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Mohammed Amin (Amin) Arnaout, MD

Dr. Arnaout is a physician-scientist in the Division of Nephrology at Massachusetts General Hospital in Boston. He is also Professor of Medicine at Harvard Medical School.

  • Phone: 617-726-5050
Department of Medicine


  • Transplant Center
  • Kidney Transplant
  • Vascular Center
  • Nephrology
Clinical Interests
Inflammatory kidney diseases
General nephrology
Polycystic kidney disease
Boston: Massachusetts General Hospital
Medical Education
MD, American University of Beirut
Residency, Johns Hopkins Hospital
Fellowship, Brigham and Women's Hospital
Fellowship, Children's Hospital Boston
Board Certifications
Nephrology, American Board of Internal Medicine
Internal Medicine, American Board of Internal Medicine
Foreign Languages
Patient Age Group
Accepting New Patients

BiographyDr. Arnaout received his medical degree with distinction from the American University of Beirut, Lebanon. He served on the medical staff of the American University of Beirut Hospital as an intern and resident in Medicine before moving to Johns Hopkins where he completed his residency. He then moved to Harvard where he finished fellowships in immunology and nephrology at Boston's Childrens Hospital and Brigham and Women's Hospital. He currently serves as a Physician-Scientist in the Division of Nephrology at Massachusetts General Hospital. 


Major research activities in Dr. Arnaout's laboratory focus on dissecting the role of leukocyte adhesion in inflammation and immune injury and on elucidating the basic cellular defects in Autosomal Dominant Polycystic Kidney Disease (ADPKD).

The leukocyte integrins are cell surface receptors that mediate adhesio-dependent functions in all cell types including leukocytes, where they mediate leukocyte homing to tissues and organs a vital component of host defense against pathogens. Deregulated activation of integrins leads to pathologic inflammation. A major focus is to define the structural basis of integrin regulation, which should help in developing novel drugs to counter inflammatory diseases.

Defective regulation of tube diameter is the basic defect in ADPKD, leading to cysts in tubules and blood vessels. Mutations in one of two genes, PKD1 or PKD2 is the underlying genetic cause, but how these proteins function and are regulated is incompletely understood and is the focus of our research.


View my most recent publications at PubMed


  1. Arnaout MA, Hakim RM, Todd RF, Dana N, Colten HR.1985. Increased expression of an adhesion-promoting surface glycoprotein in the granulocytopenia of hemodialysis. N Engl J Med. 312:457.
  2. Michishita M, Videm V, Arnaout MA. 1993. A novel divalent cation-binding site in the A- domain of the beta 2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell. 72: 857.
  3. Lee JO, Rieu P, Arnaout MA (Corresp. author), Liddington R. 1995. Crystal structure of the A domain of the alpha subunit of integrin CR3 (CD11b/CD18). Cell. 80:631.
  4. Gonzalez-Perrett S, Kim K, Ibarra C, Damiano AE, Zotta E, Batelli M, Harris PC, Reisin IL, Arnaout MA and Cantiello HF. 2000. Polycystin-2, the protein mutated in autosomal dominant Polycystic Kidney Disease (ADPKD), is a Ca2+-permeable non-selective cation channel. Proc. Natl Acad. Sci. USA. 98:1182.
  5. Xiong JP, Stehle T, Diefenbach B, Zhang R, Dunker R, Scott DL, Joachimiak A, Goodman SL, and Arnaout MA. 2001. Crystal structure of the extracellular segment of integrin aVb3. Science. Oct 12; 294:339.
  6. Xiong JP, Stehle T, Zhang R, Dunker R, Joachimiak A, Frech M, Goodman SL, and Arnaout MA. 2002. Crystal structure of the extracellular domain of integrin aVb3 in complex with an Arg-Gly-Asp Ligand. Science. Apr 5; 296:151.
  7. Xiong JP, Mahalingham B, Alonso JL, Borelli LA, Riu X, Zhang, Anand S, Hyman BT, Rysiok T, Muller-Pompalla D, Goodman SL, and Arnaout MA. 2009. Crystal structure of the complete integrin aVb3 ectodomain plus an alpha/beta transmembrane fragment. J Cell Biol. 186:589.

Mass. General study identifies path to safer drugs for heart disease, cancer

MGH investigators may have found a way to solve a problem that has plagued a group of drugs called ligand-mimicking integrin inhibitors, which have the potential to treat conditions ranging from heart attacks to cancer metastasis.

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Phone: 617-726-5050
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