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Article ; Online: Multi-omics and Alzheimer's disease: a slower but surer path to an efficacious therapy?

Pimplikar, Sanjay W

American journal of physiology. Cell physiology

2017 Volume 313, Issue 1, Page(s) C1–C2

MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/therapy ; Brain/metabolism ; Genomics/methods ; Humans ; Metabolomics/methods ; Proteomics/methods ; Treatment Outcome
Language	English
Publishing date	2017-05-17
Publishing country	United States
Document type	Editorial
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00109.2017
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Article ; Online: Neuroinflammation in Alzheimer's disease: from pathogenesis to a therapeutic target.

Pimplikar, Sanjay W

Journal of clinical immunology

2014 Volume 34 Suppl 1, Page(s) S64–9

Abstract: The top-down, reductionist approach of the past three decades has resulted in remarkable progress in identifying genes and proteins involved in Alzheimer's disease (AD), including β-amyloid (Aβ) peptides and tau protein. Recently, a number of genes of ... ...

Abstract	The top-down, reductionist approach of the past three decades has resulted in remarkable progress in identifying genes and proteins involved in Alzheimer's disease (AD), including β-amyloid (Aβ) peptides and tau protein. Recently, a number of genes of the innate immune pathway have been identified as AD risk factors and several microglial proteins have been shown to be chronically activated in AD brains. Together, these observations suggest a crucial role for neuroinflammation in AD pathogenesis and emerging evidence suggests that neuroinflammation is both a cause and a consequence of AD. Epidemiological studies show that long-term users of anti-inflammatory drugs are protected from AD but anti-inflammatory treatment in mild AD patients has not been successful. These observations suggest that anti-inflammatory treatment is likely to be successful if initiated prior to the onset of neurological symptoms. Finally, after the remarkable success of the reductionist approach, a complimentary bottom-up systems approach is necessary to gain a better understanding of the highly complex, multifactorial nature of AD pathogenesis.
MeSH term(s)	Alzheimer Disease/immunology ; Alzheimer Disease/therapy ; Amyloid beta-Peptides/immunology ; Animals ; Anti-Inflammatory Agents/therapeutic use ; Humans ; Immunity, Innate ; Immunotherapy/methods ; Molecular Targeted Therapy ; Neurogenic Inflammation ; tau Proteins/immunology
Chemical Substances	Amyloid beta-Peptides ; Anti-Inflammatory Agents ; tau Proteins
Language	English
Publishing date	2014-04-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	779361-3
ISSN	1573-2592 ; 0271-9142
ISSN (online)	1573-2592
ISSN	0271-9142
DOI	10.1007/s10875-014-0032-5
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Article ; Online: Clinical and biomarker changes in Alzheimer's disease.

Pimplikar, Sanjay W

The New England journal of medicine

2012 Volume 367, Issue 21, Page(s) 2050–1; author reply 2051–2

MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Cerebrospinal Fluid/metabolism ; Female ; Humans ; Male
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2012-11-22
Publishing country	United States
Document type	Comment ; Letter
ZDB-ID	207154-x
ISSN	1533-4406 ; 0028-4793
ISSN (online)	1533-4406
ISSN	0028-4793
DOI	10.1056/NEJMc1211767#SA2
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Article ; Online: Impairment of the Ubiquitin-Proteasome System in Ageing?

Sanjay W Pimplikar

Proceedings of Indian National Science Academy, Vol 69, Iss 2B (2015)

2015

Abstract: Impairment of the Ubiquitin-Proteasome System in Ageing? ...

Abstract	Impairment of the Ubiquitin-Proteasome System in Ageing?
Keywords	Science ; Q
Language	English
Publishing date	2015-02-01T00:00:00Z
Publisher	Indian National Science Academy
Document type	Article ; Online
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Article ; Online: Reassessing the amyloid cascade hypothesis of Alzheimer's disease.

Pimplikar, Sanjay W

The international journal of biochemistry & cell biology

2008 Volume 41, Issue 6, Page(s) 1261–1268

Abstract: Since its inception, the amyloid cascade hypothesis has dominated the field of Alzheimer's disease (AD) research and has provided the intellectual framework for therapeutic intervention. Although the details of the hypothesis continue to evolve, its core ...

Abstract	Since its inception, the amyloid cascade hypothesis has dominated the field of Alzheimer's disease (AD) research and has provided the intellectual framework for therapeutic intervention. Although the details of the hypothesis continue to evolve, its core principle has remained essentially unaltered. It posits that the amyloid-beta peptides, derived from amyloid precursor protein (APP), are the root cause of AD. Substantial genetic and biochemical data support this view, and yet a number of findings also run contrary to its tenets. The presence of familial AD mutations in APP and presenilins, demonstration of Abeta toxicity, and studies in mouse models of AD all support the hypothesis, whereas the presence of Abeta plaques in normal individuals, the uncertain nature of the pathogenic Abeta species, and repeated disappointments with Abeta-centered therapeutic trials are inconsistent with the hypothesis. The current state of knowledge does not prove nor disprove the amyloid hypothesis, but rather points to the need for its reassessment. A view that Abeta is one of the factors, as opposed to the factor, that causes AD is more consistent with the present knowledge, and is more likely to promote comprehensive and effective therapeutic strategies.
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Humans ; Mice
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
Language	English
Publishing date	2008-12-30
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2008.12.015
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Article ; Online: Knockdown of amyloid precursor protein in zebrafish causes defects in motor axon outgrowth.

