Journal: Investigative and Clinical Urology

Article Title: Suppression of CD81 promotes bladder cancer cell invasion through increased matrix metalloproteinase expression via extracellular signal-regulated kinase phosphorylation

doi: 10.4111/icu.2019.60.5.396

Figure Lengend Snippet: Increased expression and activity of MMP2/9 in CD81-knockdown bladder cancer cells. (A) Zymography for MMP activity. (B) Western blot analysis of MMP2 and MMP9. The culture supernatant was concentrated by an Amicon Ultra-2 Centrifugal Filter and MMP2/9 expression was analyzed using each specific antibody.

Article Snippet: Mouse polyclonal anti-CD81 antibody (Santa Cruz Biotechnology), rabbit anti-Akt antibody (Bioss Antibodies Inc., Woburn, MA, USA), rabbit anti-phospho-Akt antibody (Cell Signaling Technology, Beverly, CA, USA), mouse anti-ERK antibody (Bioss Antibodies Inc.), anti-phospho-ERK (Bioss Antibodies Inc.), rabbit anti-p38 antibody (Bioss Antibodies Inc.), rabbit anti-c-Jun N-terminal kinases (JNK) antibody (Bioss Antibodies Inc.), anti-phospho-JNK (Santa Cruz Biotechnology), rabbit anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Cusabio, Houston, TX, USA), rabbit anti-MMP2 antibody (Bioss Antibodies Inc.), rabbit anti-MMP9 antibody (Bioss Antibodies Inc.) were used as primary antibodies.

Techniques: Expressing, Activity Assay, Zymography, Western Blot

Journal: Investigative and Clinical Urology

Article Title: Suppression of CD81 promotes bladder cancer cell invasion through increased matrix metalloproteinase expression via extracellular signal-regulated kinase phosphorylation

doi: 10.4111/icu.2019.60.5.396

Figure Lengend Snippet: Screening for MMP2/9-associated signaling pathways in CD81-knockdown bladder cancer cells. MMP2/9-associated signaling pathways were analyzed in CD81-knockdown T24 (A) and J82 (B) bladder cancer cell lines. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as a housekeeping control. p-Akt, phospho-Akt; ERK, extracellular signal-regulated kinase; p-ERK, phospho-ERK; JNK, c-Jun N-terminal kinases; p-JNK, phospho-JNK.

Article Snippet: Mouse polyclonal anti-CD81 antibody (Santa Cruz Biotechnology), rabbit anti-Akt antibody (Bioss Antibodies Inc., Woburn, MA, USA), rabbit anti-phospho-Akt antibody (Cell Signaling Technology, Beverly, CA, USA), mouse anti-ERK antibody (Bioss Antibodies Inc.), anti-phospho-ERK (Bioss Antibodies Inc.), rabbit anti-p38 antibody (Bioss Antibodies Inc.), rabbit anti-c-Jun N-terminal kinases (JNK) antibody (Bioss Antibodies Inc.), anti-phospho-JNK (Santa Cruz Biotechnology), rabbit anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Cusabio, Houston, TX, USA), rabbit anti-MMP2 antibody (Bioss Antibodies Inc.), rabbit anti-MMP9 antibody (Bioss Antibodies Inc.) were used as primary antibodies.

Techniques:

Journal: BMC cancer

Article Title: Enhanced anti-cancer effect of AMTB hydrochloride via chitosan nanoparticles in pancreatic cancer.

doi: 10.1186/s12885-025-14356-w

Figure Lengend Snippet: Fig. 2 TRPM8 antagonist AMTB restricts pancreatic cancer cell migration and invasion. (A) Scratch assay showing reduced migration in AMTB-treated BxPC-3 and PANC-1 cells. (B) Transwell assay indicating decreased invasion in AMTB-treated cells. (C) Western blot analysis of EMT-related proteins and migration/invasion markers (MMP2, MMP9) in AMTB-treated cells. N = 3 (biological replicates)

