Degradation of actin and vimentin by calpain II, a Ca<sup>2+</sup>‐dependent cysteine proteinase, in bovine lens

Yoshida, Hideya; Murachi, Takashi; Tsukahara, I

doi:10.1016/0014-5793(84)81324-1

Cited by 49 publications

(31 citation statements)

References 17 publications

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“…Those individual cells that appeared rounded (i.e., abnormal) stained more brightly with calpain antibody, suggesting that this was attributable to less effective calpain inhibition. A number of studies in different models ranging from the lens of the eye 13 to spinal cord neurons 14 have shown that calpains are important in actin remodeling, and this study extends those observations to cold preserved SEC. Yoshida 13 reported a direct effect of calpain on actin, but calpain is also active against actin-associated proteins such as talin 33 and actin-binding protein 34,35 and localizes in some models to the site on the cell membrane where these proteins are present.…”

Section: Discussionsupporting

confidence: 70%

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Effect of cold preservation on intracellular calcium concentration and calpain activity in rat sinusoidal endothelial cells

et al. 2003

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I n the past several years, we have examined intracellular events that occur in sinusoidal endothelial cells (SEC) when they are placed in the cold. 1-4 SEC are the main targets of cold preservation injury, 5,6 and understanding the mechanisms by which they are injured might provide an avenue to development of improved preservation solutions. Our studies show that cold causes actin disassembly 2 and that this is associated with rounding of the cells 2 and release of matrix metalloproteases (MMPs) into the supernatants of SEC cell cultures. 1,3 Actin disassembly and MMP secretion lead to activation of the cell surface, as shown by increased expression of von Willebrand factor and increased adhesiveness for platelets. 4 Platelet adhesion is one of the key events that leads to allograft injury on reperfusion. 7,8 To date, the cause of cold-induced actin disassembly is unclear, but there are suggestions that abnormalities of calpain and calcium metabolism are important. There is a sharp rise in intracellular calcium when SECs are placed in the cold in the presence of extracellular calcium. 9 Calpain is a calcium-dependent intracellular protease the activity of which is increased in whole rat livers preserved in the cold 10 and in human allografts that show poor function after reperfusion. 11 Calpain activity has been shown to be associated with remodeling of actin. 12-14 Therefore, we hypothesized that exposure of SEC to cold results in the following sequence: elevated intracellular calcium concentration, increased calpain activity, and actin disassembly.

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Section: Discussionsupporting

confidence: 70%

“…11 Calpain activity has been shown to be associated with remodeling of actin. [12][13][14] Therefore, we hypothesized that exposure of SEC to cold results in the following sequence: elevated intracellular calcium concentration, increased calpain activity, and actin disassembly.…”

mentioning

confidence: 99%

Effect of cold preservation on intracellular calcium concentration and calpain activity in rat sinusoidal endothelial cells

et al. 2003

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“…This has raised interest in the involvement of the calcium-activated protease, calpain, in cataractogenesis. Several lens proteins have been demonstrated to be good substrates for calpain [18][19][20], activation of this protease has been shown in several models of cataract formation [21,22] and inhibition of calpain resulted in slower rate of cataract formation [23].…”

Section: Introductionmentioning

confidence: 99%

Calcium-Dependent Proteolysis in Rabbit Lens Epithelium after Oxidative Stress

Andersson

Sjöstrand²,

Petersen³

et al. 1998

Ophthalmic Res

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The purpose of this study was to examine changes in calcium-dependent proteolytic activity in the lens epithelium from whole rabbit lenses exposed to long-term oxidative stress at near physiological levels. Rabbit lenses, incubated in 50 µM H₂O₂ for 1 or 24 h, were checked for clarity and morphological changes in the epithelium. Proteolytic activity was measured in the epithelium using a fluorogenic synthetic substrate; N-succinyl-Leu-Tyr-7-amino-4-methylcoumarin, both in the presence and the absence of calcium (1 mM Ca²⁺ and 5 mM EDTA respectively). The effect on transparency and morphology of the epithelium following a 1-hour incubation in 100 µM H₂O₂ was also studied. Lenses incubated in 50 µM H₂O₂ were clear even after 24 h. After a 1-hour incubation in 50 µM H₂O₂ the epithelium of the exposed lens appeared normal. However, after 24 h the epithelium cells appeared swollen and microscopical examination showed extensive intracellular and subepithelial vacuolization. Incubation in 100 µM H₂O₂ for 1 h caused loss of transparency; vacuole formation, globulization of the superficial lens fibers and death of the epithelial cells. There was a 55% increase in calcium-dependent proteolytic activity after 1 h in 50 µM H₂O₂, implying a role for the calcium-activated protease calpain in oxidatively induced cataract.

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“…Both the major lens pro teins, the crystallins, and cytoskelctal proteins like vimentin, actin, spectrin and beaded fila ments are degraded by calpain resulting in fragments similar to those produced in cata ract models [9,[14][15][16]. The major gap junc tion protein, MP26, is also degraded by cal pain [17], Another fact that indicates the importance of calpain in cataract formation is the finding that calpain inhibitors, like E-64 slow the rate of cataract formation in cultured lenses as well as in the whole animal [ 18].…”

mentioning

confidence: 99%

Calpains in the Human Lens: Relations to Membranes and Possible Role in Cataract Formation

Andersson

Sjöstrand²,

Karlsson³

1996

Ophthalmic Res

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Calpains are Ca-activated neutral proteases present in all cells together with an endogenous inhibitor, calpastatin. Proposed substrates are; cytoskeletal proteins like microtubules and actin, protein kinases such as PKC and membrane-bound enzymes like Ca-ATPase and the Ca-channel. In lenses from different species calpains have been detected in decreasing amounts from the epithelium to the cortex to the nucleus. Several substrates for calpain in the lens have been demonstrated: crystallins, vimentin, actin, beaded filaments and MP26 among others. Both studies on animal models and capsulor-hexis indicate that calpains are mainly involved in cortical cataract.

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Degradation of actin and vimentin by calpain II, a Ca²⁺‐dependent cysteine proteinase, in bovine lens

Cited by 49 publications

References 17 publications

Effect of cold preservation on intracellular calcium concentration and calpain activity in rat sinusoidal endothelial cells

Effect of cold preservation on intracellular calcium concentration and calpain activity in rat sinusoidal endothelial cells

Calcium-Dependent Proteolysis in Rabbit Lens Epithelium after Oxidative Stress

Calpains in the Human Lens: Relations to Membranes and Possible Role in Cataract Formation

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Degradation of actin and vimentin by calpain II, a Ca2+‐dependent cysteine proteinase, in bovine lens

Cited by 49 publications

References 17 publications

Effect of cold preservation on intracellular calcium concentration and calpain activity in rat sinusoidal endothelial cells

Effect of cold preservation on intracellular calcium concentration and calpain activity in rat sinusoidal endothelial cells

Calcium-Dependent Proteolysis in Rabbit Lens Epithelium after Oxidative Stress

Calpains in the Human Lens: Relations to Membranes and Possible Role in Cataract Formation

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Product

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Degradation of actin and vimentin by calpain II, a Ca²⁺‐dependent cysteine proteinase, in bovine lens