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Anti-Wrinkling And Anti-Melanogenic Effect Of Pradosia Mutisii Methanol Extract Part 2

Mar 31, 2023

4. Materials and MethodsClick on Cistanche Tubulosa for Whitening

4.1. Materials

Cistanche also has the function of promoting collagen production, which can increase the elasticity and luster of the skin and help repair damaged skin cells. Cistanche Phenylethanol Glycosides have a significant down-regulating effect on tyrosinase activity, and the effect on tyrosinase is shown to be competitive and reversible inhibition, which can provide a scientific basis for developing and utilizing the whitening ingredients in Cistanche. Therefore, cistanche has a key role in skin whitening. It can inhibit melanin production to reduce discoloration and dullness; and promote collagen production to improve skin elasticity and radiance. Due to the widespread recognition of these effects of cistanche, many skin whitening products have begun to infuse herbal ingredients such as Cistanche to meet consumer demand, thus increasing the commercial value of Cistanche in skin whitening products. In summary, the role of cistanche in skin whitening is crucial. Its antioxidant effect and collagen-producing effect can reduce discoloration and dullness, improve skin elasticity and luster, and thus achieve a whitening effect. Also, the wide application of Cistanche in skin whitening products demonstrates that its role in commercial value cannot be underestimated.

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The HaCaT, B16F10, and HEK293 cells were purchased from the American Type Culture Collection (Rockville, MD, USA). Neonatal, primary HDF cells (SKU: FC-0001) were obtained from Lifeline (Oceanside, CA, USA). The MTT, fetal bovine serum (FBS), phosphate-buffered saline (PBS), penicillin, and Dulbecco’s modified Eagle’s medium (DMEM) were purchased from Gibco (Grand Island, NY, USA). L-3,4-dihydroxyphenylalanine (L-DOPA), 5-hydroxy-2-hydroxymethyl-4H-pyranone (kojic acid), monophenol monooxygenase (mushroom tyrosinase), 4-hydroxyphenyl-β-D-glucopyranoside (arbutin), α-melanocyte stimulating hormone (α-MSH), polyethyleneimine (PEI), 1-diphenyl-2 picryl-hydrazyl (DPPH), 2,20 -casino-bis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt (ABTS), hydrogen peroxide (H2O2), retinol (RE), ascorbic acid (AA), and 6-diamidino-2-phenylindole (DAPI) were purchased from Sigma–Aldrich (St. Louis, MO, USA). TRIzol reagent was purchased from Thermo Fisher Scientific (Waltham, MA, USA). The primer sets for the polymerase chain reaction were synthesized by Macrogen (Seoul, Korea), and the PCR premix was purchased from Bio-D Inc. (Seoul, Korea). Phospho- or total forms of p38, ERK, JNK, and β-actin were obtained from Cell Signaling Technology (Beverly, MA, USA).

4.2. Compound Analysis from Pm-ME by UHPLC, Coupled to Negative Electrospray Ionization High-Resolution Tandem Mass Spectrometry (UPLC/HRMS)

A 95% methanol extract of P. mutisii (Pm-EE) was purchased from Korea Plant Extract Bank (Daejeon, Korea). Compound analysis was performed by UPLC/HRMS (Orbitrap) analyses using the Shimadzu Ultra Performance LCMS 8050 system (Shimadzu, Kyoto, Japan) with a triple quadrupole mass spectrometer equipped with electrospray ionization (ESI) source operating in negative mode. Lab Solutions software version 5.2 (Shimadzu) was used as reported previously [68,69]. The sample solutions were injected into a reversed-phase column (BEH C8, 1.7 µm, 2.1 mm × 150 mm, Waters, Milford, MA, USA) with appropriate pre-columns. The column was maintained at 40 ◦C. The mobile phase consisted of a mixture of aqueous solutions of 10 mM formic acid (solvent A) and acetonitrile (solvent B) at a flow rate of 0.25 mL/min. The linear gradient and isocratic fellows of the mobile phase were 5% B for 0.8 min, 5–10% B for the next 0.4 min, isocratic 10% B for 0.70 min, 10–15% B for the next 0.5 min, isocratic 15% B for 1.30 min, 15–21% B for 1.30 min, isocratic 21% B for 1.20 min, 21–27% B for next 0.50 min, then 27–50% B for 3.30 min, 50–100% B for 2.00 min, isocratic 100% B for 1.00 min, and 100–5% B over 5 min. At the end of the program, the column was equilibrated under the initial conditions for 2.70 min. The pressure ranged from 45 to 50 MPa during the chromatographic run. The effluent was introduced into an electrospray source (interface temperature 300 ◦C, heat block temperature 400 ◦C, and capillary voltage 3.0 kV). Argon was used as the collision gas and nitrogen was the nebulizing gas. The interface between the liquid chromatography and the mass spectrometry detector was conducted using ESI. After the precursor ion full scan in the negative ion mode (i.e., [M-H]−), the product ions were determined using tandem mass spectrometry. To achieve high specificity in addition to high sensitivity, we used analysis in the multiple reaction monitoring modes. 

