Dominique Alfandari

Dominique Alfandari, Ph.D.

Associate Professor of Developmental Biology

Associate Director MCB

Office phone: 413-577-4269

Lab phone: 413-545-3739

Fax: 413-545-6326

Email: alfandar [at] vasci [dot] umass [dot] edu

Office location: 427B ISB

Mailing address:

661 North Pleasant Street
Amherst, Mass 01003

Movie is a model of ADAM13 protein. The Metalloprotease domain is grey, Disintegrin in Blue, Cystein rich in purple, EGF repeat in green.

Ph.D.: University of Pierre & Marie Curie, Paris 6 (France), 1994
Postdoctoral Training: University of Virginia, Department of Cell Biology 

Previous positions: Maitre de conference UPMC 1996-2000 (Tenure), Research Instructor UVA 2000-2003

Awards: Predoctoral fellowship MRT 1991-1994. Post doctoral fellowship FRM 1995-1996. NIH RO1DE14365 (2001-6),  NIH RO1DE16289 (2006-2017), NSF 0544015 (2005-08)


ANIML SCI  200 H01-Honors
ANIML SCI  200-Animal Cell and Molecular Biology
ANIML SCI  697J-Cell, Genes and Development

ADAM metalloprotease function during embryonic Development

Happening now: Seminar presentation.  Stowers institute , 10/1/2013. New Postdoc Iivari Kleino has joined the lab.

 The following movies show cranial neural crest cell migration in vivo (in the embryo) or in vitro (In a dish). In vivo the neural crest were labeled with a fluorescent marker before they were grafted into a host embryo.



How does a cell move? Cells move all the time in our bodies, to repair wounds, to attack pathogens, to fight cancer or in some cases to allow cancer to spread and invade new organs. In embryos, cells move great distances to produce the various shapes and complex organs.

We study how cells move in a developing embryo. More specifically, how do they start? How do they know where to go, where and when to stop? One of the best examples of cell movement (see movie) is the migration of cranial neural crest cells. They are borne at the border between the neural and non-neural ectoderm in the dorsal side of the embryo and migrate to the ventral side of the embryo to create all of the structures of the face (bones, cartilage, muscle and ganglia).

Our laboratory is funded by the NIH (NIDCR) to understand how metalloproteases that are expressed at the surface of the cranial neural crest help these cells move. We aim to understand which proteins are cut by these proteases and how this cleavage changes the function of these target proteins to favor cell movement. Clearly if these proteases can promote cell migration in the embryo, they may also promote cancer cell dispersion (Metastasis) so that understanding how they work and how we can stop their function may also lead to new approaches to cancer treatment.

The Alfandari lab in the news.

To make an advising apointment follow this link: Advising

Pawlak E, Wang L, Johnson PJ, Nuovo G, Taye A, Belknap JK, Alfandari D, Black SJ.  2012.  Distribution and processing of a disintegrin and metalloproteinase with thrombospondin motifs-4, aggrecan, versican, and hyaluronan in equine digital laminae.. American journal of veterinary research. 73(7):1035-46.
Cousin H, Alfandari D.  2011.  ADAM and cell migration: the unexpected role of the cytoplasmic domain. Médecine sciences : M/S. 27(12):1069-71.
Alfandari D, Cousin H, Marsden M.  2010.  Mechanism of Xenopus cranial neural crest cell migration.. Cell adhesion & migration. 4(4):553-60.
Neuner R, Cousin H, McCusker C, Coyne M, Alfandari D.  2009.  Xenopus ADAM19 is involved in neural, neural crest and muscle development.. Mechanisms of development. 126(3-4):240-55.
McCusker C, Cousin H, Neuner R, Alfandari D.  2009.  Extracellular cleavage of cadherin-11 by ADAM metalloproteases is essential for Xenopus cranial neural crest cell migration.. Molecular biology of the cell. 20(1):78-89.
McCusker CD, Alfandari D.  2009.  Life after proteolysis: Exploring the signaling capabilities of classical cadherin cleavage fragments.. Communicative & integrative biology. 2(2):155-7.
Coyne MJ, Cousin H, Loftus JP, Johnson PJ, Belknap JK, Gradil CM, Black SJ, Alfandari D.  2009.  Cloning and expression of ADAM-related metalloproteases in equine laminitis.. Veterinary immunology and immunopathology. 129(3-4):231-41.
Alfandari D, McCusker C, Cousin H.  2009.  ADAM function in embryogenesis.. Seminars in cell & developmental biology. 20(2):153-63.
Cousin H, Desimone DW, Alfandari D.  2008.  PACSIN2 regulates cell adhesion during gastrulation in Xenopus laevis.. Developmental biology. 319(1):86-99.
Ito J, Yoon S-Y, Lee B, Vanderheyden V, Vermassen E, Wojcikiewicz R, Alfandari D, De Smedt H, Parys JB, Fissore RA.  2008.  Inositol 1,4,5-trisphosphate receptor 1, a widespread Ca2+ channel, is a novel substrate of polo-like kinase 1 in eggs.. Developmental biology. 320(2):402-13.
Kurokawa M, Yoon SY, Alfandari D, Fukami K, Sato K-ichi, Fissore RA.  2007.  Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations during mammalian fertilization.. Developmental biology. 312(1):407-18.
Lee B, Vermassen E, Yoon S-Y, Vanderheyden V, Ito J, Alfandari D, De Smedt H, Parys JB, Fissore RA.  2006.  Phosphorylation of IP3R1 and the regulation of [Ca2+]i responses at fertilization: a role for the MAP kinase pathway.. Development (Cambridge, England). 133(21):4355-65.
Cousin H, Gaultier A, Bleux C, Darribère T, Alfandari D.  2000.  PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13.. Developmental biology. 227(1):197-210.
Name Phone Office
Abbruzzese , Genevieve MCB Graduate student 413-545-3739 455 ISB
Advani , Siddheshwari MCB Graduate Student 413-545-3739 455 ISB
Bibeau , Evan Undergraduate Student 413-545-3739 455 ISB
Clarke , Katherine Undergraduate Student 413-545-3739 455 ISB
Grennon , Joseph Undergraduate Student 413-545-3739 455 ISB
Mathavan , Ketan MCB Graduate Student 413-545-3739 455 ISB
McLinden , Gretchen Undergraduate Student 413-545-3739 455 ISB
Riedel , Rebecca Undergraduate Student 413-545-3739 455 ISB
Former Lab Personnel