Log in

Relevant bibliographies by topics / In situ zymography / Journal articles

Journal articles on the topic 'In situ zymography'

To see the other types of publications on this topic, follow the link: In situ zymography.

Author: Grafiati

Published: 11 March 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'In situ zymography.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Mungall, Bruce A., and Christopher C. Pollitt. "In situ zymography: topographical considerations." Journal of Biochemical and Biophysical Methods 47, no. 3 (February 2001): 169–76. http://dx.doi.org/10.1016/s0165-022x(00)00126-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Araújo, Eliane Avany Malveira, Geisy Rebouças Lima, Luciana Aleixo dos Santos de Melo, Leilane Bentes de Sousa, Marne Carvalho de Vasconcellos, Nikeila Chacon de Oliveira Conde, Carina Toda, Simone Assayag Hanan, Ary de Oliveira Alves Filho, and Maria Fulgência Costa Lima Bandeira. "Effect of a Copaiba Oil-Based Dental Biomodifier on the Inhibition of Metalloproteinase in Adhesive Restoration." Advances in Pharmacological and Pharmaceutical Sciences 2021 (February 17, 2021): 1–10. http://dx.doi.org/10.1155/2021/8840570.

Full text

Abstract:

Aim. This study sets out to evaluate the antiproteolytic activity of copaiba oil-based emulsion at the resin/dentin adhesive interface union formed with conventional and self-etching adhesives systems. Methods. At in situ zymography, 30 teeth were sectioned 2 mm below the enamel-dentin junction; a smear layer was standardized and subdivided into four groups. Gelatin conjugated with fluorescein was used and taken to the fluorescence microscope for evaluation. In cytotoxicity, the Trypan Blue method was used at four different time points. The tested groups were (G1) control with distilled water; (G2) 2% chlorhexidine (CLX); (G3) emulsion based on copaiba oil (EC) 10% + X; (G4) 10% EC + Y; and (G5) EC 10% alkaline. The zymographic assay used the same groups described, but in 30 seconds and 10 and 20 minutes. HT1080 cells were incubated and submitted to electrophoresis. The gel was analyzed using ImageJ software. Mann–Whitney and Kruskal–Wallis tests were used in the statistical analysis ( p < 0.05 ). Results. ECs showed higher cell viability in the cytotoxicity test and showed a significant difference in 10 and 20 minutes. In the zymographic assay, alkaline EC reduced 67% of MMP-2 activity and 44% of MMP-9 compared to 2% chlorhexidine. At in situ zymography in qualitative evaluation, all groups tested showed inhibition of activity in metalloproteinases. Conclusion. EC showed activity in the inhibition of metalloproteinases in vitro and in situ, especially the alkaline one. The survey shows the possibility of using ECs, a product from Amazonian biodiversity, as a biomodifier in dentistry.

APA, Harvard, Vancouver, ISO, and other styles

3

Madhu Narayan. "Zymography-types, advantages, uses and troubleshooting - A detailed review." International Journal of Research in Pharmaceutical Sciences 12, no. 3 (August 13, 2021): 2190–99. http://dx.doi.org/10.26452/ijrps.v12i3.4833.

Full text

Abstract:

There are many methods for the study and quantification of enzymes in the body systems. Off-late, the method of zymography has assumed immense importance in diagnostic medicine. It is a method where enzymes are visualized using the substrate conversion technique. The product of reaction appears, or the substrate disappears and the mechanisms specific for the recognition of this measure the biochemical reaction. This procedure has many advantages, the most important ones being providing both qualitative and measurable data, such as molecular zymography methods for visualising hydrolytic enzymes and differentiating among whole molecules, degradation and complexes. There are three main types of zymography, namely- In-Gel zymography (IGZ), In-Situ zymography (ISZ) and In-vivo zymography (IVZ). There are many variations of this technique like transfer 2D and reverse zymography. This method is mainly used to study the expression of matrix metalloproteinases. Alternate to the conventional zymography techniques have been suggested, like usage of the new Ponceau S staining protocol that provides significant benefits in terms of assay usability and cost reduction and is comparatively faster and easier. Mild alterations in the actual procedure of zymography can take care of minor issues arising during the procedure.

APA, Harvard, Vancouver, ISO, and other styles

4

Mayer-Santos, Eric, Tatjana Maravic, Allegra Comba, Patricia Moreira Freitas, Giovanna Bueno Marinho, Claudia Mazzitelli, Edoardo Mancuso, et al. "The Influence of Different Bleaching Protocols on Dentinal Enzymatic Activity: An In Vitro Study." Molecules 27, no. 5 (March 4, 2022): 1684. http://dx.doi.org/10.3390/molecules27051684.

Full text

Abstract:

This study aimed to investigate matrix metalloproteinase (MMP) activity in human dentin using in-situ and gelatin zymography, after at-home and in-office bleaching, related to their clinical exposure times. Dentin specimens (n = 5) were treated with 35% hydrogen peroxide (50 min per session/4 sessions), 10% carbamide peroxide (180 min/21 sessions), or no treatment. All were subjected to in-situ zymography. Dentin slices were, subsequently, obtained, covered with fluorescein-conjugated gelatin, and examined with confocal laser-scanning microscopy. The fluorescence intensity was quantified and statistically analyzed using one-way ANOVA and Bonferroni tests (α = 0.05). Furthermore, gelatin zymography was performed on protein extracts obtained from dentin powder (N = 8 teeth), treated with hydrogen peroxide or carbamide peroxide, with different exposure times (10/50 min for hydrogen peroxide; 252/1260 min for carbamide peroxide). The results of the in-situ zymography showed no statistical differences between the bleached specimens and the control group, with a medium level of gelatinolytic activity expressed in the dentin tubules. The results of gelatin zymography showed an increased expression of pro-MMP-9 in carbamide peroxide groups. The expression of pro-MMP-2 decreased in all the experimental groups. The bleaching treatments performed on the enamel of sound teeth do not influence dentinal enzymatic activity. However, when unprotected dentin tissue is bleached, matrix metalloproteinases are more expressed, particularly when carbamide peroxide is used, proportional to the exposure time.

