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News Article | February 16, 2017
Site: globenewswire.com

AUSTIN, Texas, Feb. 16, 2017 (GLOBE NEWSWIRE) -- Aeglea BioTherapeutics, Inc. (NASDAQ:AGLE), a biotechnology company committed to developing enzyme-based therapeutics in the field of amino acid metabolism to treat rare genetic diseases and cancer, today announced the appointment of Suzanne L. Bruhn, Ph.D. to its Board of Directors. Dr. Bruhn previously served as chief executive officer, president and director at Promedior, Inc., a clinical-stage biotechnology company, from 2012 to 2015. “Suzanne’s depth of experience in the early-stage biotechnology space and expertise in orphan diseases will be a valuable addition to our Board,” said David G. Lowe, Ph.D., co-founder, president and chief executive officer of Aeglea. “Her insights and guidance will be a tremendous asset as we further our clinical programs in order to pursue our mission of developing treatments for patients with rare genetic diseases and cancer.” During her time at Promedior, Dr. Bruhn focused the company’s strategy on clinical development for orphan diseases and negotiated the grant of an exclusive option to acquire Promedior to Bristol-Myers Squibb Company in 2015. Prior to Promedior, Dr. Bruhn held a number of roles in strategic and portfolio planning, program management and regulatory affairs at Shire Human Genetic Therapies, formerly known as Transkaryotic Therapies, between 1998 and 2012. She also served on the board of directors of Raptor Pharmaceuticals Corp., a biotechnology company focused on treating rare metabolic disorders, from 2011 until it was sold to Horizon Pharma plc in October 2016. Dr. Bruhn earned her bachelor’s degree in chemistry from Iowa State University of Science and Technology and her Ph.D. from Massachusetts Institute of Technology. About Aeglea BioTherapeutics Aeglea is a biotechnology company committed to developing enzyme-based therapeutics in the field of amino acid metabolism to treat rare genetic diseases and cancer. The company’s engineered human enzymes are designed to modulate the extremes of amino acid metabolism in the blood to reduce toxic levels of amino acids in inborn errors of metabolism or target tumor metabolism for cancer treatment. AEB1102, Aeglea’s lead product candidate, is currently being studied in two ongoing Phase 1 clinical trials in patients with advanced solid tumors and acute myeloid leukemia/myelodysplastic syndrome (AML/MDS). Additionally, Aeglea is recruiting patients into its ongoing Phase 1/2 trial of AEB1102 for the treatment of patients with Arginase I deficiency. The company is building a pipeline of additional product candidates targeting key amino acids, including AEB4104, which degrades homocystine, a target for an inborn error of metabolism, as well as two potential treatments for cancer, AEB3103, which degrades cysteine/cystine, and AEB2109, which degrades methionine. For more information, please visit http://aegleabio.com. Safe Harbor / Forward Looking Statements This press release contains “forward-looking” statements within the meaning of the safe harbor provisions of the U.S. Private Securities Litigation Reform Act of 1995. Forward-looking statements can be identified by words such as: “anticipate,” “intend,” “plan,” “goal,” “seek,” “believe,” “project,” “estimate,” “expect,” “strategy,” “future,” “likely,” “may,” “should,” “will” and similar references to future periods. These statements are subject to numerous risks and uncertainties that could cause actual results to differ materially from what we expect. Examples of forward-looking statements include, among others, the potential therapeutic benefits and economic value of our product candidates. Further information on potential risk factors that could affect our business and its financial results are detailed in our most recent Quarterly Report on Form 10-Q for the quarter ended September 30, 2016, filed with the Securities and Exchange Commission (SEC), and other reports as filed with the SEC. We undertake no obligation to publicly update any forward-looking statement, whether written or oral, that may be made from time to time, whether as a result of new information, future developments or otherwise.


Duffield J.S.,University of Washington | Lupher M.,Promedior | Thannickal V.J.,University of Alabama at Birmingham | Wynn T.A.,National Institute of Allergy and Infectious Diseases
Annual Review of Pathology: Mechanisms of Disease | Year: 2013

Myofibroblasts accumulate in the spaces between organ structures and produce extracellular matrix (ECM) proteins, including collagen I. They are the primary "effector" cells in tissue remodeling and fibrosis. Previously, leukocyte progenitors termed fibrocytes and myofibroblasts generated from epithelial cells through epithelial-to-mesenchymal transition (EMT) were considered the primary sources of ECM-producing myofibroblasts in injured tissues. However, genetic fate mapping experiments suggest that mesenchyme-derived cells, known as resident fibroblasts, and pericytes are the primary precursors of scar-forming myofibroblasts, whereas epithelial cells, endothelial cells, and myeloid leukocytes contribute to fibrogenesis predominantly by producing key fibrogenic cytokines and by promoting cell-to-cell communication. Numerous cytokines derived from T cells, macrophages, and other myeloid cell populations are important drivers of myofibroblast differentiation. Monocyte-derived cell populations are key regulators of the fibrotic process: They act as a brake on the processes driving fibrogenesis, and they dismantle and degrade established fibrosis. We discuss the origins, modes of activation, and fate of myofibroblasts in various important fibrotic diseases and describe how manipulation of macrophage activation could help ameliorate fibrosis. © 2013 by Annual Reviews. All rights reserved.


