Bernard H. Bressler

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Bernard H. Bressler
Bernard H. Bressler.png
Born
Alma mater McMaster University
Sir George Williams University
University of Manitoba (MSc, PhD)
Organization(s)University of British Columbia, Vancouver Coastal Health Research Institute, Rick Hansen Institute

Bernard H. Bressler FCAHS (born 1944) is a Professor in the Department of Cellular and Physiological Sciences and an Associate Member in the Department of Orthopedics at the University of British Columbia (UBC).

Contents

Bressler has been a provincial and national leader in research, teaching and governance. In 2008, Bressler was inducted as a Fellow of the Canadian Academy of Health Sciences and received the Lifetime Achievement Award from LifeSciences BC for his commitment to the commercialization of innovative technologies. He is currently a member of the Board of the Canada-Israel Industrial Research & Development Foundation (CIIRDF).[ citation needed ]

Early life and education

Bressler was born in 1944 in Winnipeg, Manitoba. He received his BSc from Sir George Williams University (now Concordia University) in 1966. He received his MSc in Anatomy (1968) and PhD in Physiology (1972) from the University of Manitoba.[ citation needed ] He completed his postdoctoral studies in Neuroscience at McMaster University.[ citation needed ]

Career

Researcher

Bressler's research program in skeletal muscle biophysics received support from the Medical Research Council of Canada and the Canadian Institutes for Health Research for 29 years.

His research focuses on providing new information about the fundamental mechanisms for force production in skeletal muscle. Experiments are designed to test some fundamental assumptions of the cross-bridge model as well as the role of the protein troponin C (TnC) in the regulation of calcium sensitivity in striated muscle.

Part of the research is designed to explore how the level of activation of skeletal muscle is controlled by the calcium binding properties of troponin C – the protein responsible for the initiation of muscle contraction. Troponin C has long been associated with the role of an on/off switch which turns a muscle 'on' by binding calcium or 'off' when it releases calcium. Bressler's lab found that a shift in the balance between calcium being bound or unbound produces a dramatic drop in the maximal levels of tension development. A measurable change in the rate at which tension develops is also observed with this shift in calcium affinity. The TnC project is only one of a series of projects designed to study the mechanical properties of cross-bridges. [1]

Educator and administrator

Bressler's teaching career began in 1973 at the University of Saskatchewan in the Departments of Anatomy and Physiology. He joined the University of British Columbia in the Department of Anatomy, Faculty of Medicine in 1976.

During his tenure as Vice President of Research at UBC (1996-1999), he was actively involved in the growth of the University Industry Liaison Office, which has become a world leader in development and management of technology transfer and biotechnology spin-offs. For these and other accomplishments in the area of commercialization of inventions, Bressler was recognized in April 2008 with a Lifetime Achievement Award from LifeSciences BC. [2]

From 1999 - 2008, Dr. Bressler served as VP Research, Vancouver Coastal Health and Executive Director, VCH Research Institute and Associate Dean, Research and Graduate Studies for the Faculty of Medicine at UBC. He oversaw the creation of Vancouver Coastal Health Research Institute, which is one of the top five health research organizations in Canada. [3]

Board governance and volunteerism

Bressler has held numerous board positions in the life sciences, biotechnology, economic and medical sectors. He has a particular interest in expanding Canada's global reach as it relates to life sciences and commercialization. Bressler has been invited to serve on the boards of the Canada Israel Industrial Research Development Foundation and International Scientific and Technology Partnerships in Canada.[ citation needed ]

Bressler served as the chair of the board of directors at the Rick Hansen Institute from 2011 to 2017. He was instrumental in helping to broaden the institute's international collaborations in spinal cord injury research and care in Israel. In 2016, RHI was accredited by Imagine Canada and was one of only 170 non-profit organizations in Canada to achieve this standard of excellence at the time. [4]

Awards

Bressler's awards and distinctions include:

Publications

Bressler has co-authored over 30 publications. Select publications include:

Related Research Articles

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<span class="mw-page-title-main">Smooth muscle</span> Involuntary non-striated muscle

Smooth muscle is an involuntary non-striated muscle, so-called because it has no sarcomeres and therefore no striations. It is divided into two subgroups, single-unit and multiunit smooth muscle. Within single-unit muscle, the whole bundle or sheet of smooth muscle cells contracts as a syncytium.

<span class="mw-page-title-main">Skeletal muscle</span> One of three major skeletal system types that connect to bones

Skeletal muscles are organs of the vertebrate muscular system and typically are attached by tendons to bones of a skeleton. The muscle cells of skeletal muscles are much longer than in the other types of muscle tissue, and are often known as muscle fibers. The muscle tissue of a skeletal muscle is striated – having a striped appearance due to the arrangement of the sarcomeres.

<span class="mw-page-title-main">Sarcomere</span> Repeating unit of a myofibril in a muscle cell

A sarcomere is the smallest functional unit of striated muscle tissue. It is the repeating unit between two Z-lines. Skeletal muscles are composed of tubular muscle cells which are formed during embryonic myogenesis. Muscle fibers contain numerous tubular myofibrils. Myofibrils are composed of repeating sections of sarcomeres, which appear under the microscope as alternating dark and light bands. Sarcomeres are composed of long, fibrous proteins as filaments that slide past each other when a muscle contracts or relaxes. The costamere is a different component that connects the sarcomere to the sarcolemma.

