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Article: Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer's disease and non-demented elderly subjects.

Castaño, Eduardo M / Roher, Alex E / Esh, Chera L / Kokjohn, Tyler A / Beach, Thomas

2006 Volume 28, Issue 2, Page(s) 155–163

Abstract: Objectives: Diagnostic tests able to reveal Alzheimer's disease (AD) in living patients before cognitive ability is destroyed are urgently needed. Such tests must distinguish AD from other dementia causes, as well as differentiate subtle changes ... ...

Abstract	Objectives: Diagnostic tests able to reveal Alzheimer's disease (AD) in living patients before cognitive ability is destroyed are urgently needed. Such tests must distinguish AD from other dementia causes, as well as differentiate subtle changes associated with normal aging from true pathology emergence. A single biomarker offering such diagnostic and prognostic capacities has eluded identification. Therefore, a valuable test for AD is likely to be based on a specific pattern of change in a set of proteins, rather than a single protein. Methods: We examined pooled cerebrospinal fluid (CSF) samples obtained from neuropathologically-confirmed AD (n=43) and non-demented control subjects (n=43) using 2-dimensional gel electrophoresis (2DE) proteomic methodology to detect differentially expressed proteins. Proteins exhibiting expression level differences between the pools were recovered and identified using matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry. Results: Five differentially-expressed proteins with potential roles in amyloid-beta metabolism and vascular and brain physiology [apolipoprotein A-1 (Apo A-1), cathepsin D (CatD), hemopexin (HPX), transthyretin (TTR), and two pigment epithelium-derived factor (PEDF) isoforms] were identified. Apo A-1, CatD and TTR were significantly reduced in the AD pool sample, while HPX and the PEDF isoforms were increased in AD CSF. Discussion: These results suggest that multi-factor proteomic pattern analysis of the CSF may provide a means to diagnose and assess AD.
MeSH term(s)	Aged ; Aged, 80 and over ; Aging/metabolism ; Alzheimer Disease/cerebrospinal fluid ; Alzheimer Disease/diagnosis ; Alzheimer Disease/physiopathology ; Amyloid beta-Peptides/metabolism ; Apolipoprotein A-I/analysis ; Apolipoprotein A-I/cerebrospinal fluid ; Biomarkers/analysis ; Biomarkers/cerebrospinal fluid ; Brain/metabolism ; Brain/pathology ; Brain/physiopathology ; Cathepsin D/analysis ; Cathepsin D/cerebrospinal fluid ; Electrophoresis, Gel, Two-Dimensional ; Eye Proteins/analysis ; Eye Proteins/cerebrospinal fluid ; Female ; Hemopexin/analysis ; Hemopexin/cerebrospinal fluid ; Humans ; Male ; Mass Spectrometry ; Nerve Growth Factors/analysis ; Nerve Growth Factors/cerebrospinal fluid ; Nerve Tissue Proteins/analysis ; Nerve Tissue Proteins/cerebrospinal fluid ; Prealbumin/analysis ; Prealbumin/cerebrospinal fluid ; Predictive Value of Tests ; Proteomics/methods ; Reference Values ; Serpins/analysis ; Serpins/cerebrospinal fluid
Chemical Substances	Amyloid beta-Peptides ; Apolipoprotein A-I ; Biomarkers ; Eye Proteins ; Nerve Growth Factors ; Nerve Tissue Proteins ; Prealbumin ; Serpins ; pigment epithelium-derived factor ; Hemopexin (9013-71-2) ; Cathepsin D (EC 3.4.23.5)
Language	English
Publishing date	2006-03
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	424428-x
ISSN	1743-1328 ; 0161-6412
ISSN (online)	1743-1328
ISSN	0161-6412
DOI	10.1179/016164106X98035
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Article: Presenilin-1 280Glu-->Ala mutation alters C-terminal APP processing yielding longer abeta peptides: implications for Alzheimer's disease.

Van Vickle, Gregory D / Esh, Chera L / Kokjohn, Tyler A / Patton, R Lyle / Kalback, Walter M / Luehrs, Dean C / Beach, Thomas G / Newel, Amanda J / Lopera, Francisco / Ghetti, Bernardino / Vidal, Ruben / Castaño, Eduardo M / Roher, Alex E

Molecular medicine (Cambridge, Mass.)

2008 Volume 14, Issue 3-4, Page(s) 184–194

Abstract: Presenilin (PS) mutations enhance the production of the Abeta42 peptide that is derived from the amyloid precursor protein (APP). The pathway(s) by which the Abeta42 species is preferentially produced has not been elucidated, nor is the mechanism by ... ...

