(s)	Alzheimer Disease/pathology ; Brain Ischemia/pathology ; Cerebral Amyloid Angiopathy/pathology ; Cerebral Arteries/pathology ; Circle of Willis/pathology ; Humans ; Intracranial Arteriosclerosis/pathology ; Myocardial Infarction/pathology ; Plaque, Amyloid/pathology ; Risk Factors ; Statistics as Topic
Language	English
Publishing date	2006-01
Publishing country	United States
Document type	Letter ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1002700-2
ISSN	1546-4156 ; 0893-0341
ISSN (online)	1546-4156
ISSN	0893-0341
DOI	10.1097/01.wad.0000201855.39246.2d
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Article: The effects of salt concentration and growth phase on MRSA solar and germicidal ultraviolet radiation resistance.

Sheldon, Jennifer L / Kokjohn, Tyler A / Martin, Eugene L

Ostomy/wound management

2005 Volume 51, Issue 1, Page(s) 36–8, 42–4, 46 passim

Abstract: The extensive use of antimicrobial drugs has led to the widespread emergence of resistant bacterial strains. One such organism, methicillin-resistant Staphylococcus aureus, is now found extensively in both healthcare facilities and diverse community ... ...

Abstract	The extensive use of antimicrobial drugs has led to the widespread emergence of resistant bacterial strains. One such organism, methicillin-resistant Staphylococcus aureus, is now found extensively in both healthcare facilities and diverse community settings such as households, correctional facilities, and athletic teams. The importance of ultraviolet radiation as an adjunctive therapy to reduce bioburden and improve wound status in patients has been documented. An in vitro study to assess the effects of different types of ultraviolet radiation on antibiotic-resistant strains was conducted to provide information that will aid in the development of rational UV irradiation medical protocols. Methicillin-resistant Staphylococcus aureus was found to be sensitive to both germicidal (ultraviolet C) and solar (ultraviolet A and B) ultraviolet radiation (ultraviolet C substantially more lethal). For both types of ultraviolet radiation, as the medium concentration of sodium chloride increased, the methicillin-resistant Staphylococcus aureus cells exhibited increased sensitivity. It also was shown for both types of ultraviolet radiation that kill curves were comparable for log and stationary phase methicillin-resistant Staphylococcus aureus cells. Photoreactivation was observed for Pseudomonas aeruginosa PAO-1 but not for methicillin-resistant Staphylococcus aureus when ultraviolet C was applied to log phase cells. The Gram-negative Pseudomonas aeruginosa PAO-1 was considerably more sensitive than the Gram-positive methicillin-resistant Staphylococcus aureus to ultraviolet C radiation. The experiments reveal that medium composition exerts a substantial effect on methicillin-resistant Staphylococcus aureus ultraviolet resistance and that this species lacks photoreactivation capacity. This suggests that in a clinical setting, eradication of the bacterium may be achieved at far lower doses of ultraviolet radiation than would be indicated by treatment protocols that do not account for ionic conditions.
MeSH term(s)	Body Burden ; Colony Count, Microbial ; Culture Media/chemistry ; Humans ; Infection Control/methods ; Infection Control/standards ; Methicillin Resistance ; Microbial Sensitivity Tests ; Pseudomonas aeruginosa/growth & development ; Pseudomonas aeruginosa/radiation effects ; Sodium Chloride/chemistry ; Staphylococcal Infections/microbiology ; Staphylococcal Infections/therapy ; Staphylococcus aureus/growth & development ; Staphylococcus aureus/radiation effects ; Ultraviolet Rays ; Wound Infection/microbiology ; Wound Infection/therapy
Chemical Substances	Culture Media ; Sodium Chloride (451W47IQ8X)
Language	English
Publishing date	2005-01
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Review
ZDB-ID	1089112-2
ISSN	1943-2720 ; 0889-5899
ISSN (online)	1943-2720
ISSN	0889-5899
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