Category: Faculty Spotlight
For some people, a job is just a job, a place to sit and pass the day while they wait to go home. This is not the case for Dr. Jamie McKnight, Associate Professor of Physiology and Biophysics, who has been at Boston University since 1995. In fact, you could say BU has long been a part of Dr. McKnight’s family. His association with Boston University goes back twenty years, to when his wife first joined BU at the Charles River campus and is still there, currently as Chair of Humanities. Dr. McKnight’s daughter spent the first three years of her life in a BU dormitory as a toddler and now currently attends BU. It is obvious how Dr. McKnight feels at home and comfortable at BUSM.
Dr. McKnight warmly welcomed me into his office for an interview without much notice, even offering refreshments and happily answering the following questions:
Q: Can you tell us a little about your personal and educational background?
A: Well I’ve been at BU for 15 years, although my wife has been on the Charles River campus for twenty. Before that I worked on my Postdoctoral Fellow at the Whitehead Institute for Biomedical Research, at the Massachusetts Institute of Technology. I received my PHD at the University of Texas Southwestern Medical Center in Dallas in Biochemistry. I earned my Bachelors in chemistry at Washington College, Chestertown, Maryland.
Q: What lead you to pursue a career in academic biomedical research?
A: I’ve always been interested in science. I began studying organic chemistry, but became interested in physiology and cell biology courses. I did consider an industry career, but academic research just provided more benefits. One, I’ve always liked students. Two, I figured it would be easier to switch from an academic to research track than the other way around. Probably most significant was the prospect of studying whatever I want. Academic research allows me to choose what I want to study.
Q: What are your current research interests?
A: Currently, I am focusing on the structure and function of proteins. The main focus is the structure, assembly and secretion of very low density lipoprotein, the precursor of low density lipoprotein (“bad cholesterol”) and its interactions with microsomal triglyceride transfer protein (MTP) a required cofactor for lipoprotein secretion.
Q: You have been actively involved in graduate education here in GMS. Please, tell us about these activities:
A: I have been an Associate Professor of Physiology and Biophysics for the last five year, was the Assistant Professor of Physiology and Biophysics before that. I direct the Boston University School of Medicine Core Facility for Structural NMR, I am part of the integrated curriculum committee for PHD students and part of the Responsible Conduct of Research committee. I’ve been on the Physiology & Biophysics Student Affairs and Admission Committee for over a decade and was its chair for five years.
Q: What were your reasons for establishing your career at a strong research oriented medical school?
A: Well, there is access to a lot more resources at a research oriented medical school. Really though, I love doing stuff that is new, I love designing new experiments. I love pushing the limits of scientific knowledge. One of the great advantages of this particular medical school is the research environment is outstanding here, due in no small part to my colleagues. There is a significant amount of collaboration here. You can just go to another colleague for advice outside of your specialty, you don’t need to make appointments months in advances.
Q: Do you have any words of wisdom for graduate students here at BUSM?
A: If you don’t know then just ask
- Learn as much as you can.
- Immerse yourself in what you are doing.
- Attend some seminars in which you know nothing about topic but are vaguely interested in.
Q: What tips do you have for students on how to build a successful career in academic research and graduate education?
A: Pay attention to people’s names and network. Network! Network! Network! Go to meetings and meet people there. Just introduce yourself. Try not to say “No” if you can. Don’t be afraid to let your path drift. It is great to have an idea of what you want and are interested in, but stay open to exploring new subjects. Find a postdoctoral advisor that is well connected.
Q: Any other words of guidance or inspiration?
A: Always be a good citizen. And be extremely honest.
Hopefully these words will not go unheard by the students of GMS. Dr. McKnight certainly has an abundance of insightful and worthwhile wisdom still to impart to the developing minds of BUSM. Motivated, dedicated, respectful, warm and friendly, Dr. McKnight is an example of why BUSM is an excellent place to study for developing scientists.
By GMS student,
Margaret Bailey Wentworth.
Passionate scientist, breakthrough researcher and GMS faculty member John H. Schwartz, M.D. is now the Director of the renowned M.D./Ph.D. program. Dr. Schwartz’ enthusiasm for science has propelled him through a prolific career in the medical sciences field – with Boston University (BU) at its center. From his undergraduate degree in biology to his current position at GMS as a professor of medicine and member of the renal section at Boston University School of Medicine (BUSM), Dr. Schwartz has long been actively involved in the promotion of programs for his fellow scientists and students at BU. Now, as newly appointed Director of the M.D./Ph.D. program, Dr. Schwartz applies this same energy, continually striving to make the program more robust and enriching.