Article Snippet: The relevant primary antibodies are as follows: GAPDH (5174 S, 1:1000, Cell signaling Technology [CST], Boston, USA), TRPM8 (ab85617, 1:1000, Abcam), E-cadherin (20874-1-AP, 1:20000, Proteintech, Wuhan, China), N-cadherin (AF4039, 1:500, Affinity Bioscience), Snail (CSB-PA004123, 1:1000, CUSABIO, Wuhan, China), MMP2 (CSB-PA003258, 1:1000, CUSABIO), and MMP9 (ab283575, 1:1000, Abcam).

Techniques: Migration, Wound Healing Assay, Transwell Assay, Western Blot

Journal: Molecular Systems Biology

Article Title: Synovial matrix turnover controls immune cell spatial patterning in inflammation resolution

doi: 10.1038/s44320-025-00149-7

Figure Lengend Snippet: Following differential expression analysis between newly defined AMP1-like fibroblast clusters of the Alivernini dataset, DEGs were prioritised based on DEG conservation between differential expression analysis methods edgeR and MAST, conservation in a newly performed MAST analysis of the Wei mouse dataset of STIA, log2FC and adjusted P values. ( A ) Ranks of the top ten prioritised matrisomal DEGs in active RA/remission lining and sub-lining fibroblasts. ( B ) Network analysis of protein abundances and correlations in Graphia. Each protein is represented by a dot. Protein clusters are grouped by colour, with orange proteins corresponding to proteins more abundant in RA, green proteins more abundant in OA, and purple and yellow proteins in neither. ( N = 12 for OA and N = 10 for RA). ( C ) Heatmaps of protein abundance for proteins found to be overrepresented in RA (orange) and OA (green) samples. Stars denote a P value < 0.05 through t test. ( N = 12 for OA and 10 for RA). ( D ) Abundance of Collagen-I and VI protein in OA and RA patient samples ( N = 12 and N = 10, respectively), each dot represents the abundance of a tryptic peptide. For Collagen-I chains Col1a1 and Col1a2 have been grouped. For Collagen-VI, chains Col6a1, Col6a2 and Col6a3 have been grouped. ( E ) The ratio of semi-tryptic collagen-I peptide abundance compared to the average tryptic peptide abundance, this is as an indicator of degradation for Collagen-I and -VI in OA and RA. Each dot represents the ratio for a single semi-tryptic peptide. ( N = 12 for OA and 10 for RA). ( F ) Supporting data from RA synovial biopsy ( N = 8) dataset. Semi-tryptic ratio of collagen-I and –VI based on relevant spectral counts. Tryptic spectral counts ( G ) and semi-tryptic ratio ( H ) from the same dataset as ( F ) but separated into lymphoid ( N = 4) and myeloid ( N = 4) endotypes for grouped collagen-I and –VI. P values for t tests are labelled above each dot plot. ( I ) Dot plot of genes for type VI collagen chains and its processing regulators in each AMP1-like fibroblast cluster, split by disease activity status, coloured by scaled average expression, and sized by percentage of expressing cells. Red asterisks separate comparisons that led to genes being classified as DEGs. ( J ) Suggested mathematical model for out-of-phase oscillations in MMP2/MMP9 and TIMP3/TIMP4 expression, the subsequent anabolism potential of the tissue they induce, and its putative impact on collagen VI deposition. ( F : collagen I vs collagen VI in RA synovium P = 0.0011, G : lymphoid vs myeloid counts for collagen I P = 0.056 and for collagen VI P = 0.1056). Exact P values are given unless they are below 0.0001 which is beyond the calculation limit of the software used. .

Article Snippet: Rabbit anti-human MMP2 , Atlas Antibodies , HPA001939.

