DUBLIN, Ireland, March 12, 2018 (GLOBE NEWSWIRE)
-- Prothena Corporation plc (Nasdaq:PRTA), a late-stage clinical
biotechnology company focused on the discovery, development and
commercialization of novel therapies in the neuroscience and orphan
categories, today announced that it will present new research in
both AL and ATTR amyloidosis at the 16th International Symposium on
Amyloidosis (ISA), to be held March 26 to 29 in Kumamoto,
Japan.
"Prothena is committed to conducting, presenting
and publishing innovative research that advances our understanding
of the underlying pathophysiology in systemic amyloidoses to
support the development of potential treatments for patients," said
Wagner Zago, Ph.D., Chief Scientific Officer of Prothena. "We look
forward to presenting a broad range of our research in both AL and
ATTR amyloidosis at ISA, including preclinical research that
provides new insights into the mechanism of action for NEOD001, a
potential treatment for AL amyloidosis and its ability to recognize
a cryptic epitope that is exposed on both kappa and lambda
light chains from even the earliest stages of the misfolding and
aggregation process. In addition, we will share data that further
describes PRX004, our investigational antibody for the treatment of
ATTR amyloidosis, including a highly specific assay we have
developed to measure the misfolded forms of TTR protein present in
plasma of patients with hereditary ATTR amyloidosis."
New research will be presented demonstrating that
NEOD001 binds to both soluble and insoluble aggregated kappa and
lambda light chains and recognizes an epitope that is exposed
during even the earliest stages of abnormal light chain misfolding
and aggregation involved in AL amyloidosis. In addition,
preclinical data will be presented that provides further insight
into how the toxicity induced by light-chains can modulate
NT-proBNP production in AL amyloidosis, which is unique from other
forms of heart failure, and offers support for the relationship
that has been reported between lowering of NT-proBNP and improved
survival in patients with AL amyloidosis. These presentations will
occur in the following poster sessions:
(Abstract #PC095) NEOD001 Binds a
Wide Repertoire of Light Chain Sequences and Aggregation States
Found in AL Amyloidosis
- Presenter: Wagner Zago, PhD,
Chief Scientific Officer, Prothena
- Date and Time: March 28,
1:00-2:00 PM JST
- Location: Poster Hall
(Abstract #PB069) Aggregated
Light Chain Increases Brain Natriuretic Peptide Production and
Induces Oxidative Stress Response in Cardiomyocytes
- Presenter: Stephen J. Tam, PhD,
Senior Scientist, Prothena
- Date and Time: March 27,
1:00-2:00 PM JST
- Location: Poster Hall
Additional research related to PRX004 will be
presented, including a proprietary assay that specifically detects
circulating misfolded-hATTR in plasma across multiple TTR mutations
using a TTR antibody that binds to an epitope uniquely exposed on
misfolded TTR but hidden in the native tetramer. Such an assay has
the potential to be used as a diagnostic that can detect misfolded
TTR in the plasma of patients with hereditary ATTR amyloidosis.