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4.3. Cell Culture

HaCaT cells (a human keratinocyte cell line), B16F10 cells (a murine melanocyte cell line), and HDF cells (a human fibroblast cell line) were cultured in DMEM supplemented with 10% FBS and 1% penicillin–streptomycin, while HEK293 cells (a human embryonic kidney cell line) were incubated in DMEM supplemented with 5% FBS and 1% penicillin–streptomycin. All cells were kept at 37 ◦C in a 5% humidified incubator.

4.4. Cell Viability Assay

The HaCaT cells were seeded at a density of 4 × 104 cells per well in a 96-well plate for 24 h, and then treated with Pm-ME for 24 h. The B16F10 cells were seeded at a density of 1 × 104cells per well in a 96-well plate and treated under the same conditions. The HDF cells were seeded at a density of 1 × 105cells per mL in a 96-well plate for 24 h. Cell viability for the previously mentioned cell lines was measured using the MTT assay, in which cells were first incubated with 10 µL/well of MTT solution for 3 h and then treated with 100 µL of MTT stopping solution (10% sodium dodecyl sulfate with 10% HCl). After 8 h, the absorbance of the solubilized formazan was measured at 570 nm using an optical density reader (BioTek, Winooski, VT, USA). 

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4.5. Free Radical Scavenging Activity

The radical scavenging activity of Pm-ME was determined using ABTS assay. The ABTS assay was performed as reported previously [70]. Briefly, 7.4 mM ABTS and 2.4 mM potassium persulfate solutions were mixed at a 1:1 ratio and incubated at room temperature overnight to generate ABTS radicalization. Then different concentrations of Pm-ME (0–200 µg/mL) or AA (100 µg/mL) were mixed with the ABTS solution and transferred to a 96-well plate, followed by an incubation period of 30 min at 37 ◦C. The absorbance was measured at 730 nm. The ABTS scavenging effect was calculated as follows:

ABTS scavenging effect (%) = [(A0−A1)/A100] × 100

where A0 is the absorbance of ABTS and A1 is the absorbance of samples. 

4.6. DAPI Staining

The HaCaT cells were seeded at a density of 4 × 105 cells/mL in a 12-well plate containing previously sterilized, round glass coverslips. After 24 h, cells were treated with Pm-ME for 30 min, washed with PBS, and treated with H2O2 (50 µM) for 24 h. Cells were washed twice with PBS and fixed with 1 mL of 3.7% paraformaldehyde in PBS for 10 min. Cells were washed with PBS two more times, stained with DAPI reagent (1 µL/mL) for 30 min, and then washed with PBS two more times. The cover slip was then mounted on a rectangular glass slide using a mounting solution and left to dry at room temperature for 24 h [71]. Samples were examined using a Nikon Eclipse Ti fluorescence microscope (Nikon, Tokyo, Japan).

4.7. UVB Irradiation and the Morphological Change Assay

The HaCaT cells were seeded at a density of 4 × 105 cells/mL in a 6-well plate. Cells were treated with Pm-ME for 30 min, washed with PBS, and then subjected to 30 mJ/cm2 of UVB radiation (absorbance peak at 312 nm) using a UVB lamp (Bio-link BLX-312, Vilber Lourmat, Collegien, France) fitted with a Kodak Kodacel K6808® filter that eliminates all wavelengths below 290 nm, as reported previously [72]. After UVB treatment, cells were treated for 24 h with Pm-ME according to previous papers [36]. Morphological changes were assessed using an inverted phase-contrast microscope (Olympus, Tokyo, Japan) attached to a video camera with NIH imaging software (Bethesda, Maryland, USA). 

