J. Cell Biol., Volume 141, Number 4, May 18, 1998 1019-1030

The 51 Integrin Mediates Elimination of Amyloid- Peptide and Protects Against Apoptosis

Michelle L. Matter,^* Zhuohua Zhang,^* Christer Nordstedt,^§ and Erkki Ruoslahti^*

^* La Jolla Cancer Research Center, The Burnham Institute, La Jolla, California 92037;  Department of Neurobiology, Harvard Medical School, and Division of Neuroscience, The Children's Hospital, Boston, Massachusetts 02115; and ^§ Department of Clinical Neuroscience, The Karolinska Hospital, Stockholm, Sweden S-171 76

The amyloid- peptide (A) can mediate cell attachment by binding to 1 integrins through an arg-his-asp sequence. We show here that the 51 integrin, a fibronectin receptor, is an efficient binder of A, and mediates cell attachment to nonfibrillar A. Cells engineered to express 51 internalized and degraded more added A1-40 than did 51-negative control cells. Deposition of an insoluble A1-40 matrix around the 51-expressing cells was reduced, and the cells showed less apoptosis than the control cells. Thus, the 51 integrin may protect against A deposition and toxicity, which is a course of Alzheimer's disease lesions.

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