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Cardiac muscle is one of three types of vertebrate muscle tissues, with the other two being skeletal muscle and smooth muscle. It is an involuntary, striated muscle that constitutes the main tissue of the wall of the heart. The cardiac muscle (myocardium) forms a thick middle layer between the outer layer of the heart wall and the inner layer, with blood supplied via the coronary circulation. It is composed of individual cardiac muscle cells joined by intercalated discs, and encased by collagen fibers and other substances that form the extracellular matrix.

<span class="mw-page-title-main">Striated muscle tissue</span> Muscle tissue with repeating functional units called sarcomeres

Striated muscle tissue is a muscle tissue that features repeating functional units called sarcomeres. The presence of sarcomeres manifests as a series of bands visible along the muscle fibers, which is responsible for the striated appearance observed in microscopic images of this tissue. There are two types of striated muscle:

<span class="mw-page-title-main">Muscle contraction</span> Activation of tension-generating sites in muscle

Muscle contraction is the activation of tension-generating sites within muscle cells. In physiology, muscle contraction does not necessarily mean muscle shortening because muscle tension can be produced without changes in muscle length, such as when holding something heavy in the same position. The termination of muscle contraction is followed by muscle relaxation, which is a return of the muscle fibers to their low tension-generating state.

<span class="mw-page-title-main">Myofilament</span> The two protein filaments of myofibrils in muscle cells

Myofilaments are the three protein filaments of myofibrils in muscle cells. The main proteins involved are myosin, actin, and titin. Myosin and actin are the contractile proteins and titin is an elastic protein. The myofilaments act together in muscle contraction, and in order of size are a thick one of mostly myosin, a thin one of mostly actin, and a very thin one of mostly titin.

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<span class="mw-page-title-main">Troponin T</span> Protein family

Troponin T is a part of the troponin complex, which are proteins integral to the contraction of skeletal and heart muscles. They are expressed in skeletal and cardiac myocytes. Troponin T binds to tropomyosin and helps position it on actin, and together with the rest of the troponin complex, modulates contraction of striated muscle. The cardiac subtype of troponin T is especially useful in the laboratory diagnosis of heart attack because it is released into the blood-stream when damage to heart muscle occurs. It was discovered by the German physician Hugo A. Katus at the University of Heidelberg, who also developed the troponin T assay.

<span class="mw-page-title-main">Troponin I</span> Muscle protein

Troponin I is a cardiac and skeletal muscle protein family. It is a part of the troponin protein complex, where it binds to actin in thin myofilaments to hold the actin-tropomyosin complex in place. Troponin I prevents myosin from binding to actin in relaxed muscle. When calcium binds to the troponin C, it causes conformational changes which lead to dislocation of troponin I. Afterwards, tropomyosin leaves the binding site for myosin on actin leading to contraction of muscle. The letter I is given due to its inhibitory character. It is a useful marker in the laboratory diagnosis of heart attack. It occurs in different plasma concentration but the same circumstances as troponin T - either test can be performed for confirmation of cardiac muscle damage and laboratories usually offer one test or the other.

<span class="mw-page-title-main">TNNT2</span> Protein-coding gene in the species Homo sapiens

Cardiac muscle troponin T (cTnT) is a protein that in humans is encoded by the TNNT2 gene. Cardiac TnT is the tropomyosin-binding subunit of the troponin complex, which is located on the thin filament of striated muscles and regulates muscle contraction in response to alterations in intracellular calcium ion concentration.

<span class="mw-page-title-main">Troponin C type 1</span> Protein-coding gene in the species Homo sapiens

Troponin C, also known as TN-C or TnC, is a protein that resides in the troponin complex on actin thin filaments of striated muscle and is responsible for binding calcium to activate muscle contraction. Troponin C is encoded by the TNNC1 gene in humans for both cardiac and slow skeletal muscle.

<span class="mw-page-title-main">TPM2</span> Protein-coding gene in the species Homo sapiens

β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.

<span class="mw-page-title-main">TNNI2</span> Protein-coding gene in the species Homo sapiens

Troponin I, fast skeletal muscle is a protein that in humans is encoded by the TNNI2 gene.

<span class="mw-page-title-main">TNNT3</span> Protein-coding gene in the species Homo sapiens

Fast skeletal muscle troponin T (fTnT) is a protein that in humans is encoded by the TNNT3 gene.

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References

  1. "Bressler | Department of Cellular & Physiological Sciences". cps.med.ubc.ca. Retrieved 2017-06-20.
  2. "LifeSciences BC Announces Recipients of the 2008 LifeSciences British Columbia Awards". www.newswire.ca. Retrieved 2017-06-20.
  3. "Vancouver Coastal Health Research Institute". Vancouver Coastal Health. Archived from the original (PDF) on 2017-06-20. Retrieved 2017-06-20.
  4. "Standards Program announces latest group of accredited organizations | Imagine Canada". www.imaginecanada.ca. Retrieved 2017-06-20.