Techniques: Quantitative Proteomics, Activity Assay, Expressing, Software

Journal: Molecular Systems Biology

Article Title: Synovial matrix turnover controls immune cell spatial patterning in inflammation resolution

doi: 10.1038/s44320-025-00149-7

Figure Lengend Snippet: ( A ) Immunofluorescent staining was used to characterise the spatial distribution of COL4A1, COL6A1, CHP, and CD14. QuPath was used to visualise immunofluorescent imaging of COL6A1 (magenta), CHP (green), CD14 (cyan), COL4A1 (red) in section JRP122 (representative of 3 OA and 3 RA sections). ( B – D ) Degraded collagen VI peptides with either increased abundance in RA (red) or OA (blue) were mapped back to 50–100 amino acid sections of the α1 ( B ), α2 ( C ), and α3 ( D ) chain structures. The frequency of cleavage sites within these sections was plotted in both bars and heatmaps. Corresponding heatmaps for these same sections were generated from Manchester proteome cleave (MPC) ( https://www.manchesterproteome.manchester.ac.uk/#/MPSC ) with a susceptibility score cut-off of 0.75 for MMP2/9 cleavage and the frequency of these were predicted cleavage sites were plotted in green. Stars indicate experimentally validated MMP9 cleavage sites. .

Article Snippet: Rabbit anti-human MMP2 , Atlas Antibodies , HPA001939.

Techniques: Staining, Imaging, Generated

Journal: Experimental and Therapeutic Medicine

Article Title: IL-32γ promotes integrin αvβ6 expression through the activation of NF-κB in HSCs

doi: 10.3892/etm.2017.4956

Figure Lengend Snippet: Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) MMP2 and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.

Article Snippet: Primary antibodies were as follows: Anti-integrin αVβ6 (cat. no. ab97588; Abcam, Cambridge, MA, USA), anti-GAPDH (cat. no. KGAA002-2; Nanjing KeyGen Biotech Co., Ltd.), anti-α-SMA (cat. no. G6669; Sigma-Aldrich; Merck KGaA), collagen type I antibody (cat. no. 600-402-103; Rockland, Limerick, PA, USA), TIMP1 (cat. no. 8946), MMP2 (cat. no. 87809), MMP9 (cat. no. 13667), NF-κB: p65 (cat. no. 8242), p50 (cat. no. 3035) (all Cell Signaling Technology, Inc., Danvers, MA, USA) and IL-32γ (cat. no. 513501; Biolegend, Inc.).

Techniques: Activation Assay, Real-time Polymerase Chain Reaction, Western Blot, Expressing, Standard Deviation, Quantitative RT-PCR

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Elucidating the Novel Mechanism of Ligustrazine in Preventing Postoperative Peritoneal Adhesion Formation

doi: 10.1155/2022/9226022

Figure Lengend Snippet: Ligustrazine inhibits hypoxia-induced PMC ECM deposition and EMT transition. (a) Western blot analysis of protein expression of ECM-associated molecules (MMP2 and TIMP-1), mesothelial-related phenotypic biomarkers (E-cadherin and cytokeratin 18), and mesenchymal-related phenotypic biomarkers (Snail and α -SMA) in hypoxia-induced PMCs treated with different concentrations of ligustrazine for 24 h. (b–g) qRT-PCR analysis of mRNA levels of ECM-associated molecules (MMP2 and TIMP-1), mesothelial-related phenotypic biomarkers (E-cadherin and cytokeratin 18), and mesenchymal-related phenotypic biomarkers (Snail and α -SMA) in hypoxia-induced PMCs treated with different concentrations of ligustrazine for 24 h. Compared with the control, ∗ P < 0.05 and ∗∗ P < 0.01. (h–k) Immunofluorescence assay of mesothelial-related phenotypic biomarkers (E-cadherin, Cytokeratin 18), and mesenchymal-related phenotypic biomarkers (Snail, α -SMA) in hypoxia-induced PMCs treated with 20 μ M ligustrazine for 24 h (200x).

