αB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells

McGreal, Rebecca; Kantorow, Wanda Lee; Chauss, Daniel; Wei, Jianning; Brennan, Lisa A.; Kantorow, Marc

doi:10.1016/j.bbagen.2012.04.004

Cited by 51 publications

(48 citation statements)

References 73 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similarly, alpha-crystallins (HSPB4 and HSPB5) and HSPB6 prevent apoptotic cell death through interaction with pro-apoptotic proteins of the Bcl-2 family, such as Bax and Bcl-X(S), intercepting their translocation from cytosol into mitochondria (Fan et al 2005b;Mao et al 2004). Additionally, alpha-crystallins preserve mitochondrial integrity and inhibit apoptosis by interacting with cytochrome c and caspase subtypes and by repressing caspase-3 activation (Bakthisaran et al 2015;Mao et al 2004;McGreal et al 2012). Detailed information on the interplay between sHSPs and the extrinsic and intrinsic apoptotic pathways can be found in excellent recent articles (Acunzo et al 2012;Arrigo and Gibert 2014;Bakthisaran et al 2015;Mymrikov et al 2011).…”

Section: Shsps In Cancermentioning

confidence: 99%

Small heat shock proteins in ageing and age-related diseases

Charmpilas

Kyriakakis

Tavernarakis

2017

Cell Stress and Chaperones

View full text Add to dashboard Cite

Small heat shock proteins (sHSPs) are gatekeepers of cellular homeostasis across species, preserving proteome integrity under stressful conditions. Nonetheless, recent evidence suggests that sHSPs are more than molecular chaperones with merely auxiliary role. In contrast, sHSPs have emerged as central lifespan determinants, and their malfunction has been associated with the manifestation of neurological disorders, cardiovascular disease and cancer malignancies. In this review, we focus on the role of sHSPs in ageing and ageassociated diseases and highlight the most prominent paradigms, where impairment of sHSP function has been implicated in human pathology.

show abstract

Section: Shsps In Cancermentioning

confidence: 99%

Small heat shock proteins in ageing and age-related diseases

Charmpilas

Kyriakakis

Tavernarakis

2017

Cell Stress and Chaperones

View full text Add to dashboard Cite

show abstract

“…The early induction at this location points to an active role of ABC in vivo. Although effects of ABC are reported in and discussed for the retina [49], both types of retinal degeneration showed almost no changes of ABC labeling in the retina itself.…”

Section: Discussionmentioning

confidence: 99%

Distribution of αB-Crystallin in the Central Retina and Optic Nerve Head of Different Mammals and its Changes during Outer and Inner Retinal Degeneration

May¹

2014

J Veterinar Sci Technol

View full text Add to dashboard Cite

Purpose: To investigate species differences in the distribution and localization of alpha B-crystallin (ABC) in the normal retina and optic nerve head region, and to describe changes during outer and inner retina degeneration. Material and methods:Animals studied included mice, rats, cats, pigs, cows, and monkeys. Sections of the optic nerve and central retina were labeled with antibodies against ABC and glial fibrillary acidic protein (GFAP).Results: ABC was located in astrocytes and Muller cells with different intensities. During outer retina degeneration (dystrophic rat and Abyssinian cat), only late stages showed an increase in ABC in the retina and optic nerve head. Inner retina degeneration in the glaucoma mouse model showed no increase of ABC. In the monkey glaucoma model, only the innermost layer of the optic nerve head showed increased labeling for ABC. Conclusions:The distribution of ABC is species dependent and is (excluding the mouse) present in the nerve fiber layer of the retina and in the optic nerve head (localization of astrocytes). Chronic retinal degeneration does not necessarily lead to an over-expression of ABC. While in outer retinal degeneration induction was predominantly present in late stages, pressure-induced glaucoma led to a specific increase in ABC already in early stages indicating a local stress-response in this region.

show abstract

“…Consistently, the eye lens has evolved multiple protective and repair systems to preserve its transparent function in the face of environmental insults (63). These include abundant anti-oxidant systems (64 -66), protein protective systems (67)(68)(69), protein salvaging systems (70,71), protein repair systems (72)(73)(74), as well autophagy systems for clearance of damaged organelles (41)(42)(43). Loss of the functions of these systems results in a range of lens effects including, but not limited to, accumulation of damaged and modified proteins (75)(76)(77), apoptosis of lens cells (78,79), and cataract formation (73,80).…”

Section: Discussionmentioning

confidence: 99%

Integrin αVβ5-mediated Removal of Apoptotic Cell Debris by the Eye Lens and Its Inhibition by UV Light Exposure

Chauss

Brennan

Бакина

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Accumulation of apoptotic material is toxic and associated with cataract and other disease states. Identification of mechanisms that prevent accumulation of apoptotic debris is important for establishing the etiology of these diseases. The ocular lens is routinely assaulted by UV light that causes lens cell apoptosis and is associated with cataract formation. To date, no molecular mechanism for removal of toxic apoptotic debris has been identified in the lens. Vesicular debris within lens cells exposed to UV light has been observed raising speculation that lens cells themselves could act as phagocytes to remove toxic apoptotic debris. However, phagocytosis has not been confirmed as a function of the intact eye lens, and no mechanism for lens phagocytosis has been established. Here, we demonstrate that the eye lens is capable of phagocytizing extracellular lens cell debris. Using high throughput RNA sequencing and bioinformatics analysis, we establish that lens epithelial cells express members of the integrin ␣V␤5-mediated phagocytosis pathway and that internalized cell debris co-localizes with ␣V␤5 and with RAB7 and Rab-interacting lysosomal protein that are required for phagosome maturation and fusion with lysosomes. We demonstrate that the ␣V␤5 receptor is required for lens epithelial cell phagocytosis and that UV light treatment of lens epithelial cells results in damage to the ␣V␤5 receptor with concomitant loss of phagocytosis. These data suggest that loss of ␣V␤5-mediated phagocytosis by the eye lens could result in accumulation of toxic cell debris that could contribute to UV light-induced cataract formation.

show abstract

αB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells

Cited by 51 publications

References 73 publications

Small heat shock proteins in ageing and age-related diseases

Small heat shock proteins in ageing and age-related diseases

Distribution of αB-Crystallin in the Central Retina and Optic Nerve Head of Different Mammals and its Changes during Outer and Inner Retinal Degeneration

Integrin αVβ5-mediated Removal of Apoptotic Cell Debris by the Eye Lens and Its Inhibition by UV Light Exposure

Contact Info

Product

Resources

About