Patent
Promedior | Date: 2012-11-06

Polypeptides are susceptible to denaturation or enzymatic degradation in the blood, liver or kidney. Due to the low stability of some polypeptides, it has been required to administer polypeptide drugs in a sustained frequency to a subject in order to maintain an effective plasma concentration of the active substance. Furthermore, pharmaceutical compositions of therapeutic peptides preferably have a shelf-life of several years in order to be suitable for common use. However, peptide compositions are inherently unstable due to sensitivity towards chemical and physical degradation. In part, the invention provides SAP variant proteins, compositions, pharmaceutical preparations and formulations having a prolonged in vivo half-life, prolonged shelf-life, or rather increased in vitro stability, or increased manufacturing efficiency compared to human SAP. Advantages of increased plasma half-life include, but are not limited to, reducing the amount and/or frequency of dosing.


Patent
Promedior | Date: 2012-12-21

Functionalized pentraxin-2 (PTX-2) protomers and functionalized PTX-2 pentamers, methods for preparing functionalized PTX-2 protomers and functionalized PTX-2 pentamers, pharmaceutical compositions including functionalized PTX-2 pentamers, and methods for using the same are described herein.


Patent
Promedior | Date: 2012-09-07

The disclosure relates to methods for delivery of serum amyloid P to the respiratory system. Pharmaceutical compositions comprising SAP suitable for respiratory delivery are also provided.


Patent
Promedior | Date: 2014-10-08

In part, the disclosure relates to methods of treating fibrotic cancers by administering one or more Serum Amyloid Protein (SAP) agonists. In certain aspects, the method further comprises the conjoint administration of an anti-cancer therapeutic, e.g., a chemotherapeutic agent. In certain aspects, the disclosure relates to methods of treating myelofibrosis by administering an SAP agonist and optionally one or more anti-cancer therapeutic agents.


Patent
Promedior | Date: 2016-02-24

Polypeptides are susceptible to denaturation or enzymatic degradation in the blood, liver or kidney. Due to the low stability of some polypeptides, it has been required to administer polypeptide drugs in a sustained frequency to a subject in order to maintain an effective plasma concentration of the active substance. Furthermore, pharmaceutical compositions of therapeutic peptides preferably have a shelf- life of several years in order to be suitable for common use. However, peptide compositions are inherently unstable due to sensitivity towards chemical and physical degradation. In part, the invention provides SAP variant proteins, compositions, pharmaceutical preparations and formulations having a prolonged in vivo half-life, prolonged shelf-life, or rather increased in vitro stability, or increased manufacturing efficiency compared to human SAP. Advantages of increased plasma half-life include, but are not limited to, reducing the amount and/or frequency of dosing.


Patent
Promedior | Date: 2014-03-24

Functionalized pentraxin-2 (PTX-2) protomers and functionalized PTX-2 pentamers, methods for preparing functionalized PTX-2 protomers and functionalized PTX-2 pentamers, pharmaceutical compositions including functionalized PTX-2 pentamers, and methods for using the same are described herein.


Patent
Promedior | Date: 2016-07-13

One aspect of the present invention relates to the surprising discovery that modification of a glycan structure on a human SAP polypeptide can increase the biological activity of the SAP polypeptide relative to a corresponding sample of wild-type SAP isolated from human serum. The disclosure provides both variant human SAP polypeptides and methods for making the same. In particular, the present invention provides methods and compositions for in vitro and in vivo addition, deletion, or modification of sugar residues to produce SAP polypeptides, such as a human SAP polypeptide, having a desired glycosylation pattern.


Patent
Promedior | Date: 2010-06-17

Polypeptides are susceptible to denaturation or enzymatic degradation in the blood, liver or kidney. Due to the low stability of some polypeptides, it has been required to administer polypeptide drugs in a sustained frequency to a subject in order to maintain an effective plasma concentration of the active substance. Furthermore, pharmaceutical compositions of therapeutic peptides preferably have a shelf-life of several years in order to be suitable for common use. However, peptide compositions are inherently unstable due to sensitivity towards chemical and physical degradation. In part, the invention provides SAP variant proteins, compositions, pharmaceutical preparations and formulations having a prolonged in vivo half-life, prolonged shelf-life, or rather increased in vitro stability, or increased manufacturing efficiency compared to human SAP. Advantages of increased plasma half-life include, but are not limited to, reducing the amount and/or frequency of dosing.

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