scholarly journals A Comprehensive Review of the Cosmeceutical Benefits of Vanda Species (Orchidaceae)

2015 ◽  
Vol 10 (8) ◽  
pp. 1934578X1501000 ◽  
Author(s):  
Hazrina Hadi ◽  
Syarifah Nazira Said Razali ◽  
Ammar Ihsan Awadh
Keyword(s):  
Cytochrome C ◽  
Protein Expression ◽  
Cytochrome C Oxidase ◽  
Binding Capacity ◽  
Active Agent ◽  
Fold Increase ◽  
Skin Hydration ◽  
Water Evaporation ◽  
Structural Function ◽  
Water Binding

Orchidaceae is the largest family of flowering plants with over 35000 species and 850 genera. About 3300 species of orchids are found in Malaysia and the diversity is highest in the Main, Keledang, Bintang and Tahan Ranges. Apart from being prized for their beauty, orchids have long been used by humans for medicinal purposes. Today the uses of orchids have been expanded to the food and cosmetics industries. Many cosmeceutical companies use orchid extracts as an active ingredient in their products. Previous studies provide riveting insights into the potential uses of orchid extracts as an active agent in cosmetics. This paper describes the cosmeceutical potential of orchids as an anti-aging, and skin moisturizing agent. Orchid extracts from Vanda coerulea and V. teres delay aging caused by reactive oxygen species (ROS) following UV irradiation through their antioxidant and anti-inflammatory activity. These extracts also show anti-aging properties by stimulating cytochrome c oxidase (complex IV), which is part of the electron transport chain in mitochondria. Stimulation of cytochrome c oxidase improves the respiratory function of mitochondria in keratinocytes. The presence of mucilage in orchids enables them to maintain skin hydration. Mucilage functions as a moisturizer and emollient due to its high water binding capacity. Additionally, orchid extracts provide skin hydration by stimulating aquaporin 3 (AQP3) and LEKTI protein expression. The presence of AQP3 leads to a five-fold increase in water permeability, which subsequently increases stratum corneum hydration. Increased LEKTI protein expression mediated by orchid extracts reduces the degradation of desmoglein-1 and enhances the structural function of desmosomes, which play important roles in preventing water evaporation.

Cytochrome c oxidase is regulated by modulations in protein expression and mitochondrial membrane phospholipid composition in estivating African lungfish

2010 ◽  
Vol 298 (3) ◽  
pp. R608-R616 ◽  
Author(s):  
N. T. Frick ◽  
J. S. Bystriansky ◽  
Y. K. Ip ◽  
S. F. Chew ◽  
J. S. Ballantyne
Keyword(s):  
Cytochrome C ◽  
Protein Expression ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Membrane ◽  
Translational Regulation ◽  
Phospholipid Composition ◽  
Liver Mitochondria ◽  
Membrane Phospholipids ◽  
Tissue Specific ◽  
African Lungfish

We examined some of the potential mechanisms lungfish ( Protopterus dolloi ) use to regulate cytochrome c oxidase (CCO), during metabolic depression. CCO activity was reduced by 67% in isolated liver mitochondria of estivating fish. This was likely accomplished, in part, by the 46% reduction in CCO subunit I protein expression in the liver. No change in the mRNA expression levels of CCO subunits I, II, III, and IV were found in the liver, suggesting CCO is under translational regulation; however, in the kidney, messenger limitation may be a factor as the expression of subunits I and II were depressed (∼10-fold) during estivation, suggesting tissue-specific mechanisms of regulation. CCO is influenced by mitochondrial membrane phospholipids, particularly cardiolipin (CL). In P. dolloi , the phospholipid composition of the liver mitochondrial membrane changed during estivation, with a ∼2.3-fold reduction in the amount of CL. Significant positive correlations were found between CCO activity and the amount of CL and phosphatidylethanolamine within the mitochondrial membrane. It appears CCO activity is regulated through multiple mechanisms in P. dolloi , and individual subunits of CCO are regulated independently, and in a tissue-specific manner. It is proposed that altering the amount of CL within the mitochondrial membrane may be a means of regulating CCO activity during metabolical depression in the African lungfish, P. dolloi .

scholarly journals Cytochrome c oxidase III as a mechanism for apoptosis in heart failure following myocardial infarction

2009 ◽  
Vol 297 (4) ◽  
pp. C928-C934 ◽  
Author(s):  
Changgong Wu ◽  
Lin Yan ◽  
Christophe Depre ◽  
Sunil K. Dhar ◽  
You-Tang Shen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Myocardial Infarction ◽  
Heart Failure ◽  
Cytochrome C ◽  
Protein Expression ◽  
Cell Viability ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Gene