APA, Harvard, Vancouver, ISO, and other styles

5

Maravic, Tatjana, Lorenzo Breschi, Federica Paganelli, Giulio Alessandri Bonetti, Stefano Martina, Gianni Di Giorgio, Maurizio Bossù, et al. "Endogenous Enzymatic Activity of Primary and Permanent Dentine." Materials 14, no. 14 (July 20, 2021): 4043. http://dx.doi.org/10.3390/ma14144043.

Full text

Abstract:

Matrix metalloproteinases (MMPs) play an important role in tooth development and influence caries development and hybrid layer degradation. Literature is scant on the differences in the activity of MMPs between primary and permanent dentine. Accordingly, the aim of the present study was to investigate endogenous gelatinolytic activity in primary and permanent dentine. Separate batches of dentine powder were obtained from intact human primary and permanent molars (n = 6). Each batch was divided in two subgroups: (1) mineralised; and (2) demineralised with 10% H3PO4. After protein extraction, gelatine zymography was performed. Furthermore, in situ zymography was performed on dentine sections of the same groups (n = 3). The slices were polished, covered with fluorescein-conjugated gelatine and evaluated using a confocal microscope. In situ zymography data were analysed using two-way analysis of variance and post hoc Holm–Šidák statistics (α = 0.05). Primary dentine showed poorly defined bands in the zymograms that vaguely corresponded to the pro-form and active form of MMP-2 and the pro-form of MMP-9. In permanent dentine, demineralised powder demonstrated stronger gelatinolytic activity than mineralised powder. In situ zymography identified stronger enzymatic activity in primary etched dentine (p < 0.05). Stronger enzymatic activity recorded in primary dentine may be related to the differences in morphology and composition between primary and permanent dentine.

APA, Harvard, Vancouver, ISO, and other styles

6

Guignabert, Christophe, Laurent Taysse, Jean-Henri Calvet, Emmanuelle Planus, Séraphin Delamanche, Stéphane Galiacy, and Marie-Pia d'Ortho. "Effect of doxycycline on sulfur mustard-induced respiratory lesions in guinea pigs." American Journal of Physiology-Lung Cellular and Molecular Physiology 289, no. 1 (July 2005): L67—L74. http://dx.doi.org/10.1152/ajplung.00475.2004.

Full text

Abstract:

Respiratory tract lesions induced by the chemical warfare agent sulfur mustard (SM) are characterized by epithelial damages associated with inflammatory cell infiltration. Here we evaluated the imbalance between gelatinase and tissue inhibitors of metalloproteinases (TIMPs), and we tested pretreatment with the protease inhibitor doxycycline. Guinea pigs were intoxicated intratracheally with SM and evaluated 24 h after exposure. Matrix metalloproteinase (MMP) gelatinase activity of bronchial lavage (BL) fluid from SM-exposed guinea pigs was high compared with controls, as shown by both zymography and biotinylated substrate degradation, whereas TIMP-1 and -2 levels by immunoblotting were similar. Extensive areas of lysis were evidenced by in situ zymography, indicating imbalance between gelatinases and inhibitors towards net proteolytic activity. Doxycycline pretreatment resulted in 1) decreased gelatinase activity (zymography, free gelatinase activity assay, and in situ zymography); 2) decreased inflammation (BL fluid cellularity and protein level); and 3) dramatic decrease in histological epithelial lesions. Our results suggest inadequate levels of TIMP to counteract increased gelatinase activity and further support a role for MMP gelatinases in SM-induced respiratory lesions. They also suggest that doxycycline may hold promise as a therapeutic tool.

APA, Harvard, Vancouver, ISO, and other styles

7

Porto, Isabel M., Lenaldo B. Rocha, Marcos A. Rossi, and Raquel F. Gerlach. "In Situ Zymography and Immunolabeling in Fixed and Decalcified Craniofacial Tissues." Journal of Histochemistry & Cytochemistry 57, no. 7 (February 2, 2009): 615–22. http://dx.doi.org/10.1369/jhc.2009.952127.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Chen, Qian, Li Shen, Qi-Lin He, Yan-Yan Tao, and Cheng-Hai Liu. "Detection for gelatinase activity of liver using flourescent in situ zymography." World Chinese Journal of Digestology 16, no. 15 (2008): 1607. http://dx.doi.org/10.11569/wcjd.v16.i15.1607.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Mazzoni, A., F. D. Nascimento, M. Carrilho, I. Tersariol, V. Papa, L. Tjäderhane, R. Di Lenarda, F. R. Tay, D. H. Pashley, and L. Breschi. "MMP Activity in the Hybrid Layer Detected with in situ Zymography." Journal of Dental Research 91, no. 5 (February 21, 2012): 467–72. http://dx.doi.org/10.1177/0022034512439210.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Alcalá-Canto, Yazmín, Froylán Ibarra-Velarde, Jesús Gracia-Mora, and Héctor Sumano-López. "Fasciola hepatica proteolytic activity in liver revealed by in situ zymography." Parasitology Research 96, no. 5 (May 26, 2005): 308–11. http://dx.doi.org/10.1007/s00436-005-1367-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Nardiello, Tricia Lynn, Josephine Ruth Giles, and Sharon A. Stranford. "Differential Protease Activity in the Secondary Lymphoid Tissues of Disease Resistant and Susceptible Mouse Strains in the MAIDS Model (45.12)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S59. http://dx.doi.org/10.4049/jimmunol.178.supp.45.12.