Article Snippet: VEGF (sc-57496, Santa Cruz, USA), CTGF (sc-373936, Santa Cruz, USA), vascular cell adhesion molecule-1 (VCAM-1; ab134047, Abcam, USA), intercellular cell adhesion molecular-1 (ICAM-1; sc-8439, Santa Cruz, USA), cofilin (bs-2759R, Bioss, China), phospho-cofilin (p-cofilin, bs-20261R, Bioss, China), fibroblast-specific protein 1 (FSP1; bs-3759R, Bioss, China), matrix metalloproteinases 2 (MMP2; bs-4605R, Bioss, China), tissue inhibitor of metalloproteinases-1 (TIMP-1; bs-0415R, Bioss, China), E-cadherin (bs-1519R, Bioss, China), cytokeratin 18 (bs-2043R, Bioss, China), Snail (bs-1371R, Bioss, China), α -smooth muscle actin ( α -SMA; bs-10196R, Bioss, China), F-actin (FITC-conjugated phalloidin, C1033, Beyotime, China), vinculin (bs-6640R, Bioss, China), peroxisome proliferator-activated receptor γ (PPAR γ ; bs-4590R, Bioss, China), lamin B1 (sc-377000, Santa Cruz, USA), β -actin (CW0096M, CWBIO, China), and hypoxia-inducible factor 1 α (HIF-1 α ; sc-71247, Santa Cruz, USA) were used.

Techniques: Western Blot, Expressing, Quantitative RT-PCR, Immunofluorescence

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Elucidating the Novel Mechanism of Ligustrazine in Preventing Postoperative Peritoneal Adhesion Formation

doi: 10.1155/2022/9226022

Figure Lengend Snippet: Ligustrazine suppresses hypoxia-induced PMC functions by activating PPAR γ . (a, b) Western blot and qRT-PCR analysis of PPAR γ levels in hypoxia-induced PMCs treated with different concentrations of ligustrazine for 24 h. Compared with the control, ∗ P < 0.05 and ∗∗ P < 0.01. (c) Immunofluorescence analysis of PPAR γ nuclear distribution in hypoxia-induced PMCs treated with 20 μ M ligustrazine for 24 h (200x). (d) Flow cytometry analysis of PPAR γ nuclear translocation in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h. (e) Western blot analysis of protein expression of profibrotic cytokines (VEGF and CTGF) in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h. (f, g) FDA staining assay of cell viability in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h (200x). Compared with the control, ∗ P < 0.05 and ∗∗ P < 0.01. Compared with the ligustrazine group, # P < 0.05 and ## P < 0.01. (h) Western blot analysis of protein expression of migration and adhesion-associated molecules (VCAM-1 and ICAM-1) in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h. (i) Western blot analysis of cytoskeleton protein (vinculin) expression in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h. (j) Western blot analysis of protein expression of FSP1 in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h. (k) Western blot analysis of protein expression of ECM-associated molecules (MMP2 and TIMP-1), mesothelial-related phenotypic biomarkers (E-cadherin and cytokeratin 18), and mesenchymal-related phenotypic biomarkers (Snail and α -SMA) in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h.

Article Snippet: VEGF (sc-57496, Santa Cruz, USA), CTGF (sc-373936, Santa Cruz, USA), vascular cell adhesion molecule-1 (VCAM-1; ab134047, Abcam, USA), intercellular cell adhesion molecular-1 (ICAM-1; sc-8439, Santa Cruz, USA), cofilin (bs-2759R, Bioss, China), phospho-cofilin (p-cofilin, bs-20261R, Bioss, China), fibroblast-specific protein 1 (FSP1; bs-3759R, Bioss, China), matrix metalloproteinases 2 (MMP2; bs-4605R, Bioss, China), tissue inhibitor of metalloproteinases-1 (TIMP-1; bs-0415R, Bioss, China), E-cadherin (bs-1519R, Bioss, China), cytokeratin 18 (bs-2043R, Bioss, China), Snail (bs-1371R, Bioss, China), α -smooth muscle actin ( α -SMA; bs-10196R, Bioss, China), F-actin (FITC-conjugated phalloidin, C1033, Beyotime, China), vinculin (bs-6640R, Bioss, China), peroxisome proliferator-activated receptor γ (PPAR γ ; bs-4590R, Bioss, China), lamin B1 (sc-377000, Santa Cruz, USA), β -actin (CW0096M, CWBIO, China), and hypoxia-inducible factor 1 α (HIF-1 α ; sc-71247, Santa Cruz, USA) were used.