Cytochrome c oxidase (COX) is composed of 13 subunits, of which COX I, II, and III are encoded by a mitochondrial gene. COX I and II function as the main catalytic components, but the function of COX III is unclear. Because myocardial ischemia affects mitochondrial oxidative metabolism, we hypothesized that COX activity and expression would be affected during postischemic cardiomyopathy. This hypothesis was tested in a monkey model following myocardial infarction (MI) and subsequent pacing-induced heart failure (HF). In this model, COX I protein expression was decreased threefold after MI and fourfold after HF ( P < 0.05 vs. sham), whereas COX II expression remained unchanged. COX III protein expression increased 5-fold after MI and further increased 10-fold after HF compared with sham ( P < 0.05 vs. sham). The physiological impact of COX III regulation was examined in vitro. Overexpression of COX III in mitochondria of HL-1 cells resulted in an 80% decrease in COX I, 60% decrease in global COX activity, 60% decrease in cell viability, and threefold increase in apoptosis ( P < 0.05). Oxidative stress induced by H2O2 significantly ( P < 0.05) increased COX III expression. H2O2 decreased cell viability by 47 ± 3% upon overexpression of COX III, but only by 12 ± 5% in control conditions ( P < 0.05). We conclude that ischemic stress in vivo and oxidative stress in vitro lead to upregulation of COX III, followed by downregulation of COX I expression, impaired COX oxidative activity, and increased apoptosis. Therefore, upregulation of COX III may contribute to the increased susceptibility to apoptosis following MI and subsequent HF.

Tissue-specific regulation of cytochrome c oxidase subunit expression by thyroid hormone

2004 ◽  
Vol 286 (6) ◽  
pp. E968-E974 ◽  
Author(s):  
Treacey E. Sheehan ◽  
Ponni A. Kumar ◽  
David A. Hood
Keyword(s):  
Thyroid Hormone ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Fold Increase ◽  
Mitochondrial Respiratory Chain ◽  
Functional Changes ◽  
Mitochondrial Transcription Factor ◽  
Subunit Expression ◽  
Mitochondrial Transcription Factor A ◽  
Specific Regulation

The influence of thyroid hormone (T3) on respiration is partly mediated via its effect on the cytochrome c oxidase (COX) enzyme, a multi-subunit complex within the mitochondrial respiratory chain. We compared the expression of COX subunits I, III, Vb, and VIc and thyroid receptors (TR)α1 and TRβ1 with functional changes in COX activity in tissues that possess high oxidative capacities. In response to 5 days of T3 treatment, TRβ1 increased 1.6-fold in liver, whereas TRα1 remained unchanged. T3 also induced concomitant increases in the protein and mRNA expression of nuclear-encoded subunit COX Vb in liver, matched by a 1.3-fold increase in binding to a putative thyroid response element (TRE) within the COX Vb promoter in liver, suggesting transcriptional regulation. In contrast, T3 had no effect on COX Vb expression in heart. T3 produced a significant increase in COX III mRNA in liver but decreased COX III mRNA in heart. These changes were matched by parallel alterations in mitochondrial transcription factor A expression in both tissues. In contrast, COX I protein increased in both liver and heart 1.7- and 1.5-fold ( P < 0.05), respectively. These changes in COX I closely paralleled the T3-induced increases in COX activity observed in both of these tissues. In liver, T3 induced a coordinated increase in the expression of the nuclear (COX Vb) and mitochondrial (COX I) genomes at the protein level. However, in heart, the main effect of T3 was restricted to the expression of mitochondrial DNA subunits. Thus our data suggest that T3 regulates the expression of COX subunits by both transcriptional and posttranscriptional mechanisms. The nature of this regulation differs between tissues possessing a high mitochondrial content, like liver and heart.

scholarly journals δ-Aminolaevulinate synthase expression in muscle after contractions and recovery

1993 ◽  
Vol 291 (1) ◽  
pp. 219-223 ◽  
Author(s):  
M Takahashi ◽  
D T M McCurdy ◽  
D A Essig ◽  
D A Hood
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Biogenesis ◽  
Mrna Stability ◽  
Tibialis Anterior ◽  
Fold Increase ◽  
Mrna Levels ◽  
Mrna Content

