NDLI: FE65 and FE65L1 amyloid precursor protein–binding protein compound null mice display adult-onset cataract and muscle weakness

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Multitarget fatty acid amide hydrolase/cyclooxygenase blockade suppresses intestinal inflammation and protects against nonsteroidal anti-inflammatory drug-dependent gastrointestinal damage

FE65 and FE65L1 amyloid precursor protein–binding protein compound null mice display adult-onset cataract and muscle weakness

A single-chain variable fragment intrabody prevents intracellular polymerization of Z α 1-antitrypsin while allowing its antiproteinase activity

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FE65 and FE65L1 amyloid precursor protein–binding protein compound null mice display adult-onset cataract and muscle weakness

Content Provider	PubMed Central
Author	Suh, Jaehong Moncaster, Juliet A. Wang, Lirong Hafeez, Imran Herz, Joachim Tanzi, Rudolph E. Goldstein, Lee E. Guénette, Suzanne Y.
Copyright Year	2015
Abstract	FE65 and FE65L1 are cytoplasmic adaptor proteins that bind a variety of proteins, including the amyloid precursor protein, and that mediate the assembly of multimolecular complexes. We previously reported that FE65/FE65L1 double knockout (DKO) mice display disorganized laminin in meningeal fibroblasts and a cobblestone lissencephaly-like phenotype in the developing cortex. Here, we examined whether loss of FE65 and FE65L1 causes ocular and muscular deficits, 2 phenotypes that frequently accompany cobblestone lissencephaly. Eyes of FE65/FE65L1 DKO mice develop normally, but lens degeneration becomes apparent in young adult mice. Abnormal lens epithelial cell migration, widespread small vacuole formation, and increased laminin expression underneath lens capsules suggest impaired interaction between epithelial cells and capsular extracellular matrix in DKO lenses. Cortical cataracts develop in FE65L1 knockout (KO) mice aged 16 months or more but are absent in wild-type or FE65 KO mice. FE65 family KO mice show attenuated grip strength, and the nuclei of DKO muscle cells frequently locate in the middle of muscle fibers. These findings reveal that FE65 and FE65L1 are essential for the maintenance of lens transparency, and their loss produce phenotypes in brain, eye, and muscle that are comparable to the clinical features of congenital muscular dystrophies in humans.—Suh, J., Moncaster, J. A., Wang, L., Hafeez, I., Herz, J., Tanzi, R. E., Goldstein, L. E., Guénette, S. Y. FE65 and FE65L1 amyloid precursor protein–binding protein compound null mice display adult-onset cataract and muscle weakness.
Related Links	http://dx.doi.org/10.1096/fj.14-261453
Ending Page	2639
Page Count	12
Starting Page	2628
File Format	PDF
ISSN	08926638
e-ISSN	15306860
Journal	The FASEB Journal
Issue Number	6
Volume Number	29
Language	English
Publisher	Federation of American Societies for Experimental Biology
Publisher Date	2015-06-01
Access Restriction	Open
Rights Holder	Federation of American Societies for Experimental Biology
Subject Keyword	Biotechnology Genetics Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology Biochemistry Biotechnology

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FE65 and FE65L1 amyloid precursor protein–binding protein compound null mice display adult-onset cataract and muscle weakness