Full text

Abstract:

Abstract Murine leukemia virus (MuLV) is used as a mouse model system to study human AIDS. There are two strains of mice used in this model, BALB/c and C57 BL/6. Although both strains of mice will become infected, BALB/c strain recover while the BL/6 strain becomes immunocompromised (MAIDS). Previous DNA microarray work comparing the two strains has shown that certain proteases are up regulated in the BALB/c lymph nodes and spleen shortly after infection. Lymphatic remolding and cell activation are possible consequences of protease activity, and therefore the up regulation of these proteases in the BALB/c strain may be important for recovery. Using immunofluoresent microscopy and in situ zymography, quantification of protease activity in the lymph nodes of each strain was studied in the first days after MuLV infection. Serial sections were stained for lymphatic (LYVE-1) and vascular (CD31) endothelial structures using primary and fluorescently-conjugated secondary antibodies. This was combined with protease-mediated activation of quenched substrate fluorphores (in situ zymography) allowing co-localization of protease activity and lymphatic morphology. Preliminary in situ zymography results show that there is an increase in protease activity in BALB/c mice when compared to BL/6 in the lymph nodes. Furthermore, preliminary immunofluorescent results show an increase in the vascular and lymphatic branching within the BALB/c lymph nodes following MuLV infection.

APA, Harvard, Vancouver, ISO, and other styles

12

Gawlak, M., T. Górkiewicz, A. Gorlewicz, F. A. Konopacki, L. Kaczmarek, and G. M. Wilczynski. "High resolution in situ zymography reveals matrix metalloproteinase activity at glutamatergic synapses." Neuroscience 158, no. 1 (January 2009): 167–76. http://dx.doi.org/10.1016/j.neuroscience.2008.05.045.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Yi, Chin-Feng, Anna Gosiewska, Diann Burtis, and Jeffrey Geesin. "Incorporation of Fluorescent Enzyme Substrates in Agarose Gel for in Situ Zymography." Analytical Biochemistry 291, no. 1 (April 2001): 27–33. http://dx.doi.org/10.1006/abio.2001.5017.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Takano, Shingo, Koji Tsuboi, Akira Matsumura, Hiroshige Sato, and Tadao Nose. "Localization of gelatinase activities in glioma tissues by film in situ zymography." Brain Tumor Pathology 18, no. 2 (September 2001): 145–50. http://dx.doi.org/10.1007/bf02479428.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Mungall, B. A., Rita Collins, and Christopher C. Pollitt. "Localisation of gelatinase activity in epidermal hoof lamellae by in situ zymography." Histochemistry and Cell Biology 110, no. 5 (October 9, 1998): 535–40. http://dx.doi.org/10.1007/s004180050315.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Pestereva, N. S., A. Z. Marshak, and M. N. Karpenko. "CALPAIN ACTIVITY UNDER EXPERIMENTAL INCREASING OF DOPAMINE LEVEL." Medical academic journal 19, no. 1S (December 15, 2019): 221–22. http://dx.doi.org/10.17816/maj191s1221-222.

Full text

Abstract:

The aim of our study was to identify the activity of calpains under conditions of an experimental increase in the level of dopamine. The work was performed at three levels: in vivo, in situ, in vitro. An in situ study was carried on a model of isolated nerve endings - synaptosomes. Using casein zymography in solution with FITC-casein, it was shown that incubation of synaptosomes dopamine leads to calpains secretion into the synaptosomal medium. The dopamine ability to directly activate calpain was demonstrated by casein zymography in a gel. Incubation in an activation buffer containing dopamine instead of the classical activator, calcium chloride, led to the activation of calpain-2. An in vivo experiment was performed on Wistar rats. The experimental group was orally administered the drug L-dopa (100 mg/kg), the control group - saline was injected in the same way.

APA, Harvard, Vancouver, ISO, and other styles

17

Frederiks, Wilma M., and Olaf R. F. Mook. "Metabolic Mapping of Proteinase Activity with Emphasis on In Situ Zymography of Gelatinases." Journal of Histochemistry & Cytochemistry 52, no. 6 (June 2004): 711–22. http://dx.doi.org/10.1369/jhc.4r6251.2004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Nemori, Ryoichi, Masayoshi Yamamoto, Fumio Kataoka, Gakuji Hashimoto, Hiroshi Arakatsu, Takayuki Shiomi, and Yasunori Okada. "Development of In Situ Zymography to Localize Active Matrix Metalloproteinase-7 (Matrilysin-1)." Journal of Histochemistry & Cytochemistry 53, no. 10 (June 27, 2005): 1227–34. http://dx.doi.org/10.1369/jhc.5a6631.2005.