The synthesis of haem has been postulated to be a key regulatory step in muscle mitochondrial biogenesis. We examined the expression of delta-aminolaevulinate synthase (ALAs), the regulatory enzyme of haem metabolism, in 10 Hz electrically stimulated and non-stimulated control rat tibialis anterior (TA) muscle. ALAs activity and mRNA levels were measured at 0, 18 and 48 h of recovery after 3 h of acute stimulation, or after 7 days of stimulation (3 h/day). ALAs activity in control muscles averaged 7.8 +/- 0.8 nmol/h per g (n = 30). After 3 h of stimulation and during recovery, no change in ALAs activity occurred. ALAs mRNA during the same time was unchanged except at 48 h of recovery, when it increased 1.3-fold above control (P < 0.05). After 7 days of stimulation, ALAs activity was unchanged at 0 h, but increased at 18 and 48 h of recovery to 2.0- and 1.8-fold above control (P < 0.05). ALAs mRNA was also increased, but to a level averaging 1.6-fold above control (P < 0.05) at all times, indicating an increased mRNA stability or synthesis. No change in the haem-containing enzyme cytochrome c oxidase (CYTOX) activity occurred after 3 h of stimulation in the red section of the TA. After 7 days of stimulation, the increase in CYTOX activity averaged 1.7-fold above control (P < 0.05) at all times. Thus the induction of ALAs during recovery after 7 days was regulated by factors which not only change ALAs mRNA content, but which also affect ALAs mRNA at translational or post-translational steps. This induction occurred despite a 1.7-fold increase in CYTOX, implying that a precursor-product relationship does not always exist.

Extension of enzyme half-life during quiescence in Artemia embryos

1993 ◽  
Vol 264 (1) ◽  
pp. R85-R89 ◽  
Author(s):  
T. J. Anchordoguy ◽  
G. E. Hofmann ◽  
S. C. Hand
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Half Life ◽  
Fold Increase ◽  
Artemia Franciscana ◽  
Protein Damage ◽  
Metabolic Enzyme ◽  
Catabolic Pathways ◽  
A Value

Encysted gastrulae of Artemia franciscana are known to enter a reversible state of quiescence in which biosynthetic and catabolic pathways are markedly suppressed. Given that these embryos can survive months of anoxia, we investigated their ability to extend the half-life of cytochrome-c oxidase (COX), a key metabolic enzyme, during anoxia. We calculate that the half-life of COX is extended to 101 days under anoxia, an estimated 77-fold increase compared with aerobic values. During conditions of aerobic acidosis, the half-life of COX was extended sevenfold to a value of 9.7 days. We propose that the extended lifetimes of COX in both cases may be due to suppressed mitochondrial proteolysis under depressed pH. The shorter enzyme half-life observed under the latter condition may be due to the availability of ATP for degradative processes during aerobic acidosis. We also suggest that the presence of oxygen in aerobic acidosis may lead to increased rates of protein damage due to autooxidation.

Protein kinase C-ε coimmunoprecipitates with cytochrome oxidase subunit IV and is associated with improved cytochrome-c oxidase activity and cardioprotection

2007 ◽  
Vol 293 (4) ◽  
pp. H2219-H2230 ◽  
Author(s):  
Dehuang Guo ◽  
Tiffany Nguyen ◽  
Mourad Ogbi ◽  
Huda Tawfik ◽  
Guochun Ma ◽  
...  
Keyword(s):  
At Risk ◽  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Fold Increase ◽  
P Fractions ◽  
Cytochrome Oxidase Subunit ◽  
Oxidase Subunit ◽  
Activity Measurements

We have utilized an in situ rat coronary ligation model to establish a PKC-ε cytochrome oxidase subunit IV (COIV) coimmunoprecipitation in myocardium exposed to ischemic preconditioning (PC). Ischemia-reperfusion (I/R) damage and PC protection were confirmed using tetrazolium-based staining methods and serum levels of cardiac troponin I. Homogenates prepared from the regions at risk (RAR) and not at risk (RNAR) for I/R injury were fractionated into cell-soluble (S), 600 g low-speed centrifugation (L), Percoll/Optiprep density gradient-purified mitochondrial (M), and 100,000 g particulate (P) fractions. COIV immunoreactivity and cytochrome- c oxidase activity measurements estimated the percentages of cellular mitochondria in S, L, M, and P fractions to be 0, 55, 29, and 16%, respectively. We observed 18, 3, and 3% of PKC-δ, -ε, and -ζ isozymes in the M fraction under basal conditions. Following PC, we observed a 61% increase in PKC-ε levels in the RAR M fraction compared with the RNAR M fraction. In RAR mitochondria, we also observed a 2.8-fold increase in PKC-ε serine 729 phosphoimmunoreactivity (autophosphorylation), indicating the presence of activated PKC-ε in mitochondria following PC. PC administered before prolonged I/R induced a 1.9-fold increase in the coimmunoprecipitation of COIV, with anti-PKC-ε antisera and a twofold enhancement of cytochrome- c oxidase activity. Our results suggest that PKC-ε may interact with COIV as a component of the cardioprotection in PC. Induction of this interaction may provide a novel therapeutic target for protecting the heart from I/R damage.

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