Abstract	Presenilin (PS) mutations enhance the production of the Abeta42 peptide that is derived from the amyloid precursor protein (APP). The pathway(s) by which the Abeta42 species is preferentially produced has not been elucidated, nor is the mechanism by which PS mutations produce early-onset dementia established. Using a combination of histological, immunohistochemical, biochemical, and mass spectrometric methods, we examined the structural and morphological nature of the amyloid species produced in a patient expressing the PS1 280Glu-->Ala familial Alzheimer's disease mutation. Abundant diffuse plaques were observed that exhibited a staining pattern and morphology distinct from previously described PS cases, as well as discreet amyloid plaques within the white matter. In addition to finding increased amounts of CT99 and Abeta42 peptides, our investigation revealed the presence of a complex array of Abeta peptides substantially longer than 42/43 amino acid residue species. The increased hydrophobic nature of longer Abeta species retained within the membrane walls could impact the structure and function of plasma membrane and organelles. These C-terminally longer peptides may, through steric effects, dampen the rate of turnover by critical amyloid degrading enzymes such as neprilysin and insulin degrading enzyme. A complete understanding of the deleterious side effects of membrane bound Abeta as a consequence of gamma-secretase alterations is needed to understand Alzheimer's disease pathophysiology and will aid in the design of therapeutic interventions.
MeSH term(s)	Adult ; Aged ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/physiopathology ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Autopsy ; Chromatography ; Humans ; Male ; Mass Spectrometry ; Middle Aged ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Point Mutation ; Presenilin-1/genetics ; Presenilin-1/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Peptide Fragments ; Presenilin-1 ; amyloid beta-protein (1-42)
Language	English
Publishing date	2008-01-27
Publishing country	England
Document type	Case Reports ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1283676-x
ISSN	1076-1551
ISSN	1076-1551
DOI	10.2119/2007-00094.Van Vickle
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Article: Interaction of cardiovascular disease and neurodegeneration: transcranial Doppler ultrasonography and Alzheimer's disease.

Roher, Alex E / Garami, Zsolt / Alexandrov, Andrei V / Kokjohn, Tyler A / Esh, Chera L / Kalback, Walter M / Vedders, Linda J / Wilson, Jeffrey R / Sabbagh, Marwan N / Beach, Thomas G

Neurological research

2006 Volume 28, Issue 6, Page(s) 672–678

Abstract: Objective: Recent post-mortem studies have reported that the severity of atheromatous deposits in the circle of Willis is significantly greater, relative to non-demented (ND) elderly persons, in subjects with neuropathologically diagnosed Alzheimer's ... ...

Abstract	Objective: Recent post-mortem studies have reported that the severity of atheromatous deposits in the circle of Willis is significantly greater, relative to non-demented (ND) elderly persons, in subjects with neuropathologically diagnosed Alzheimer's disease (AD). Additionally, the severity of intracranial atherosclerosis correlates significantly with the densities of neuritic plaques and neurofibrillary tangles. In this study, we examine the arteries of the circle of Willis by transcranial Doppler (TCD) ultrasonography. Methods: TCD was used to measure, in 25 AD patients and 30 ND elderly subjects, mean flow velocities and pulsatility indices in 16 different segments of the circle of Willis. The data were compared with and without adjustment for age, gender and systolic blood pressure. Results: The AD patients had systematically higher pulsatility indices (p<0.005) than the ND group. Incremental increases of pulsatility indices in these segments had odds ratios ranging from 1.8 to 48 for the presence of AD when adjusted for age, gender and systolic blood pressure. The left internal carotid artery siphon and the left posterior cerebral artery were the two vessels that were strongly associated with AD diagnosis. Mean flow velocities were generally lower in patients with AD but the differences did not reach the significance level. Discussion: The pulsatility indices of the arteries of AD patients were generally greater than those of similarly-aged ND subjects. This difference is most likely due to increased arterial wall rigidity imposed by atherosclerotic changes. Atherosclerotic disease of intracranial arteries may be a risk factor for AD.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/complications ; Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/pathology ; Anterior Cerebral Artery/diagnostic imaging ; Cardiovascular Diseases/complications ; Cardiovascular Diseases/diagnostic imaging ; Cardiovascular Diseases/pathology ; Cerebrovascular Circulation ; Circle of Willis/diagnostic imaging ; Female ; Humans ; Male ; Nerve Degeneration/complications ; Nerve Degeneration/diagnostic imaging ; Nerve Degeneration/pathology ; Posterior Cerebral Artery/diagnostic imaging ; Ultrasonography, Doppler, Transcranial
Language	English
Publishing date	2006-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	424428-x
ISSN	1743-1328 ; 0161-6412
ISSN (online)	1743-1328
ISSN	0161-6412
DOI	10.1179/016164106X130470
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Zs.A 1491: Show issues

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Article ; Online: Tg-SwDI transgenic mice exhibit novel alterations in AbetaPP processing, Abeta degradation, and resilient amyloid angiopathy.