Techniques: Western Blot, Quantitative RT-PCR, Immunofluorescence, Flow Cytometry, Translocation Assay, Expressing, Staining, Migration

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Elucidating the Novel Mechanism of Ligustrazine in Preventing Postoperative Peritoneal Adhesion Formation

doi: 10.1155/2022/9226022

Figure Lengend Snippet: The suppression effect of ligustrazine is achieved by the activated PPAR γ on the transrepression of SMRT-mediated HIF-1 α . (a) Western blot analysis of protein expression of profibrotic cytokines (VEGF and CTGF) in hypoxia-induced PMCs treated with KC7F2 for 24 h. (b, c) FDA staining assay of cell viability in hypoxia-induced PMCs treated with KC7F2 for 24 h (200x). Compared with the control, ∗ P < 0.05 and ∗∗ P < 0.01. (d) Western blot analysis of protein expression of migration and adhesion-associated molecules (VCAM-1 and ICAM-1) in hypoxia-induced PMCs treated with KC7F2 for 24 h. (e) Western blot analysis of cytoskeleton protein (vinculin) expression in hypoxia-induced PMCs treated with KC7F2 for 24 h. (f) Western blot analysis of protein expression of FSP1 in hypoxia-induced PMCs treated with KC7F2 for 24 h. (g) Western blot analysis of protein expression of ECM-associated molecules (MMP2 and TIMP-1), mesothelial-related phenotypic biomarkers (E-cadherin and cytokeratin 18), and mesenchymal-related phenotypic biomarkers (Snail and α -SMA) in hypoxia-induced PMCs treated with KC7F2 for 24 h. (h, i) qRT-PCR and Western blot analysis of HIF-1 α levels in hypoxia-induced PMCs treated with 20 μ M ligustrazine and/or 1 μ M GW9662 for 24 h. Compared with the control, ∗ P < 0.05 and ∗∗ P < 0.01. Compared with the ligustrazine group, # P < 0.05 and ## P < 0.01. (j, k) qRT-PCR analysis of mRNA levels of SMRT and NCoR in hypoxia-induced HPMCs after different transfection for 24 h. Compared with the control, ∗ P < 0.05 and ∗∗ P < 0.01. (l) qRT-PCR analysis of mRNA levels of HIF-1 α in hypoxia-induced HPMCs treated with 20 μ M ligustrazine and/or with different transfection for 24 h. Compared with the control, ∗ P < 0.05 and ∗∗ P < 0.01. Compared with the ligustrazine group, # P < 0.05 and ## P < 0.01. (m) Western blot analysis of protein expression of HIF-1 α in hypoxia-induced HPMCs treated with 20 μ M ligustrazine and/or with different transfection for 24 h.

Article Snippet: VEGF (sc-57496, Santa Cruz, USA), CTGF (sc-373936, Santa Cruz, USA), vascular cell adhesion molecule-1 (VCAM-1; ab134047, Abcam, USA), intercellular cell adhesion molecular-1 (ICAM-1; sc-8439, Santa Cruz, USA), cofilin (bs-2759R, Bioss, China), phospho-cofilin (p-cofilin, bs-20261R, Bioss, China), fibroblast-specific protein 1 (FSP1; bs-3759R, Bioss, China), matrix metalloproteinases 2 (MMP2; bs-4605R, Bioss, China), tissue inhibitor of metalloproteinases-1 (TIMP-1; bs-0415R, Bioss, China), E-cadherin (bs-1519R, Bioss, China), cytokeratin 18 (bs-2043R, Bioss, China), Snail (bs-1371R, Bioss, China), α -smooth muscle actin ( α -SMA; bs-10196R, Bioss, China), F-actin (FITC-conjugated phalloidin, C1033, Beyotime, China), vinculin (bs-6640R, Bioss, China), peroxisome proliferator-activated receptor γ (PPAR γ ; bs-4590R, Bioss, China), lamin B1 (sc-377000, Santa Cruz, USA), β -actin (CW0096M, CWBIO, China), and hypoxia-inducible factor 1 α (HIF-1 α ; sc-71247, Santa Cruz, USA) were used.

