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© The Rockefeller University Press, 0021-9525/1998//1019 $5.00
The Journal of Cell Biology, Volume 141, Number 4, , 1998 1019-1030

Articles

The {alpha}5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis



Michelle L. Matter*, Zhuohua Zhang*,{ddagger}, Christer Nordstedt§, and Erkki Ruoslahti*

* La Jolla Cancer Research Center, The Burnham Institute, La Jolla, California 92037; {ddagger} 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-β peptide (Aβ) can mediate cell attachment by binding to β1 integrins through an arg-his-asp sequence. We show here that the {alpha}5β1 integrin, a fibronectin receptor, is an efficient binder of Aβ, and mediates cell attachment to nonfibrillar Aβ. Cells engineered to express {alpha}5β1 internalized and degraded more added Aβ1-40 than did {alpha}5β1-negative control cells. Deposition of an insoluble Aβ1-40 matrix around the {alpha}5β1-expressing cells was reduced, and the cells showed less apoptosis than the control cells. Thus, the {alpha}5β1 integrin may protect against Aβ deposition and toxicity, which is a course of Alzheimer's disease lesions.

Abbreviations used in this paper: Aβ, amyloid β peptide; AD, Alzheimer's disease, LDH, lactate dehydrogenase; RHD, arg-his-asp.

The present address of Z. Zhang is Department of Neurobiology, Harvard Medical School, The Children's Hospital, Enders 260, 300 Longwood Ave., Boston, MA 02115.

Address all correspondence to Erkki Ruoslahti, The Burnham Institute, 10901 North Torrey Pines Rd., La Jolla, CA 90237. Tel.: 619-646-3125; Fax: 619-646-3199; E-mail: ruoslahti{at}burnham-inst.org


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