Van Vickle, Gregory D / Esh, Chera L / Daugs, Ian D / Kokjohn, Tyler A / Kalback, Walter M / Patton, R Lyle / Luehrs, Dean C / Walker, Douglas G / Lue, Lih-Fen / Beach, Thomas G / Davis, Judianne / Van Nostrand, William E / Castaño, Eduardo M / Roher, Alex E

The American journal of pathology

2008 Volume 173, Issue 2, Page(s) 483–493

Abstract: Alzheimer's disease (AD) is characterized by the accumulation of extracellular insoluble amyloid, primarily derived from polymerized amyloid-beta (Abeta) peptides. We characterized the chemical composition of the Abeta peptides deposited in the brain ... ...

Abstract	Alzheimer's disease (AD) is characterized by the accumulation of extracellular insoluble amyloid, primarily derived from polymerized amyloid-beta (Abeta) peptides. We characterized the chemical composition of the Abeta peptides deposited in the brain parenchyma and cerebrovascular walls of triple transgenic Tg-SwDI mice that produce a rapid and profuse Abeta accumulation. The processing of the N- and C-terminal regions of mutant AbetaPP differs substantially from humans because the brain parenchyma accumulates numerous, diffuse, nonfibrillar plaques, whereas the thalamic microvessels harbor overwhelming amounts of compact, fibrillar, thioflavine-S- and apolipoprotein E-positive amyloid deposits. The abundant accretion of vascular amyloid, despite low AbetaPP transgene expression levels, suggests that inefficient Abeta proteolysis because of conformational changes and dimerization may be key pathogenic factors in this animal model. The disruption of amyloid plaque cores by immunotherapy is accompanied by increased perivascular deposition in both humans and transgenic mice. This analogous susceptibility and response to the disruption of amyloid deposits suggests that Tg-SwDI mice provide an excellent model in which to study the functional aftermath of immunotherapeutic interventions. These mice might also reveal new avenues to promote amyloidogenic AbetaPP processing and fundamental insights into the faulty degradation and clearance of Abeta in AD, pivotal issues in understanding AD pathophysiology and the assessment of new therapeutic agents.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Apolipoproteins E/metabolism ; Benzothiazoles ; Cerebral Amyloid Angiopathy/metabolism ; Cerebral Amyloid Angiopathy/pathology ; Dimerization ; Disease Models, Animal ; Humans ; Mice ; Mice, Transgenic ; Plaque, Amyloid/metabolism ; Plaque, Amyloid/pathology ; Protein Conformation ; Thiazoles/metabolism
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Apolipoproteins E ; Benzothiazoles ; Thiazoles ; thioflavin T (2390-54-7)
Language	English
Publishing date	2008-07-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2943-9
ISSN	1525-2191 ; 0002-9440
ISSN (online)	1525-2191
ISSN	0002-9440
DOI	10.2353/ajpath.2008.071191
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Article: TgCRND8 amyloid precursor protein transgenic mice exhibit an altered gamma-secretase processing and an aggressive, additive amyloid pathology subject to immunotherapeutic modulation.

Van Vickle, Gregory D / Esh, Chera L / Kalback, Walter M / Patton, R Lyle / Luehrs, Dean C / Kokjohn, Tyler A / Fifield, Frederick G / Fraser, Paul E / Westaway, David / McLaurin, Joanne / Lopez, John / Brune, Daniel / Newel, Amanda J / Poston, Marissa / Beach, Thomas G / Roher, Alex E

Biochemistry

2007 Volume 46, Issue 36, Page(s) 10317–10327

Abstract: We investigated the morphology and biochemistry of the amyloid-beta (Abeta) peptides produced in TgCRND8 Tg mice carrying combined amyloid precursor protein (APP) Swedish (K670M/N671L) and Indiana (V717F) mutations. Histological analyses employing ... ...