Song, Ping / Pimplikar, Sanjay W

PloS one

2012 Volume 7, Issue 4, Page(s) e34209

Abstract: Amyloid precursor protein (APP) plays a pivotal role in Alzheimer's disease (AD) pathogenesis, but its normal physiological functions are less clear. Combined deletion of the APP and APP-like protein 2 (APLP2) genes in mice results in post-natal ... ...

Abstract	Amyloid precursor protein (APP) plays a pivotal role in Alzheimer's disease (AD) pathogenesis, but its normal physiological functions are less clear. Combined deletion of the APP and APP-like protein 2 (APLP2) genes in mice results in post-natal lethality, suggesting that APP performs an essential, if redundant, function during embryogenesis. We previously showed that injection of antisense morpholino to reduce APP levels in zebrafish embryos caused convergent-extension defects. Here we report that a reduction in APP levels causes defective axonal outgrowth of facial branchiomotor and spinal motor neurons, which involves disorganized axonal cytoskeletal elements. The defective outgrowth is caused in a cell-autonomous manner and both extracellular and intracellular domains of human APP are required to rescue the defective phenotype. Interestingly, wild-type human APP rescues the defective phenotype but APPswe mutation, which causes familial AD, does not. Our results show that the zebrafish model provides a powerful system to delineate APP functions in vivo and to study the biological effects of APP mutations.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/therapeutic use ; Animals ; Axons/metabolism ; Axons/pathology ; Cells, Cultured ; Gene Expression Regulation, Developmental ; Gene Knockdown Techniques ; Humans ; Motor Neurons/metabolism ; Motor Neurons/pathology ; Mutation ; Phenotype ; Zebrafish/embryology ; Zebrafish/genetics
Chemical Substances	Amyloid beta-Protein Precursor
Language	English
Publishing date	2012-04-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0034209
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Article ; Online: Amyloid precursor protein: more than just neurodegeneration.

Pimplikar, Sanjay W / Ghosal, Kaushik

Stem cell research & therapy

2011 Volume 2, Issue 5, Page(s) 39

Abstract: Amyloid precursor protein (APP) fascinates cell biologists because it is proteolytically processed to generate multiple peptides, including amyloid-β, which is implicated in Alzheimer's disease. However, a large body of data also shows that the ... ...

Abstract	Amyloid precursor protein (APP) fascinates cell biologists because it is proteolytically processed to generate multiple peptides, including amyloid-β, which is implicated in Alzheimer's disease. However, a large body of data also shows that the extracellular soluble fragment of APP produced by α-secretase (sAPPα) is neuroprotective and promotes neuronal outgrowth. A study by Demars and colleagues appearing in the previous issue provides data showing that sAPPα is a general growth factor for stem cells of multiple lineages. Thus, APP seems to play complex and disparate roles in neurodegeneration and neuroprotection.
MeSH term(s)	Amyloid Precursor Protein Secretases/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Humans ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neurons/metabolism ; Stem Cells/cytology ; Stem Cells/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Amyloid Precursor Protein Secretases (EC 3.4.-)
Language	English
Publishing date	2011-10-14
Publishing country	England
Document type	Editorial ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2548671-8
ISSN	1757-6512 ; 1757-6512
ISSN (online)	1757-6512
ISSN	1757-6512
DOI	10.1186/scrt80
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Article ; Online: Detection of APP intracellular domain in brain tissue.

Pimplikar, Sanjay W / Suryanarayana, Anupama

Methods in molecular biology (Clifton, N.J.)

2011 Volume 670, Page(s) 85–91

Abstract: The cleavage of amyloid precursor protein (APP) by γ-secretase produces Aβ peptides, which are prominent features in Alzheimer's disease and have been extensively studied. By contrast, APP intracellular domain (AICD), also a product of this cleavage ... ...

