F-actin-capping protein subunit a-2 regulates growth of the actin filament by capping the barbed end of growing actin filaments. Members of the actin-depolymerizing factor /cofilin family are important regulators of actin dynamics. ADF and cofilin’s ability to increase actin filament dynamics is Gomisin-D inhibited by their phosphorylation on Ser3 by LIM kinase 1 and other kinases Ab dystrophy requires LIM kinase 1-mediated phosphorylation of ADF/cofilin and the remodeling of the actin cytoskeleton. Biotinylated 15d-PGJ2 covalently binds to actin b in various cells other than neurons, supporting our results in neurons. Internexin ais classified as a type IV neuronal intermediate filament. Internexin a also co-assembles with the neurofilament triplet proteins. The protein is expressed by most, if not all, neurons as they commence differentiation and precedes the expression of the 
NF triplet proteins. Although the interaction of internexin a with amyloid proteins has not yet been reported, Internexin a, and not NF triplet, ring-like reactive neurites are present in end-stage AD cases, indicating the relatively late involvement of neurons that selectively contain Internexin a. Another intermediate filament protein, GFAP is expressed exclusively in astrocytes. Ab increased the total number of activated astrocytes, and elevated the expression of GFAP by Ab-induced spontaneous calcium transients. 15d-PGJ2 suppresses inflammatory response by inhibiting NF-kB signaling at multiple steps as well as by inhibiting the PI3K/Akt pathway independent of PPARc in primary astrocytes. In conclusion, membrane target proteins for 15d-PGJ2 were factors associated with the two remarks of AD, the amyloid plaque and the neurofibrillary tangle. Beyond classical roles as glycolytic enzymes and molecular chaperones, GAPDH, enolase 2 and Hsp8a can form the antioxidant complex of PMOs responded to the extracellular oxidative stress. 15d-PGJ2 might regulate the activity of PMOs during inflammation and degeneration. Apart from glycolysis, pyruvate kinase and enolase might be involved in the 15d-PGJ2�Cinduced apoptosis as autoantigens. Thus, the present study sheds light on the ecto-enzymes targeted for 15dPGJ2 as a prelude to the death receptor stimulated by 15d-PGJ2 or the antioxidant complex regulated by 15d-PGJ2. The aBcrystallin protein has a subunit mass of 20 kDa but forms molecular aggregates with a mass of approximately 650 kDa. It is abundantly expressed in the eye lens fiber cells, where it is associated with the closely related protein aA-crystallin, and is also constitutively expressed at significant levels in heart and skeletal muscle and lens epithelial cells. aB-crystallin is a functional chaperone protein that can bind to denatured Pimozide substrate proteins, thereby preventing their non-specific aggregation. It is upregulated in several pathologic conditions where, as a molecular chaperone, it is thought to provide a first line of defense against misfolded or aggregation-prone proteins. aBcrystallin has received significant attention in recent years because it has been linked to muscle and neurological disorders, as well as immunity and cancer. However, how aB-crystallin contributes to these pathologies is not clearly understood. Hereditary cataracts exhibit diverse etiology and morphology. Cataracts may be inherited by an autosomal recessive, autosomal dominant, or X-linked mechanism. Cataracts caused by missense mutations in crystallin genes are most commonly autosomal dominant disorders. Understanding the pathophysiology of hereditary cataracts can yield insight into the mechanisms of cataractogenesis in general. However, the relationships between cataract etiology, lens morphology, and the underlying molecular mechanisms that control lens structure and function are currently unclear. Numerous crystallin gene mutations have been reported to be associated with hereditary cataracts. Mutations in the aB-crystallin gene cause either isolated cataracts or cataracts associated with myopathy.