Abstract	We investigated the morphology and biochemistry of the amyloid-beta (Abeta) peptides produced in TgCRND8 Tg mice carrying combined amyloid precursor protein (APP) Swedish (K670M/N671L) and Indiana (V717F) mutations. Histological analyses employing amyloid-specific staining and electron microscopy revealed that the TgCRND8 Tg mice produce an aggressive pathology, evident as early as 3 months of age, that is a composite of core plaques and peculiar floccular diffuse parenchymal deposits. The Abeta peptides were purified using combined FPLC-HPLC, Western blots, and immunoprecipitation methods and characterized by MALDI-TOF/SELDI-TOF mass spectrometry. The C-terminal APP peptides, assessed by Western blot experiments and mass spectrometry, suggested an alteration in the order of secretase processing, yielding a C-terminal fragment pattern that is substantially different from that observed in sporadic Alzheimer's disease (AD). This modified processing pattern generated longer Abeta peptides, as well as those ending at residues 40/42/43, which may partially explain the early onset and destructive nature of familial AD caused by APP mutations. Despite an aggressive pathology that extended to the cerebellum and white matter, these animals tolerated the presence of an imposing amount of Abeta load. Abeta immunization resulted in an impressive 7-fold reduction in the number of amyloid core plaques and, as previously demonstrated, a significant memory recovery. However, given the phylogenetic distance and the differences in APP processing and Abeta chemistry between Tg mice and AD, caution should be applied in projecting mouse therapeutic interventions onto human subjects.
MeSH term(s)	Alzheimer Disease/pathology ; Alzheimer Disease/therapy ; Amino Acid Sequence ; Amyloid/ultrastructure ; Amyloid Precursor Protein Secretases/metabolism ; Amyloid beta-Protein Precursor/chemistry ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Brain/metabolism ; Brain/pathology ; Chromatography, High Pressure Liquid ; Immunotherapy ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Plaque, Amyloid/pathology ; Plaque, Amyloid/ultrastructure ; Protein Processing, Post-Translational ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Thiazoles/metabolism
Chemical Substances	Amyloid ; Amyloid beta-Protein Precursor ; Thiazoles ; thioflavin T (2390-54-7) ; Amyloid Precursor Protein Secretases (EC 3.4.-)
Language	English
Publishing date	2007-09-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi700951u
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Article: Amyloid-beta peptide remnants in AN-1792-immunized Alzheimer's disease patients: a biochemical analysis.

Patton, R Lyle / Kalback, Walter M / Esh, Chera L / Kokjohn, Tyler A / Van Vickle, Gregory D / Luehrs, Dean C / Kuo, Yu-Min / Lopez, John / Brune, Daniel / Ferrer, Isidro / Masliah, Eliezer / Newel, Amanda J / Beach, Thomas G / Castaño, Eduardo M / Roher, Alex E

The American journal of pathology

2006 Volume 169, Issue 3, Page(s) 1048–1063

Abstract: Experiments with amyloid-beta (Abeta)-42-immunized transgenic mouse models of Alzheimer's disease have revealed amyloid plaque disruption and apparent cognitive function recovery. Neuropathological examination of patients vaccinated against purified ... ...

Abstract	Experiments with amyloid-beta (Abeta)-42-immunized transgenic mouse models of Alzheimer's disease have revealed amyloid plaque disruption and apparent cognitive function recovery. Neuropathological examination of patients vaccinated against purified Abeta-42 (AN-1792) has demonstrated that senile plaque disruption occurred in immunized humans as well. Here, we examined tissue histology and quantified and biochemically characterized the remnant amyloid peptides in the gray and white matter and leptomeningeal/cortical vessels of two AN-1792-vaccinated patients, one of whom developed meningoencephalitis. Compact core and diffuse amyloid deposits in both vaccinated individuals were focally absent in some regions. Although parenchymal amyloid was focally disaggregated, vascular deposits were relatively preserved or even increased. Immunoassay revealed that total soluble amyloid levels were sharply elevated in vaccinated patient gray and white matter compared with Alzheimer's disease cases. Our experiments suggest that although immunization disrupted amyloid deposits, vascular capture prevented large-scale egress of Abeta peptides. Trapped, solubilized amyloid peptides may ultimately have cascading toxic effects on cerebrovascular, gray and white matter tissues. Anti-amyloid immunization may be most effective not as therapeutic or mitigating measures but as a prophylactic measure when Abeta deposition is still minimal. This may allow Abeta mobilization under conditions in which drainage and degradation of these toxic peptides is efficient.
MeSH term(s)	Aged ; Alzheimer Disease/immunology ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/therapy ; Alzheimer Vaccines/administration & dosage ; Alzheimer Vaccines/adverse effects ; Alzheimer Vaccines/immunology ; Amyloid beta-Peptides/immunology ; Amyloid beta-Peptides/metabolism ; Animals ; Cerebral Cortex/blood supply ; Cerebral Cortex/metabolism ; Cerebral Cortex/pathology ; Humans ; Immunization/adverse effects ; Male ; Meningoencephalitis/etiology ; Meningoencephalitis/metabolism ; Meningoencephalitis/pathology ; Mice ; Mice, Transgenic
Chemical Substances	Alzheimer Vaccines ; Amyloid beta-Peptides
Language	English
Publishing date	2006-08-23
Publishing country	United States
Document type	Case Reports ; Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2943-9
ISSN	1525-2191 ; 0002-9440
ISSN (online)	1525-2191
ISSN	0002-9440
DOI	10.2353/ajpath.2006.060269
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Article ; Online: Amyloid beta peptides in human plasma and tissues and their significance for Alzheimer's disease.