4.8. Semi-Quantitative RT-PCR Analysis

The HaCaT cells were seeded at a density of 4 × 105cells/mL in a 12-well plate. For UVB analysis, cell treatments were carried out as previously described in the previous section. For H2O2 treatment, cells were also seeded at a density of 4 × 105cells/mL in a 12-well plate, treated with Pm-ME for 30 min, washed with PBS, and then treated with H2O2 (50 µM) for 24 h. To determine the Pm-ME moisturizing effect on HaCaT cells, they were first treated with the compound (0–100 µg/mL) and then subjected to mRNA extraction. For determining the role of MAPK in skin aging and moisturizing, HaCaT cells were pretreated for 30 min with 20 µM of SB203580 (p38 inhibitor), SP600125 (a JNK inhibitor), followed by incubation with H2O2 (50 µM) for 24 h, and mRNA was extracted and the levels of MMP-9 and COX-2 was quantified. For determining ERK’s role, HaCaT cells were treated with 20 µM of ERK inhibitor (U0126) alone or with Pm-ME (100 µg/mL) for 24 h, after which HAS-2 levels were measured. For determining the effect of Pm-ME on Col1A1 expression, HDF cells were seeded at a density of 1 × 105 cells per mL in a 6-well plate for 24 h, treated with Pm-ME (0–100 µg/mL) for 24 h, and then subjected to mRNA extraction. For determining if Pm-ME could recover gene expression of collagen decreased after UVR and ROS exposure, HDF cells were seeded at a density of 1 × 105 cells per mL in a 6-well plate for 24 h, treated with Pm-ME (0–100 µg/mL) for 30 min, subjected to H2O2 (50 µM) or UVB radiation (30 mJ/cm2 ), and further cultivated with Pm-ME (0–100 µg/mL) for 24 h. Total mRNA was extracted using TRIzol reagent according to the manufacturer’s instructions. Semiquantitative RT-PCR assay was carried out using MuLV reverse transcriptase, as previously described [37]. The RNA (1 µg) was incubated with oligo-dT15 at 70 ◦C for 5 min and mixed with a 5× first-strand buffer, 10 mM of dNTPs and 0.1 M dithiothreitol, then further incubated at 37 ◦C for 5 min, and for 60 min following the addition of MuLV reverse transcriptase (2 U). The reactions were finished at 70 ◦C for 10 min and the total RNA was removed by adding RNase H. The PCR reaction was conducted with the incubation mixture (2 µL cDNA, 4 M 50 and 30 primers, 10× buffer (10 mM Tris–HCl, pH 8.3, 50 mM KCl, 0.1% Triton X-100), 250 µM of dNTPs, 25 mM of MgCl2 and 1 unit of Taq polymerase (Promega, Madison, WI, USA)) under the following incubation conditions: a 45 s denaturation time at 94 ◦C, annealing time of 45 s at 55–60 ◦C, an extension time of 60 s at 72 ◦C and final extension of 7 min at 72 ◦C after 25–30 cycles. The primers (Bioneer, Seoul, Korea) used in this experiment are listed in Table 1.                  

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4.9. Plasmid Transfection and Luciferase Reporter Gene Assay 

For the luciferase reporter gene assay, HEK293 and HDF cells were first seeded at a density of 1 × 105 cells/well in 24-well plates. Both cell lines were then transfected with pCMV0Red Fireflfly Luc plasmids containing 1 kb of Col1A1 promoter region and β-galactosidase (as a transfection control) genes (0.8 µg/mL). Transfection was achieved using the PEI method for 24 h. This was followed by treatment with the compound (0–100 µg/mL) for a further 24 h. Retinol (10 µg/mL), a Col1A1 gene upregulating compound [60], was used as a positive control. Luciferase activity was measured according to the Luciferase Assay System (Promega), as previously reported [37]. Cell lysates were centrifuged at maximum speed for 10 min in an Eppendorf microcentrifuge. Then, 50 µL of the supernatant fraction was incubated with 50 µL of luciferase substrate, and the relative luciferase activity was determined with a Luminoskan Ascent (Thermo Labsystems Oy, Helsinki, Finland). Luciferase activity was normalized to β-galactosidase activity, and measured at 405 nm, by enzymatic reaction with X-gal and lysate for 5 min at 37 ◦C.