Full text

Abstract:

Matrix metalloproteinase-7 (MMP-7) is upregulated during carcinogenesis and its expression correlates with metastasis of human endometrial and gastrointestinal carcinomas. In the present study, we have developed a new method to localize the activity of MMP-7 within tissues. Polyethylene terephthalate films were uniformly coated with crosslinked carboxymethylated transferrin (CCm-Tf) as a substrate and incubated with frozen tissue sections mounted on the films. CCm-Tf on the films was degraded selectively by MMP-7, but showed little or no susceptibility to MMP-1, -2, -3, -9, or -13; MT1-MMP; MT3-MMP; or ADAMTS4. Although some serine proteinases such as elastase also digested CCm-Tf, CCm-Tf films impregnated with serine proteinase inhibitors prevented the digestion. When frozen sections of human endometrial carcinoma and lung carcinoma tissues were incubated on CCm-Tf films or those treated with proteinase inhibitors, the activity was detected in the carcinoma cell nests, where MMP-7 was immunolocalized. The present in situ zymography using CCm-Tf may be a useful method to analyze the functions of MMP-7 in pathophysiological conditions.

APA, Harvard, Vancouver, ISO, and other styles

19

MURAMATSU, Michiko, Shinji TAKAI, and Mizuo MIYAZAKI. "Detections of matrix metalloproteinases activities and localization by Film in situ zymography (FIZ)." Folia Pharmacologica Japonica 121, no. 2 (2003): 113–18. http://dx.doi.org/10.1254/fpj.121.113.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Duan, Chengjiao, Linchuan Fang, Congli Yang, Weibin Chen, Yongxing Cui, and Shiqing Li. "Reveal the response of enzyme activities to heavy metals through in situ zymography." Ecotoxicology and Environmental Safety 156 (July 2018): 106–15. http://dx.doi.org/10.1016/j.ecoenv.2018.03.015.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Mook, Olaf R. F., Claudia Van Overbeek, Eleonora G. Ackema, Febe Van Maldegem, and Wilma M. Frederiks. "In Situ Localization of Gelatinolytic Activity in the Extracellular Matrix of Metastases of Colon Cancer in Rat Liver Using Quenched Fluorogenic DQ-gelatin." Journal of Histochemistry & Cytochemistry 51, no. 6 (June 2003): 821–29. http://dx.doi.org/10.1177/002215540305100613.

Full text

Abstract:

Matrix metalloproteinases (MMPs) such as gelatinases are believed to play an important role in invasion and metastasis of cancer. In this study we investigated the possible role of MMP-2 and MMP-9 in an experimental model of colon cancer metastasis in rat liver. We demonstrated with gelatin zymography that the tumors contained MMP-2 and MMP-9, but only MMP-2 was present in the active form. Immunolocalization of MMP-2 showed that the protein was localized at basement membranes of colon cancer cells and in intratumor stroma, associated with extracellular matrix (ECM) components. However, zymography and immunohistochemistry (IHC) do not provide information on the localization of MMP activity. Therefore, we developed an in situ zymography technique using the quenched fluorogenic substrate DQ-gelatin in unfixed cryostat sections. The application of DQ-gelatin in combination with a gelled medium allows precise localization of gelatinolytic activity. Fluorescence due to gelatinolytic activity was found in the ECM of tumors and was localized similarly to both MMP-2 protein and collagen type IV, its natural substrate. The localization of MMP-2 activity and collagen type IV at similar sites suggests a role of MMP-2 in remodeling of ECM of stroma in colon cancer metastases in rat liver.

APA, Harvard, Vancouver, ISO, and other styles

22

Maravic, T., E. Mancuso, A. Comba, V. Checchi, L. Generali, C. Mazzitelli, U. Josic, et al. "Dentin Cross-linking Effect of Carbodiimide After 5 Years." Journal of Dental Research 100, no. 10 (May 19, 2021): 1090–98. http://dx.doi.org/10.1177/00220345211014799.

Full text

Abstract:

Carbodiimide (EDC)–based dentin primers preserve hybrid layer (HL) integrity. However, aging >1 y has not been investigated. The present study examined whether the cross-linking effect of EDC was reflected in dentin bond strength, endogenous enzymatic activity, and the chemical profile of the HL after 5-y aging in artificial saliva. Noncarious human third molars ( N = 42) were cut to expose middle/deep coronal dentin and treated as follows: group 1, dentin etched with 35% H3PO4, pretreated with a 0.3M aqueous EDC primer for 1 min and restored with XP Bond (Dentsply Sirona); group 2, as in group 1 but without EDC pretreatment; group 3, Clearfil SE Bond (Kuraray-Noritake) primer applied to dentin surface, followed by EDC pretreatment as in group 1 and application of bond; group 4, as in group 3 without EDC pretreatment. After composite buildup, the specimens were cut into sticks or slabs, depending on the experiment. All tests were performed at baseline (T0) and after 5 y of aging (T5) in artificial saliva at 37 °C. Microtensile bond strength (µTBS) was tested at a crosshead speed of 1 mm/min until failure. Endogenous enzymatic activity was investigated with in situ zymography. The chemical profile of HL was determined via Raman spectroscopy. Three-way analysis of variance and post hoc Tukey test were used to analyze µTBS and in situ zymography data (α = 0.05). EDC pretreatment and aging significantly influenced µTBS and in situ zymography results ( P < 0.05). Higher bond strength and lower gelatinolytic activity were identified in the EDC-treated groups at T5 ( P < 0.05), especially in the etch-and-rinse groups. Raman spectra revealed less defined amide III peaks in control specimens at T5. The EDC cross-linking effect persisted in the HL for 5 y in terms of bond strength, collagen structure preservation, and dentinal enzyme silencing.