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

2008 Volume 5, Issue 1, Page(s) 18–29

Abstract: Background: We evaluated the amounts of amyloid beta (Abeta)) peptides in the central nervous system (CNS) and in reservoirs outside the CNS and their potential impact on Abeta plasma levels and Alzheimer's disease (AD) pathology.: Methods: Amyloid ... ...

Abstract	Background: We evaluated the amounts of amyloid beta (Abeta)) peptides in the central nervous system (CNS) and in reservoirs outside the CNS and their potential impact on Abeta plasma levels and Alzheimer's disease (AD) pathology. Methods: Amyloid beta levels were measured in (1) the plasma of AD and nondemented (ND) controls in a longitudinal study, (2) the plasma of a cohort of AD patients receiving a cholinesterase inhibitor, and (3) the skeletal muscle, liver, aorta, platelets, leptomeningeal arteries, and in gray and white matter of AD and ND control subjects. Results: Plasma Abeta levels fluctuated over time and among individuals, suggesting continuous contributions from brain and peripheral tissues and associations with reactive circulating proteins. Arteries with atherosclerosis had larger amounts of Abeta40 than disease-free vessels. Inactivated platelets contained more Abeta peptides than activated ones. Substantially more Abeta was present in liver samples from ND patients. Overall, AD brain and skeletal muscle contained increased levels of Abeta. Conclusions: Efforts to use plasma levels of Abeta peptides as AD biomarkers or disease-staging scales have failed. Peripheral tissues might contribute to both the circulating amyloid pool and AD pathology within the brain and its vasculature. The wide spread of plasma Abeta values is also due in part to the ability of Abeta to bind to a variety of plasma and membrane proteins. Sources outside the CNS must be accounted for because pharmacologic interventions to reduce cerebral amyloid are assessed by monitoring Abeta plasma levels. Furthermore, the long-range impact of Abeta immunotherapy on peripheral Abeta sources should also be considered.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/blood ; Amyloid beta-Peptides/metabolism ; Aorta/metabolism ; Biomarkers/blood ; Biomarkers/metabolism ; Blood Platelets/metabolism ; Brain/metabolism ; Cholinesterase Inhibitors/therapeutic use ; Female ; Humans ; Liver/metabolism ; Longitudinal Studies ; Male ; Meningeal Arteries/metabolism ; Middle Aged ; Muscle, Skeletal/metabolism
Chemical Substances	Amyloid beta-Peptides ; Biomarkers ; Cholinesterase Inhibitors
Language	English
Publishing date	2008-12-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1016/j.jalz.2008.10.004
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Article: Comparative proteomics of cerebrospinal fluid in neuropathologically-confirmed Alzheimer's disease and non-demented elderly subjects.

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Article: Presenilin-1 280Glu-->Ala mutation alters C-terminal APP processing yielding longer abeta peptides: implications for Alzheimer's disease.

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Article: Interaction of cardiovascular disease and neurodegeneration: transcranial Doppler ultrasonography and Alzheimer's disease.

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Article ; Online: Tg-SwDI transgenic mice exhibit novel alterations in AbetaPP processing, Abeta degradation, and resilient amyloid angiopathy.

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Article: TgCRND8 amyloid precursor protein transgenic mice exhibit an altered gamma-secretase processing and an aggressive, additive amyloid pathology subject to immunotherapeutic modulation.

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Article: Amyloid-beta peptide remnants in AN-1792-immunized Alzheimer's disease patients: a biochemical analysis.

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Article ; Online: Amyloid beta peptides in human plasma and tissues and their significance for Alzheimer's disease.

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