Journal of Physical Chemistry & Biophysics

Journal of Physical Chemistry & Biophysics
Open Access

ISSN: 2161-0398

+44 7868 792050

Aladin M Boriek

Aladin M Boriek

Aladin M Boriek
Professor, Baylor College of Medicine


Dr. Aladin M. Boriek, PhD is a Professor of Medicine and Physiology at Baylor College of Medicine. Dr. Boriek received a master degree from University of Michigan in 1984 and a PhD degree from Rice University in 1990. He completed his postdoctoral training at Baylor College of Medicine in respiratory mechanics under the mentorship of Dr. Rodarte. Dr. Boriek has been a regular member of the Respiratory Integrative Biology and Translational Research Study Section (2005-2009).  Dr. Boriek has served on other NIH study sections including The Respiratory and Applied Physiology, and The Skeletal Muscle Biology and Exercise Physiology, and The Bioengineering and Physiology. He has also served as an external reviewer for the Surgery Review Board of the Department of Veteran Affairs, the Canadian Institutes of Health Research, the Canadian Lung Association /Canadian Thoracic Society, the Research Grant Council of Hong Kong. He has also served on numerous review panels for the National Science Foundation. He served as a member of the editorial board of the Journal of Applied Physiology (2000-2008). Dr. Boriek has published nearly sixty papers in peer reviewed journals. Dr. Boriek’s research interests include respiratory muscle mechanics, mechanical signal transduction, and muscular dystrophy.

Research Interest

Modeling and assessing diaphragm mechanics
Investigation of the determinants of diaphragm muscle mechanics and kinematics, including the unique mechanical properties of the diaphragm and structural issues such as the geodesic properties of diaphragm muscle fibers. Current work describes numerous approaches of  dealing with these determinants, including measuring diaphragm curvature, displacement and muscle shortening, as well as computational modeling of the effect of muscle anisotropic properties on diaphragm shape. This work is established in collaboration with Dr. Rolf Hubmayr at Mayo Clinic.
Assessment of respiratory muscle function in mouse models of muscular dystrophy. 
A complex rearrangement mutation in the mouse titin gene leads to an in-frame 83-amino acid deletion in the N2A region of titin. Autosomal recessive inheritance of the titin muscular dystrophy with myositis (Ttn(mdm/mdm)) mutation leads to a severe early-onset muscular dystrophy and premature death. We have tested the hypothesis that the titin N2A deletion in the mdm mouse diaphragm would have a deleterious impact on the force-generating capacity and altered passive mechanical properties, independent of major histopathology. Our data show significant structural and functional aberrations of the respiratory pump in the mdm mouse that may be attributable to a critical function of titin&primel\'s N2A region. This work was part of the PhD thesis of Dr. Michael Lopez who has been a member of our research group.
Mechanical signal transduction:
We have been interested in the anisotropic regulation of the mechanosensitive genes, the Ankrd2. We found that axial stretch activated Akt, which up-regulated Ankrd2 expression through NF-kappaB. However, stretch in the orthogonal direction to the muscle fibers activated Ras-GTP, Raf-1, and Erk1/2 proteins, which up-regulated Ankrd2 expression through AP-1. Our data show the anisotropic regulation of Ankrd2 gene expression in the diaphragm muscles occurs via two distinct mechanosensitive signaling pathways. This work was conducted in collaboration with his colleague Dr. Junaith Mohamed, a Research Associate in the Department of Medicine, and a member of their research group.
  they have been interested in the physiologic role of Sirt1 in skeletal muscles. they  have recently unraveled a mechanism of transcription regulation of the Sirt1 gene by the EGR1 (early growth response factor 1), which occurs in response to mechanical stretch. This stretch-responsive gene activation program is required to eliminate ROS generated during stretch. This work was conducted in collaboration with my colleague Dr. Patricia Pardo, a Research Associate in the Department of Medicine, and a member of our research group.

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