Changes in cellular degradation activity in young and old worker honeybees (Apis mellifera)

Hsu, Chin-Yuan; Chuang, Yi‐Hsuan; Chan, Yu-Pei

doi:10.1016/j.exger.2013.12.003

Cited by 17 publications

(26 citation statements)

References 66 publications

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“…Immunofluorescence detection and immunoblot analysis of Lamp1 have confirmed the rising number of lysosomes in aged cells [168], [169], [170]. Regarding the lysosomal activity several studies postulated that lysosomal activity increases during cellular aging [17], [147], [169], while others reported the opposite direction [171], [172]. The limitation in CMA is that only Hcs70 containing lysosomes, responsible for substrate translocation, are active for CMA [165].…”

Section: Proteostasis In Agingmentioning

confidence: 87%

Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence

et al. 2017

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Aging is a complex phenomenon and its impact is becoming more relevant due to the rising life expectancy and because aging itself is the basis for the development of age-related diseases such as cancer, neurodegenerative diseases and type 2 diabetes. Recent years of scientific research have brought up different theories that attempt to explain the aging process. So far, there is no single theory that fully explains all facets of aging. The damage accumulation theory is one of the most accepted theories due to the large body of evidence found over the years. Damage accumulation is thought to be driven, among others, by oxidative stress. This condition results in an excess attack of oxidants on biomolecules, which lead to damage accumulation over time and contribute to the functional involution of cells, tissues and organisms. If oxidative stress persists, cellular senescence is a likely outcome and an important hallmark of aging. Therefore, it becomes crucial to understand how senescent cells function and how they contribute to the aging process. This review will cover cellular senescence features related to the protein pool such as morphological and molecular hallmarks, how oxidative stress promotes protein modifications, how senescent cells cope with them by proteostasis mechanisms, including antioxidant enzymes and proteolytic systems. We will also highlight the nutritional status of senescent cells and aged organisms (including human clinical studies) by exploring trace elements and micronutrients and on their importance to develop strategies that might increase both, life and health span and postpone aging onset.

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Section: Proteostasis In Agingmentioning

confidence: 87%

Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence

et al. 2017

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“…The protein concentration was determined using a protein assay reagent (500-0006; Bio-Rad Laboratories, Hercules, CA, USA). The activity of the 20S proteasome was quantified using a 20S Proteasome Activity Assay Kit (APT280; Chemicon International, Temecula, CA, USA) according to the manufacturer's instructions, as described previously (Hsu et al 2014). The specific activity was expressed as 7-amino-4-methylcoumarin (AMC) pmol min −1 mg −1 of protein.…”

Section: S Proteasome Activitymentioning

confidence: 99%

“…Acid phosphatase is one of the acid hydrolases present in the lysosome. Thus, we evaluated lysosomal activity by measuring acid phosphatase activity with an Acid Phosphatase Assay Kit (CS0740; Sigma, Saint Louis, MO, USA) according to the manufacturer's instructions, as described previously (Hsu et al 2014). The specific activity was expressed as milliunits (mUnits) mg −1 .…”

Section: Lysosomal Activitymentioning

confidence: 99%

“…Lysosomes play important roles in cellular degradation. Acid phosphatase is one of the acid hydrolases found in lysosomes that has been used as a classical marker of lysosome activity (Hsu et al 2014). Therefore, we measured acid phosphatase activity to evaluate lysosome function.…”

Section: Lysosome Activity and Densitymentioning

confidence: 99%

“…Microtubule-associated protein 1 light chain 3 (LC3) (Atg8) serves as a regulatory protein for macroautophagy. Specifically, microtubule-associated protein 1 light chain 3-II (LC3-II) is a membranebound form of LC3 that localizes to autophagosomes and can be used as a biomarker of macroautophagic activity (Kabeya et al 2000;Hsu et al 2014). 70-kD heat shock cognate protein (Hsc 70) recognizes substrate proteins containing the KFERQ pentapeptide motif and subsequently binds to the lysosomal membrane receptor Lamp 2a.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Ambient temperature reduction extends lifespan via activating cellular degradation activity in an annual fish (Nothobranchius rachovii)

Hsu

2015

AGE

Self Cite

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Ambient temperature reduction (ATR) can extend the lifespan of organisms, but the underlying mechanism is poorly understood. In this study, cellular degradation activity was evaluated in the muscle of an annual fish (Nothobranchius rachovii) reared under high (30 °C), moderate (25 °C), and low (20 °C) ambient temperatures. The results showed the following: (i) the activity of the 20S proteasome and the expression of polyubiquitin aggregates increased with ATR, whereas 20S proteasome expression did not change; (ii) the expression of microtubule-associated protein 1 light chain 3-II (LC3-II) increased with ATR; (iii) the expression of lysosome-associated membrane protein type 2a (Lamp 2a) increased with ATR, whereas the expression of the 70-kD heat shock cognate protein (Hsc 70) decreased with ATR; (iv) lysosome activity increased with ATR, whereas the expression of lysosome-associated membrane protein type 1 (Lamp 1) did not change with ATR; and (v) the expression of molecular target of rapamycin (mTOR) and phosphorylated mTOR (p-mTOR) as well as the p-mTOR/mTOR ratio did not change with ATR. These findings indicate that ATR activates cellular degradation activity, constituting part of the mechanism underlying the longevity-promoting effects of ATR in N. rachovii.

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Energy-regulated molecules maintain young status in the trophocytes and fat cells of old queen honeybees

Hsu

2014

Biogerontology

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Queen honeybees (Apis mellifera) have much longer lifespans than worker bees. Energy-regulated molecules in the trophocytes and fat cells of workers during aging have been determined, but are unknown in queen bees. In the present study, energy-regulated molecules were evaluated in the trophocytes and fat cells of young and old queen bees. Adenosine monophosphate-activated protein kinase α2 (AMPK-α2), phosphorylated AMPK-α2 (pAMPK-α2), and cAMP-specific phosphodiesterases activity increased with aging. The pAMPK-α2/AMPK-α2 ratio and AMPK activity; adenosine triphosphate (ATP), adenosine diphosphate (ADP), and adenosine monophosphate (AMP) concentrations; the ADP/ATP ratio and the AMP/ATP ratio; the cyclic adenosine monophosphate concentration; forkhead box protein O expression; Silent information regulator T1 (SirT1) expression and activity; and peroxisome proliferator-activated receptor-α (PPAR-α) expression were not significantly different between young and old queen bees. These results show that energy-regulated molecules maintain a youthful status in the trophocytes and fat cells of queen bees during aging. These cells seem to have longevity-promoting mechanisms and may clarify the secret of longevity in queen bees.

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Changes in cellular degradation activity in young and old worker honeybees (Apis mellifera)

Cited by 17 publications

References 66 publications

Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence

Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence

Ambient temperature reduction extends lifespan via activating cellular degradation activity in an annual fish (Nothobranchius rachovii)

Energy-regulated molecules maintain young status in the trophocytes and fat cells of old queen honeybees

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