Abstract	The cleavage of amyloid precursor protein (APP) by γ-secretase produces Aβ peptides, which are prominent features in Alzheimer's disease and have been extensively studied. By contrast, APP intracellular domain (AICD), also a product of this cleavage event, has received little or no investigative attention. A major reason for this is that AICD is generally not detected in tissue lysates and, therefore, is neglected as a non-relevant product of APP metabolism. However, recent studies have shown that AICD regulates a number of important cellular events. Furthermore, we found that contrary to previous assertions, AICD can be detected in brain lysates using Western blotting if an antigen retrieval protocol is employed. Here we describe the protocol for AICD detection and note the biological relevance of AICD in physiological and pathological conditions.
MeSH term(s)	Amyloid beta-Protein Precursor/metabolism ; Animals ; Blotting, Western ; Brain/metabolism ; Electrophoresis, Polyacrylamide Gel ; Mice ; Mice, Transgenic ; Protein Structure, Tertiary
Chemical Substances	Amyloid beta-Protein Precursor
Language	English
Publishing date	2011
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-60761-744-0_7
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Article ; Online: Tau Protein Mediates APP Intracellular Domain (AICD)-Induced Alzheimer's-Like Pathological Features in Mice.

Ghosal, Kaushik / Fan, Qingyuan / Dawson, Hana N / Pimplikar, Sanjay W

PloS one

2016 Volume 11, Issue 7, Page(s) e0159435

Abstract: Amyloid precursor protein (APP) is cleaved by gamma-secretase to simultaneously generate amyloid beta (Aβ) and APP Intracellular Domain (AICD) peptides. Aβ plays a pivotal role in Alzheimer's disease (AD) pathogenesis but recent studies suggest that ... ...

Abstract	Amyloid precursor protein (APP) is cleaved by gamma-secretase to simultaneously generate amyloid beta (Aβ) and APP Intracellular Domain (AICD) peptides. Aβ plays a pivotal role in Alzheimer's disease (AD) pathogenesis but recent studies suggest that amyloid-independent mechanisms also contribute to the disease. We previously showed that AICD transgenic mice (AICD-Tg) exhibit AD-like features such as tau pathology, aberrant neuronal activity, memory deficits and neurodegeneration in an age-dependent manner. Since AD is a tauopathy and tau has been shown to mediate Aβ-induced toxicity, we examined the role of tau in AICD-induced pathological features. We report that ablating endogenous tau protects AICD-Tg mice from deficits in adult neurogenesis, seizure severity, short-term memory deficits and neurodegeneration. Deletion of tau restored abnormal phosphorylation of NMDA receptors, which is likely to underlie hyperexcitability and associated excitotoxicity in AICD-Tg mice. Conversely, overexpression of wild-type human tau aggravated receptor phosphorylation, impaired adult neurogenesis, memory deficits and neurodegeneration. Our findings show that tau is essential for mediating the deleterious effects of AICD. Since tau also mediates Aβ-induced toxic effects, our findings suggest that tau is a common downstream factor in both amyloid-dependent and-independent pathogenic mechanisms and therefore could be a more effective drug target for therapeutic intervention in AD.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/psychology ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/chemistry ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Disease Models, Animal ; Female ; Gene Expression ; Gene Knockout Techniques ; Humans ; Kainic Acid/adverse effects ; Lithium/pharmacology ; Male ; Maze Learning ; Memory, Short-Term ; Mice ; Mice, Transgenic ; Neurogenesis/drug effects ; Neurogenesis/genetics ; Neurons/metabolism ; Neurons/pathology ; Phenotype ; Phosphorylation/drug effects ; Protein Interaction Domains and Motifs ; Receptors, N-Methyl-D-Aspartate/metabolism ; Seizures/chemically induced ; Seizures/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; NR2B NMDA receptor ; Receptors, N-Methyl-D-Aspartate ; tau Proteins ; Lithium (9FN79X2M3F) ; Kainic Acid (SIV03811UC)
Language	English
Publishing date	2016-07-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0159435
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Article ; Online: Knockdown of amyloid precursor protein in zebrafish causes defects in motor axon outgrowth.

Ping Song / Sanjay W Pimplikar

PLoS ONE, Vol 7, Iss 4, p e

2012 Volume 34209

Abstract	Amyloid precursor protein (APP) plays a pivotal role in Alzheimer's disease (AD) pathogenesis, but its normal physiological functions are less clear. Combined deletion of the APP and APP-like protein 2 (APLP2) genes in mice results in post-natal lethality, suggesting that APP performs an essential, if redundant, function during embryogenesis. We previously showed that injection of antisense morpholino to reduce APP levels in zebrafish embryos caused convergent-extension defects. Here we report that a reduction in APP levels causes defective axonal outgrowth of facial branchiomotor and spinal motor neurons, which involves disorganized axonal cytoskeletal elements. The defective outgrowth is caused in a cell-autonomous manner and both extracellular and intracellular domains of human APP are required to rescue the defective phenotype. Interestingly, wild-type human APP rescues the defective phenotype but APPswe mutation, which causes familial AD, does not. Our results show that the zebrafish model provides a powerful system to delineate APP functions in vivo and to study the biological effects of APP mutations.
Keywords	Medicine ; R ; Science ; Q
Subject code	616 ; 572
Language	English
Publishing date	2012-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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