Techniques: Western Blot, Expressing, Staining, Migration, Quantitative RT-PCR, Transfection

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Elucidating the Novel Mechanism of Ligustrazine in Preventing Postoperative Peritoneal Adhesion Formation

doi: 10.1155/2022/9226022

Figure Lengend Snippet: LN attenuates peritoneal adhesion in PPA rats by inhibiting PMC functions. (a) Scanning electron microscope image of LN (×200 nm). (b, c) Adhesion scores and frequency of different groups. Compared with the sham group, ∗ P < 0.05 and ∗∗ P < 0.01. Compared with the model group, # P < 0.05 and ## P < 0.01. (d) Representative images of adhesion formation, HE, and Masson staining of cecum sections in different groups (100x). (e) Western blot analysis of protein expression of profibrotic cytokines (VEGF and CTGF), migration and adhesion-associated molecules (VCAM-1 and ICAM-1), and ECM-associated molecules (MMP2 and TIMP-1) in different groups. (f–k) qRT-PCR analysis of mRNA levels of profibrotic cytokines (VEGF and CTGF), migration and adhesion-associated molecules (VCAM-1 and ICAM-1), and ECM-associated molecules (MMP2 and TIMP-1) in different groups. Compared with the sham group, ∗ P < 0.05 and ∗∗ P < 0.01. Compared with the model group, # P < 0.05 and ## P < 0.01. (l) Immunohistochemistry analysis of profibrotic cytokine (CTGF), migration and adhesion-associated molecule (VCAM-1), and ECM-associated molecule (MMP2) in different groups (100x). (m) Immunofluorescence analysis of PPAR γ and HIF-1 α in different groups (100x).

Article Snippet: VEGF (sc-57496, Santa Cruz, USA), CTGF (sc-373936, Santa Cruz, USA), vascular cell adhesion molecule-1 (VCAM-1; ab134047, Abcam, USA), intercellular cell adhesion molecular-1 (ICAM-1; sc-8439, Santa Cruz, USA), cofilin (bs-2759R, Bioss, China), phospho-cofilin (p-cofilin, bs-20261R, Bioss, China), fibroblast-specific protein 1 (FSP1; bs-3759R, Bioss, China), matrix metalloproteinases 2 (MMP2; bs-4605R, Bioss, China), tissue inhibitor of metalloproteinases-1 (TIMP-1; bs-0415R, Bioss, China), E-cadherin (bs-1519R, Bioss, China), cytokeratin 18 (bs-2043R, Bioss, China), Snail (bs-1371R, Bioss, China), α -smooth muscle actin ( α -SMA; bs-10196R, Bioss, China), F-actin (FITC-conjugated phalloidin, C1033, Beyotime, China), vinculin (bs-6640R, Bioss, China), peroxisome proliferator-activated receptor γ (PPAR γ ; bs-4590R, Bioss, China), lamin B1 (sc-377000, Santa Cruz, USA), β -actin (CW0096M, CWBIO, China), and hypoxia-inducible factor 1 α (HIF-1 α ; sc-71247, Santa Cruz, USA) were used.

Techniques: Microscopy, Staining, Western Blot, Expressing, Migration, Quantitative RT-PCR, Immunohistochemistry, Immunofluorescence