APA, Harvard, Vancouver, ISO, and other styles

23

Jalalah, S. M. "Glomerular changes in microscopic haematuria, studied by quantitative immunoelectron microscopy and in situ zymography." Nephrology Dialysis Transplantation 17, no. 9 (September 1, 2002): 1586–93. http://dx.doi.org/10.1093/ndt/17.9.1586.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Furuya, Mitsuko, Hiroshi Ishikura, Ryoichi Nemori, Masahiko Shibata, Seiichiro Fujimoto, and Takashi Yoshiki. "Clarification of the active gelatinolytic sites in human ovarian neoplasms using in situ zymography." Human Pathology 32, no. 2 (February 2001): 163–68. http://dx.doi.org/10.1053/hupa.2001.21558.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Baruwa, Abayomi Omokeji, Claudia Mazzitelli, Tatjana Maravic, Jorge N. R. Martins, Annalisa Mazzoni, and António Ginjeira. "In Situ Zymography Analysis of Matrix Metalloproteinases Activity Following Endodontic Irrigation Protocols and Correlation to Root Dentine Bond Strength." Polymers 14, no. 17 (August 30, 2022): 3567. http://dx.doi.org/10.3390/polym14173567.

Full text

Abstract:

The objective was to evaluate the effect of different root canal irrigating solutions on the activity of matrix metalloproteinases (MMPs), and correlation to the push-out bond strength (PBS) and nanoleakage expression (NL) in the root dentin. Seventy-two single-rooted teeth were treated endodontically and distributed into four groups (n = 6 for in-situ zymography, n = 10 for PBS, and n = 2 for NL per group) according to the irrigating solutions used: (I) saline (S); (II) 5.25% sodium hypochlorite (SH); (III) 5.25% SH + 10% citric acid (CA); and (IV) 5.25% SH + 10% CA + 0.2% chlorhexidine (CHX). After root canal obturation, post space was prepared to receive the glass fiber post. Dual-cure resin was used for luting and light polymerization was performed. The root/fiber post assemblies were sectioned and subjected to in situ zymography, and PBS and NL expression analysis tests. The enzymatic activity was quantified and expressed as a percentage of the green fluorescence, while fractographic evaluation was performed after PBS with a stereomicroscope, and data were statistically analyzed at p < 0.05. The zymography analysis shows high expression of MMPs in the middle third of the root in all groups, while the most abundant activity of MMPs following the irrigating solutions is observed in groups I and III, where saline and citric acid are used, respectively. Inversely, group IV, where chlorhexidine is the final rinse, records the lowest MMP activity with the highest PBS, and the statistical analysis of the groups are ranked as: IV > II > III > I (p < 0.05). The combination of SH, CA, and CHX results in lower expression of MMPs and higher push-out bond strength of fiber posts to root dentin, with no difference seen in the nanoleakage expression (p > 0.05); hence, this irrigation regime with chlorhexidine as a final rinse is more favorable than other combinations in ensuring optimal adhesion to root dentine.

APA, Harvard, Vancouver, ISO, and other styles

26

Maravić, Tatjana, Eugenia Baena, Claudia Mazzitelli, Uroš Josić, Edoardo Mancuso, Vittorio Checchi, Luigi Generali, Laura Ceballos, Lorenzo Breschi, and Annalisa Mazzoni. "Endogenous Enzymatic Activity in Dentin Treated with a Chitosan Primer." International Journal of Molecular Sciences 22, no. 16 (August 17, 2021): 8852. http://dx.doi.org/10.3390/ijms22168852.

Full text

Abstract:

The aim of this study was to evaluate the effect of different concentrations of chitosan polymer on dentinal enzymatic activity by means of gelatin and in situ zymography. Human dentin was frozen and ground in a miller. Dentin powder aliquots were demineralized with phosphoric acid and treated with three different concentrations of lyophilized chitosan polymer (1, 0.5 and 0.1 wt%) dissolved in distilled water. Dentin proteins were extracted from each experimental group and electrophoresed under non-reducing conditions in 10% SDS-PAGE containing fluorescein-labeled gelatin. After 48 h in the incubation buffer at 37 °C, proteolytic activity was registered under long-wave UV light scanner and quantified by using Image J software. Furthermore, additional teeth (n = 4) were prepared for the in situ zymographic analysis in unrestored as well as restored dentin pretreated with the same chitosan primers. The registered enzymatic activity was directly proportional to the chitosan concentration and higher in the restored dentin groups (p < 0.05), except for the 0.1% chitosan primer. Chitosan 0.1% only showed faint expression of enzymatic activity compared to 1% and 0.5% concentrations. Chitosan 0.1% dissolved in water can produce significant reduction in MMPs activity and could possibly contribute to bond strength preservation over time.

APA, Harvard, Vancouver, ISO, and other styles

27

Cao, Tingting, Xiangshi Kong, Weihua He, Yunru Chen, You Fang, Qiang Li, Qi Chen, Yunchao Luo, and Xingjun Tian. "Spatiotemporal characteristics of enzymatic hotspots in subtropical forests: In situ evidence from 2D zymography images." CATENA 216 (September 2022): 106365. http://dx.doi.org/10.1016/j.catena.2022.106365.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Yan, S. J., and E. A. G. Blomme. "In Situ Zymography: A Molecular Pathology Technique to Localize Endogenous Protease Activity in Tissue Sections." Veterinary Pathology 40, no. 3 (May 2003): 227–36. http://dx.doi.org/10.1354/vp.40-3-227.