The M.D./Ph.D. program was already significantly strengthened in 2008 when GMS committed itself to providing M.D./Ph.D. students with full funding. This new standard for financial support, which continues to this day, ensures students complete tuition remission as well as stipends for living expenses during their graduate study years. As Director, Dr. Schwartz also works to make it possible for M.D./Ph.D. students to participate in special meetings, seminars and a retreat as well as in national conferences that focus on physician scientist training. To allow for these types of activities and to increase selectivity, the number of students supported in the M.D./Ph.D. program has been reduced to eight per year.
By training scientists in the M.D./Ph.D. program and acting as program Director, Dr. Schwartz aims to nurture and mold leaders in biomedical research and clinical practice. He maintains the philosophy that the clinical encounter is central in the generation of relevant questions that can be best explored by scientific methodology – and therefore central in producing effective physician-scientists. For this reason, the M.D./Ph.D. program emphasizes a balance between clinical and scientific training.
Dr. Schwartz grew up in Fall River, Ma. As an undergraduate at Boston University, he became interested in basic research and was involved in a National Science Foundation sponsorship program for undergraduates. He went on to earn his M.D. at the New York University School of Medicine and train in the laboratory of Dr. Philip Steinmetz at Harvard Medical School. He also completed a residency in Integral Medicine at the Beth Israel Hospital in Boston and post doctoral fellowship in Nephrology. In 1971, he became a staff member of the renal unit at the Walter Reed Army Institute of Research, eventually acting as chief of the unit from 1973 to 1977. Dr. Schwartz also acts as a mentor to physician scientists at GMS.
Dr. Schwartz has made research contributions (link out) in a number of areas including the cellular regulation of H+ transport in renal epithelia, coupling in excitable cells and pathogenesis of acute renal failure. His research is supported by grants from NIH.
Dr. Schwartz’s Research Activities:
Control Mechanisms of Acid Secretion
Renal inner medullary collecting duct cells transport protons, mediated by an H+-ATPase, and H2O, mediated by aquaporin-2 (AQP2) across their apical membrane. In our cultured line of IMCD cells, as in the kidney both of these processes are controlled by regulated exocytic insertion and endocytic retrieval of vesicles that carry either an H+-ATPase or AQP2 as cargo in their membranes, but not both. The targeting and fusion of these vesicles to the apical membrane may be mediated by SNARE proteins, the same proteins that mediate exocytosis at the synaptic membrane. However, despite the similarity of the postulated targeting-fusion system, exocytosis of H+-ATPase and AQP2 are independently regulated. Our group is evaluating how a polar renal epithelial cell target two distinct cargo-laden vesicles to the apical membrane utilizing similar docking-fusion proteins. We propose the following hypotheses which will be the focus of our current studies: 1) the minimal machinery, the SNAREpin, required for targeting and fusion of H+-ATPase or AQP2 vesicle subtypes to the apical membrane consists of a distinct set of v & t-SNAREs; 2) the cargo proteins (H+-ATPase and AQP2), per se, participate in the regulation, targeting and exocytic insertion of their carrier vesicles and 3) regulated exocytosis of these vesicles is not only initiated but proceeds by different signal cascades that modify (phosphorylate) dissimilar proteins in either the vesicles or target (apical) membrane.
Gene Expression Associated with Acute Renal Injury – Cellular Mechanisms of Injury in Acute Renal Failure
Although ischemia is a common cause of acute renal failure (ARF), the cellular pathogenesis of injury is unknown and no therapeutic interventions presently exist. Recent investigations in Dr. Borkan’s and other laboratories have suggest that the kidney in vivo and cultured cells in vitro respond to ischemia by producing a host of “stress proteins”. These proteins include the heat stress proteins (HSPs), well-known “cell protectants” that may be capable of preventing or ameliorating acute renal failure if increased prior to the insult. Current studies are intended to quantify the protection afforded by HSP 70 by selectively manipulating the content of the wild type hsp70 and several of its well-characterized mutants. This model system is being used to dissect the potential mechanisms by which HSPs protect the cell from ischemic injury. We are presently investigating the interaction between hsp70 and members of the BCL2 family, as well as identifying the events that result in mitochondrial membrane injury, a key step in triggering the apoptotic cascade that results in cell death.