4.10. Melanogenesis and Melanin Secretion Assays

The B16F10 cells were treated with α-MSH (100 nM) and either Pm-ME (0–100 µg/mL) or arbutin (1 mM) for 48 h. To determine the melanin secretion from cells, the absorbance of the cell culture medium was measured at 475 nm using a Spectramax 250 microplate reader (Molecular Devices, San Jose, CA, USA). Cells were washed with cold PBS and harvested. For measurement of melanin content, cells were lysed with 20 mL cell lysis buffer (50 mM Tris-HCl pH 7.5, 20 mM NaF, 25 mM β-glycerolphosphate pH 7.5, 120 mM NaCl, and 2% NP-40 in distilled water) and centrifuged at 12,000 rpm for 10 min. The supernatants were removed and the pellet was dissolved in 100 µL 1 M NaOH containing 10% DMSO at 60 ◦C for 30 min. The absorbance of each fraction was measured at 405 nm using a Spectramax 250 microplate reader (Molecular Devices, San Jose, CA, USA) [36]. 

4.11. Tyrosinase Assay

For determining the tyrosinase enzyme activity, 50 mL of L-DOPA, 50 mL of Pm-ME (0–400 µg/mL), or 300 µM of Kojic acid were incubated for 15 min with mushroom tyrosinase (100 U/mL) at room temperature. The absorbance of each sample was measured at 475 nm using a Spectramax 250 microplate reader (Molecular Devices, San Jose, CA, USA). 

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4.12. Western Blot Analysis 

The HaCaT cells were pretreated with Pm-ME (0–100 µg/mL) for 30 min and then treated with H2O2 (50 µM) for 24 h. Cell lysates were prepared as previously described by Park et al. [73]. Lysates were subjected to sodium dodecyl sulfate–polyacrylamide gel electrophoresis followed by transfer to polyvinylidene fluoride membranes. Using specific antibodies, total and phosphorylated forms of target proteins were detected and visualized by chemiluminescence reagents. 

4.13. Statistical Analysis

All data are presented as the mean ± standard deviation of at least three independent experiments. A Mann–Whitney test was used to compare statistical differences between experimental and control groups. A p-value < 0.05 was considered statistically signifificant. All statistical analyses were conducted using the SPSS program (SPSS, Chicago, IL, USA).

Data availability: The data used to support the findings of this study are available from the corresponding author upon request.

Author Contributions: L.R.L., M.-Y.K., B.C.Y., and J.Y.C. designed the experiments. L.R.L. performed the laboratory assays. L.R.L., M.-Y.K., B.C.Y., and J.Y.C. analyzed the data. L.R.L., M.-Y.K., B.C.Y., and J.Y.C. wrote the manuscript. All authors read and approved the manuscript. 

Funding: This research including the APC was funded by the National Cancer Center, Republic of Korea, (Grant number: 1810960-1). 

Conflicts of Interest: The authors have no conflicts of interest to declare.

Abbreviations 

Pm-ME  P. mutisii methanol extract 

MMPs    matrix metalloproteinases

α-MSH  α-melanocyte-stimulating hormone
ROS       reactive oxygen species 
KA         kojic acid 

L-DOPA L-3,4-dihydroxyphenylalanine 

UV         ultraviolet light 
DAPI      6-diamidino-2-phenylindole 
H2O2    hydrogen peroxide 
MAPK    mitogen-activated protein kinases 
ERK       extracellular signal-regulated kinase 
JNK       c-Jun-N-terminal kinase
MTT      3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide 
ABTS     2,2’-Azino-bis (3-ethylbenzothiazoline-6-sulphonic acid) diammonium salt 
AA        ascorbic acid 
RT-PCR reverse transcription-polymerase chain reaction

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