Additional preclinical research will be presented showing that
conformation-specific antibodies target misfolded TTR and immune
mediated clearance of amyloid through phagocytosis. These
presentations will occur in the following oral and poster
sessions:
(Abstract #PB052) Detection of
Misfolded Forms of TTR in Plasma from Patients with Hereditary ATTR
Using Conformation-specific TTR Antibodies
- Presenter: Jeffrey N. Higaki PhD,
Director, Biochemistry, Prothena
- Date and Time: March 27,
8:20-8:30 AM JST (oral)
- Date and Time: March 27,
1:00-2:00 PM JST (poster)
- Location: Poster Hall
(Abstract #PC009) In Vivo Target
Engagement and Phagocytosis of Aggregated TTR by a
Conformation-specific TTR Antibody
- Presenter: Jeffrey N. Higaki,
PhD, Director, Biochemistry, Prothena
- Date and Time: March 28,
1:00-2:00 PM JST
- Location: Poster Hall
Presentations on Quality of life, health economics
and epidemiology research in patients with AL amyloidosis,
including real world data elucidating the burden of disease from
delayed diagnosis to substantial comorbidities and healthcare
resource use, will also be presented in the following poster
sessions:
(Abstract #PA085) A Mixed Methods
Study of the Journey to Diagnosis Among Patients with Light Chain
Amyloidosis
- Presenter: Tiffany P. Quock, PhD,
MS, Senior Director, Health Economics and Outcomes Research,
Prothena
- Date and Time: March 26,
1:30-2:30 PM JST
- Location: Poster Hall
(Abstract #PA086)
Real-world Burden of Comorbidities in Patients with Newly Diagnosed
AL Amyloidosis
- Presenter: Tiffany P. Quock, PhD, MS, Senior
Director, Health Economics and Outcomes Research, Prothena
- Date and Time: March 26,
1:30-2:30 PM JST
- Location: Poster Hall
(Abstract #PA087) Real-world
Healthcare Utilization and Costs in Patients with Newly Diagnosed
AL Amyloidosis
- Presenter: Tiffany P. Quock, PhD,
MS, Senior Director, Health Economics and Outcomes Research,
Prothena
- Date and Time: March 26,
1:30-2:30 PM JST
- Location: Poster Hall
(Abstract #PC070)
Epidemiology of AL Amyloidosis in US Commercially Insured
Population
- Presenter: Tiffany P. Quock, PhD,
MS, Senior Director, Health Economics and Outcomes Research,
Prothena
- Date and Time: March 28,
1:00-2:00 PM JST
- Location: Poster Hall
About AL and ATTR
Amyloidosis
Systemic amyloidoses are a complex group of
diseases caused by tissue deposition of misfolded proteins that
result in progressive organ damage.
Amyloid light chain amyloidosis (AL amyloidosis),
the most common type, is a rare, progressive, and typically fatal
protein misfolding disease caused by extracellular deposition of
aggregated immunoglobulin light chains. An excess of light chains
prone to misfolding are produced by clonal plasma
cells. Soluble toxic aggregates and deposited fibrils
(amyloid) lead to progressive failure of vital organs including the
heart, kidneys and nervous system, causing significant morbidity
and mortality. It is estimated that approximately 30,000 - 45,000
patients in the U.S. and Europe suffer from this disease. There are
no approved treatments for AL amyloidosis, although patients may be
treated with off-label therapies directed at the plasma cell
dyscrasia. There is a large unmet need for therapies that
specifically target soluble toxic aggregates and deposited fibrils,
thereby improving vital organ function.
Transthyretin amyloidosis (ATTR amyloidosis) is a
rare, progressive and often fatal disease characterized by
deposition of aggregates of misfolded protein, or amyloid. There
are three types of ATTR amyloidosis: hereditary ATTR with
cardiomyopathy (hATTR-CM); wild-type ATTR (wtATTR) which occurs
sporadically and also involves cardiomyopathy; and hereditary ATTR
with polyneuropathy (hATTR-PN). The TTR protein is produced
primarily in the liver and in its normal tetrameric form serves as
a carrier for thyroxin and vitamin A. In hereditary hATTR-PN and
hATTR-CM the body makes a mutant form of the TTR protein. There are
more than 100 reported types of TTR mutations that promote amyloid
fibril formation, which most commonly affect the heart (hATTR-CM)
and nervous system (hATTR-PN). Wild-type ATTR (wtATTR) is similar
to hereditary ATTR except that the protein that is deposited is the
misfolded, non-mutated transthyretin protein.
For more information on AL and ATTR amyloidosis,
please visit the websites of the Amyloidosis Support
Groups, The Amyloidosis Research Consortium, and
the Amyloidosis Foundation.