Full text

Abstract:

Proteases play important roles in modulating a wide range of cellular functions, in the regulation of biologic processes, and in the pathogenesis of various diseases. Several molecular techniques are available to identify and characterize proteases in cells and tissues. Most of these techniques do not provide information on the activity of proteases in tissues. In situ zymography (ISZ) is a relatively lowcost technique that uses specific protease substrates to detect and localize specific protease activities in tissue sections. Used in combination with other techniques, ISZ provides data that further our understanding of the role of specific proteases in various pathologic and physiologic conditions. This review describes the general principle of ISZ and highlights the past and future applications of this technique in molecular pathology.

APA, Harvard, Vancouver, ISO, and other styles

29

van Smeden, Jeroen, Irini M. Dijkhoff, Richard W. J. Helder, Hanin Al-Khakany, Daphne E. C. Boer, Anne Schreuder, Wouter W. Kallemeijn, et al. "In situ visualization of glucocerebrosidase in human skin tissue: zymography versus activity-based probe labeling." Journal of Lipid Research 58, no. 12 (October 12, 2017): 2299–309. http://dx.doi.org/10.1194/jlr.m079376.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Krejci-Papa, N. C., and R. Paus. "A novel in-situ-zymography technique localizes gelatinolytic activity in human skin to mast cells." Experimental Dermatology 7, no. 6 (December 1998): 321–26. http://dx.doi.org/10.1111/j.1600-0625.1998.tb00331.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Spohn, Marie, Andrea Carminati, and Yakov Kuzyakov. "Soil zymography – A novel in situ method for mapping distribution of enzyme activity in soil." Soil Biology and Biochemistry 58 (March 2013): 275–80. http://dx.doi.org/10.1016/j.soilbio.2012.12.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

32

Sakuraba, Ichiro, Junko Hatakeyama, Yuji Hatakeyama, Ichiro Takahashi, Hideaki Mayanagi, and Yasuyuki Sasano. "The MMP activity in developing rat molar roots and incisors demonstrated by in situ zymography." Journal of Molecular Histology 37, no. 1-2 (July 8, 2006): 87–93. http://dx.doi.org/10.1007/s10735-006-9037-6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Iwata, Hiroji, Masayoshi Yamamoto, Ryoichi Nemori, Mitsuhiro Mizutani, Takuji Iwase, Shigeto Miura, Yuicni Obata, et al. "Localization of gelatinolytic activity can be detected in Breast Cancer tissues by filmin situ zymography." Breast Cancer 8, no. 2 (April 2001): 111–15. http://dx.doi.org/10.1007/bf02967489.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Hadler-Olsen, E., J. O. Winberg, F. P. Reinholt, T. Larsen, L. Uhlin-Hansen, T. Jenssen, E. Berg, and S. O. Kolset. "Proteases in Plasma and Kidney of db/db Mice as Markers of Diabetes-Induced Nephropathy." ISRN Endocrinology 2011 (August 4, 2011): 1–10. http://dx.doi.org/10.5402/2011/832642.

Full text

Abstract:

Db/db mice are overweight, dyslipidemic and develop diabetic complications, relevant for similar complications in human type 2 diabetes. We have used db/db and db/+ control mice to investigate alterations in proteinase expression and activity in circulation and kidneys by SDS-PAGE zymography, electron microscopy, immunohistochemistry, Western blotting, and in situ zymography. Plasma from db/db mice contained larger amounts of serine proteinases compared to db/+ mice. Kidneys from the db/db mice had a significantly larger glomerular surface area and somewhat thicker glomerular basement membranes compared to the db/+ mice. Furthermore, kidney extracts from db/+ mice contained metalloproteinases with Mr of approximately 92000, compatible with MMP-9, not observed in db/db mice. These results indicate that higher levels of serine proteinases in plasma may serve as potential markers for kidney changes in db/db mice, whereas a decrease in MMP-9 in the kidney may be related to the glomerular changes.

APA, Harvard, Vancouver, ISO, and other styles

35

Mutch, N. J., L. A. Robbie, and N. A. Booth. "Human Thrombi Contain an Abundance of Active Thrombin." Thrombosis and Haemostasis 86, no. 10 (2001): 1028–34. http://dx.doi.org/10.1055/s-0037-1616529.

Full text

Abstract:

SummaryThis study assessed the abundance and activity of thrombin in human thrombi, removed at autopsy or during surgery. Arterial and venous thrombus sections showed thrombin activity by in situ zymography, based on conversion of fibrinogen to fibrin. Hirudin or antibodies to thrombin abolished the activity. Thrombin activity in extracts of 40 thrombi was quantified by cleavage of fibrinogen or small peptide substrates; the results correlated well (r = 0.87, p<0.0001) with a median activity of about 4.5 IU/g of thrombus (wet weight). Activity correlated poorly with total prothrombin (median 27 μg/g) and was inversely related to antithrombin, but not to PAI-1. Zymography showed two major active bands, thrombin at 37 kDa, and a 50 kDa form that probably corresponds to meizothrombin desF1. The abundant local thrombin demonstrated here has implications for thrombus lysis and extension; incomplete lysis and exposure of active thrombin may lead to re-occlusion of vessels.

