B. Slack PhD
Barbara E. Slack
Degree(s) - BSc., MSc., PhD.
Academic Title - Associate Professor
Education/Training –
BSc. Life Sciences (Honours), Queen’s University, Kingston , Ontario , Canada , 1976.
MSc. Pharmacology, Queen’s University, 1978.
PhD. Pharmacology, Queen’s University, 1982.
Postdoctoral Fellow, Department of Applied Biological Sciences, MIT, 1982-1984.
Research Fellow, Department of Physiology and Biophysics, Harvard Medical School, 1984-1985.
Postdoctoral Associate, Department of Brain and Cognitive Sciences, MIT, 1986-1988.
Research Scientist, Department of Brain and Cognitive Sciences, MIT, 1988 to 1995.
Research Interests –
We study signaling pathways activated by muscarinic acetylcholine receptor subtypes. In particular, we are interested in how interactions between integrins and extracellular matrix (ECM) proteins regulate these pathways.
Our second interest is the regulation of the discoidin domain receptor 1 (DDR1) by ECM proteins. DDR1 is a tyrosine kinase receptor for collagen that is often overexpressed in epithelial cell cancers. We wish to determine if differential responsiveness of DDR1 to collagen type IV (a component of the basement membrane) and collagen type I (a constituent of the stroma) plays a role in the development of breast cancer.
A third interest is the regulation of proteolytic processing of the amyloid precursor protein (APP) of Alzheimer’s disease (AD). APP proteolysis by beta- and gamma-secretases releases an amyloidogenic protein, Abeta, that forms insoluble deposits in the brain in AD. We are studying the mechanisms by which receptor-coupled signaling pathways activate another class of proteases, known as alpha-secretases, that cleave APP within the A domain, and preclude the formation of amyloid.
Recent Publications–
- Slack, B.E. and Wurtman, R.J. (2007) Regulation of Synthesis and Metabolism of the Amyloid Precursor Protein by Extracellular Signals. In: Research Progress in Alzheimer’s Disease and Dementia, M.-K. Sun, ed., Vol. 2, pp. 1-25, Nova Science Publishers, Inc.
- Alfa Cissé, M., Sunyach,C., Slack, B.E., Fisher, A., Vincent, B., and Checler, F. (2007) M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity. J. Neurosci. 27: 4083-4092.
- Slack, B.E., Siniaia, M.S., and Blusztajn, J.K. (2006) Collagen type I selectively activates ectodomain shedding of the discoidin domain receptor I: Involvement of Src tyrosine kinase. J. Cell. Biochem. 98: 672-684.
- Slack, B.E. and Siniaia, M.S. (2005) Adhesion-dependent redistribution of MAP kinase and MEK promotes muscarinic receptor-mediated signaling to the nucleus. J. Cell. Biochem. 95: 366-378.
- Carey, R.M., Balcz, B.A., Lopez-Coviella, I., Slack, B.E. (2005) Inhibition of dynamin-dependent endocytosis increases shedding of the amyloid precursor protein ectodomain and reduces generation of amyloid beta protein. BMC Cell Biol. 6:30.
- Lopez-Coviella, I., Follettie, M., Mellott, T.J., Kovacheva, V.P., Slack, B.E.., Diesl, V., Berse, B., Thies, R.S., and Blusztajn, J.K. (2005) Bone morphogenetic protein 9 induces the transcriptome of basal forebrain cholinergic neurons. Proc. Natl. Acad. Sci. USA 102: 6984-6989.
- Slack, B.E., Ma, L. K., and Seah, C.C. (2001) Constitutive shedding of the amyloid precursor ectodomain is up-regulated by tumor necrosis factor-alpha converting enzyme (TACE). Biochem. J. 357, 787-794.
- Slack, B.E. (2000) The m3 muscarinic acetylcholine receptor is coupled to mitogen-activated protein kinase via protein kinase C and epidermal growth factor receptor kinase. Biochem. J. 348, 381-387.
- Slack, B.E. (1998) Tyrosine phosphorylation of paxillin and focal adhesion kinase by activation of muscarinic m3 receptors is dependent on integrin engagement by the extracellular matrix. Proc. Natl. Acad. Sci. USA 95, 7281-7286.
Contact Information
Telephone – 617-638-5487
Email - bslack@bu.edu