About NEOD001
NEOD001 is an investigational first-in-class
antibody that specifically targets disease-causing misfolded light
chain aggregates in AL amyloidosis. There are two ongoing global
clinical studies for NEOD001. The PRONTO study, a global, Phase 2b,
double-blind, placebo-controlled, registration-directed study, will
evaluate NEOD001 vs. placebo in previously-treated patients with AL
amyloidosis and persistent cardiac dysfunction, and will assess
best response over 12 months of the cardiac biomarker NT-proBNP,
defined by the consensus criteria of NT-proBNP change, in addition
to other biomarker, quality of life and functional endpoints.
The VITAL Amyloidosis Study, a global, Phase 3, double-blind,
placebo-controlled, registrational study, is evaluating NEOD001 vs.
placebo in newly-diagnosed, treatment-naïve patients with AL
amyloidosis and cardiac dysfunction, with both arms of the study
receiving standard of care. The VITAL study will assess a composite
endpoint of all-cause mortality or cardiac hospitalizations in
addition to biomarker, quality of life and functional endpoints.
More information on the PRONTO study and The VITAL Amyloidosis
Study is available at www.clinicaltrials.gov, by searching NCT
#02632786 for PRONTO, and NCT #02312206 for VITAL
or www.clinicaltrialsregister.eu, by searching
EudraCT #2015-004318-14 for PRONTO, and EudraCT
#2014-003865-11 for VITAL.
About PRX004
PRX004 is a monoclonal antibody designed to
specifically target and clear the misfolded forms of the amyloid
TTR protein found in both hereditary (hATTR-CM and hATTR-PN) and
wild type (wtATTR) ATTR amyloidosis, and leave the native form of
the protein unaffected. Currently in preclinical development,
Prothena plans to advance PRX004 into the clinic as a potential
therapy for ATTR amyloidosis.
About Prothena
Prothena Corporation plc is a global, late-stage
clinical biotechnology company establishing fully integrated
research, development and commercial capabilities and focused on
advancing new therapies in the neuroscience and orphan categories.
Fueled by its deep scientific understanding built over decades of
research in protein misfolding, Prothena seeks to fundamentally
change the course of grave or currently untreatable diseases
associated with this biology. Prothena's pipeline of antibody
therapeutic candidates targets a number of indications including AL
amyloidosis (NEOD001), Parkinson's disease and other related
synucleinopathies (PRX002/RG7935) and ATTR amyloidosis (PRX004).
The Company continues to advance additional discovery programs
against targets including tau, A beta (Amyloid beta) and
ALECT2 where its deep scientific understanding of disease pathology
can be leveraged. For more information, please visit the Company's
website at www.prothena.com.
Forward-looking
Statements
This press release contains
forward-looking statements. These statements relate to, among other
things, the proposed mechanism of action
of NEOD001; the relationship between NT-proBNP and survival in
patients with AL amyloidosis; the proposed mechanism of action of
PRX004; the potential of our proprietary assay to be used as a
diagnostic to detect misfolded TTR in patients with hereditary ATTR
amyloidosis; the expected timing of advancing PRX004 into clinical
development; and whether we can continue to advance additional
discovery programs. These statements are based on estimates,
projections and assumptions that may prove not to be accurate, and
actual results could differ materially from those anticipated due
to known and unknown risks, uncertainties and other factors,
including but not limited to the risks, uncertainties and other
factors described in the "Risk Factors" sections of our Annual
Report on Form 10-K filed with the Securities and Exchange
Commission (SEC) on February 26, 2018 and our subsequent Quarterly
Reports on Form 10-Q filed with the SEC. Prothena undertakes no
obligation to update publicly any forward-looking statements
contained in this press release as a result of new information,
future events or changes in Prothena's expectations.
Investor and Media
Contact:
Media: Ellen Rose, Head of
Communications
650-922-2405, ellen.rose@prothena.com
This
announcement is distributed by Nasdaq Corporate Solutions on behalf
of Nasdaq Corporate Solutions clients.
The issuer of this announcement warrants that they are solely
responsible for the content, accuracy and originality of the
information contained therein.
Source: Prothena Corporation plc via Globenewswire
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