APA, Harvard, Vancouver, ISO, and other styles

36

Hadler-Olsen, Elin, Premasany Kanapathippillai, Eli Berg, Gunbjørg Svineng, Jan-Olof Winberg, and Lars Uhlin-Hansen. "Gelatin In Situ Zymography on Fixed, Paraffin-embedded Tissue: Zinc and Ethanol Fixation Preserve Enzyme Activity." Journal of Histochemistry & Cytochemistry 58, no. 1 (September 15, 2009): 29–39. http://dx.doi.org/10.1369/jhc.2009.954354.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Kaji, M. "Gelatinolytic activity of matrix metalloproteinase in lung cancer studied using film in situ zymography stamp method." Lung Cancer 39, no. 2 (February 2003): 125–30. http://dx.doi.org/10.1016/s0169-5002(02)00453-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Faia, Kerrie L., Wendell P. Davis, Adele J. Marone, and Thomas L. Foxall. "Matrix metalloproteinases and tissue inhibitors of metalloproteinases in hamster aortic atherosclerosis: correlation with in-situ zymography." Atherosclerosis 160, no. 2 (February 2002): 325–37. http://dx.doi.org/10.1016/s0021-9150(01)00590-1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Chhabra, Aastha, Astha Jaiswal, Umang Malhotra, Shrey Kohli, and Vibha Rani. "Cell in situ zymography: an in vitro cytotechnology for localization of enzyme activity in cell culture." In Vitro Cellular & Developmental Biology - Animal 48, no. 8 (July 21, 2012): 463–68. http://dx.doi.org/10.1007/s11626-012-9529-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Chesler, Naomi C., David N. Ku, and Zorina S. Galis. "Transmural pressure induces matrix-degrading activity in porcine arteries ex vivo." American Journal of Physiology-Heart and Circulatory Physiology 277, no. 5 (November 1, 1999): H2002—H2009. http://dx.doi.org/10.1152/ajpheart.1999.277.5.h2002.

Full text

Abstract:

Extracellular matrix components must be degraded and resynthesized for vascular remodeling to occur. We hypothesized that the hemodynamic environment regulates activity of matrix metalloproteinases (MMPs), the primary agents for in vivo matrix degradation, during vascular remodeling in response to changes in transmural pressure and shear stress. Pathological hemodynamic conditions were reproduced in an ex vivo system in which we maintained porcine carotid arteries for 24 and 48 h. Total levels of MMP-2 and MMP-9 extracted from tissue homogenates and analyzed by SDS-PAGE zymography were stimulated by transmural pressure and were unaffected by shear stress changes. Degradation of two specific gelatinase substrates, gelatin and elastin, increased with increasing pressure, but the degradation was not affected by shear stress changes in tissue specimens analyzed using in situ zymography (gelatin) and fluorescent measurement of endogenous elastin degradation (elastin). Our results suggest that transmural pressure activates at least two members of the MMP family and that activity of these enzymes is accompanied by degradation of matrix components, effects that may be implicated in hypertensive vascular remodeling.

APA, Harvard, Vancouver, ISO, and other styles

41

Robbie, Linda, Susan Berry, Bruce Bennett, Nicola Mutch, Elaine Moir, and Nuala Booth. "Localization and Identification of Thrombin and Plasminogen Activator Activities in Model Human Thrombi by in situ Zymography." Thrombosis and Haemostasis 88, no. 12 (2002): 996–1002. http://dx.doi.org/10.1055/s-0037-1613346.

Full text

Abstract:

SummaryHuman thrombi vary in their susceptibility to lysis and this is clinically important. Several potential contributory factors were examined in this study by using model thrombi, created under flow; these provide a robust, reproducible and easily-manipulated system. Here we identify the plasminogen activators (PA) active in model thrombi of known age and define the cellular and plasma contribution to activity in different areas. The cell-rich head of model thrombi had strong thrombin and PA activity, with coagulant activity also at the tail. Thrombin activity decreased as model thrombi were aged. PA activity in the thrombus head also decreased on ageing of thrombi but activity emerged around the thrombi, including the tail. Activity in the head of fresh model thrombi was primarily due to uPA, with some contribution from tPA. Experiments with thrombi prepared from platelet-rich plasma and added leucocytes showed that uPA activity at the head of fresh thrombi was derived from PMN. Older thrombi had tPA activity around the tail of the thrombus; this activity occurred in the absence of cells. This study highlights the importance of PMN-derived uPA activity in the lysis of fresh thrombi, with activity originating in the leucocyte-rich head. It also shows that thrombi are dynamic structures in which fibrin can be repeatedly laid down and lysed, observations that are relevant to therapeutic lysis and potential rethrombosis.

APA, Harvard, Vancouver, ISO, and other styles

42

Calis, Zorina S., Galina K. Sukhova, and Peter Libby. "Microscopic localization of active proteases by in situ zymography: detection of matrix metalloproteinase activity in vascular tissue." FASEB Journal 9, no. 10 (July 1995): 974–80. http://dx.doi.org/10.1096/fasebj.9.10.7615167.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Koyama, H., H. Iwata, Y. Kuwabara, H. Iwase, S. Kobayashi, and Y. Fujii. "Gelatinolytic activity of matrix metalloproteinase-2 and -9 in oesophageal carcinoma; a study using in situ zymography." European Journal of Cancer 36, no. 16 (October 2000): 2164–70. http://dx.doi.org/10.1016/s0959-8049(00)00297-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Liu, Dan, XingHao Yang, JiaFeng Huang, RiBang Wu, CuiLing Wu, HaiLun He, and Hao Li. "In situ Demonstration and Characteristic Analysis of the Protease Components from Marine Bacteria Using Substrate Immersing Zymography." Applied Biochemistry and Biotechnology 175, no. 1 (October 15, 2014): 489–501. http://dx.doi.org/10.1007/s12010-014-1287-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Sasaki, K., N. Tateoka, H. Ando, and F. Yoshizaki. "Effect of flavones on rat brain and lung matrix metalloproteinase activity measured by film in-situ zymography." Journal of Pharmacy and Pharmacology 57, no. 4 (April 2005): 459–65. http://dx.doi.org/10.1211/0022357055588.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

RANKIN, CAROLYN A., YOSHIFUMI ITOH, CHUNQIAO TIAN, DONNA M. ZIEMER, JAMES P. CALVET, and VINCENT H. GATTONE. "Matrix Metalloproteinase-2 in a Murine Model of Infantile-Type Polycystic Kidney Disease." Journal of the American Society of Nephrology 10, no. 2 (February 1999): 210–17. http://dx.doi.org/10.1681/asn.v102210.

Full text

Abstract:

Abstract. It was previously found that elevated levels of matrix metalloproteinase (MMP)-2 (gelatinase A) and -9 (gelatinase B) were synthesized and secreted into the medium by cultured kidney tubules derived from cystic C57BL/6J-cpk mice. To determine whether increased synthesis and secretion occur in vivo in this mouse model of polycystic kidney disease, kidney protein extracts, mRNA, and tissue sections were compared for expression and activity of MMP-2 and -9. Although both MMP were detected in tissue extracts, the differences in expression levels and activity in normal and cystic kidneys were far greater for MMP-2. High levels of MMP-2 seemed to result from increased expression by the cystic kidneys predominantly in the second and third postnatal weeks (a time when the kidneys are undergoing rapid cystic enlargement). Much of the increased MMP was present in the inactive zymogen form, although active enzyme was readily detected by sodium dodecyl sulfate-polyacrylamide gel zymography and in situ zymography. MMP-2 was abnormally localized to the interstitium and to foci between cysts, suggesting that MMP-2 may regulate collagen accumulation at those sites, thus allowing cyst enlargement and limiting the severity of interstitial fibrosis.

APA, Harvard, Vancouver, ISO, and other styles

47

Li, Wei, Kuniyoshi Tanaka, Yukio Chiba, Tetsuya Kimura, Kouichi Morioka, Takahiko Uesaka, Akio Ihaya, Masato Sasaki, Takeshi Tsuda, and Narihisa Yamada. "Role of MMPs and plasminogen activators in angiogenesis after transmyocardial laser revascularization in dogs." American Journal of Physiology-Heart and Circulatory Physiology 284, no. 1 (January 1, 2003): H23—H30. http://dx.doi.org/10.1152/ajpheart.00240.2002.

Full text

Abstract:

We examined the role of matrix metalloproteinases (MMPs), tissue inhibitors of MMP (TIMPs), and plasminogen activator (PA) in transmyocardial laser revascularization (TMLR)-induced angiogenesis. TMLR was accomplished with a carbon dioxide laser in seven dogs whose left anterior descending coronary artery (LAD) was ligated. Seven control dogs underwent only LAD ligation, and four dogs underwent a sham operation, consisting only of a left thoracotomy. Two weeks later, transmural myocardial samples were harvested from the distributions of the LAD and the left circumflex artery for substrate zymography, immunohistochemical staining, and in situ zymography. MMP-1, MMP-2, TIMP-1, TIMP-2, and urokinase-type PA levels in the distribution of the LAD were higher in the laser group than in the control or sham group. Counts of von Willebrand factor-positive microvessels and smooth muscle α-actin-positive arterioles demonstrated that the angiogenesis and ateriogenesis was promoted in the laser group and correlated directly with the number of MMP-stained microvessels. We conclude that TMLR induces the expression of MMPs, TIMPs, and urokinase-type PA and that these proteinases play an important role in angiogenesis after TMLR.

APA, Harvard, Vancouver, ISO, and other styles

48

Fukuda, Yuh, Masamichi Ishizaki, Yasunori Okada, Motoharu Seiki, and Nobuaki Yamanaka. "Matrix metalloproteinases and tissue inhibitor of metalloproteinase-2 in fetal rabbit lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 279, no. 3 (September 1, 2000): L555—L561. http://dx.doi.org/10.1152/ajplung.2000.279.3.l555.

Full text

Abstract:

Cell-extracellular matrix interaction and extracellular matrix remodeling are known to be important in fetal lung development. We investigated the localization of matrix metalloproteinases (MMPs) in fetal rabbit lungs. Immunohistochemistry for type IV collagen, MMP-1, MMP-2, MMP-9, membrane type (MT) 1 MMP, and tissue inhibitor of metalloproteinase (TIMP)-2 and in situ hybridization for MMP-9 mRNA were performed. Gelatin zymography and Western blotting for MT1-MMP in lung tissue homogenates were also studied. MMP-1 and MT1-MMP were detected in epithelial cells, and MMP-2 and TIMP-2 were detected in epithelial cells and some mesenchymal cells in each stage. MMP-9 was found in epithelial cells mainly in the late stage. Gelatin zymography revealed that the ratio of active MMP-2 to latent MMP-2 increased dramatically during the course of development. MT1-MMP was detected in tissue homogenates, especially predominant in the late stage. These findings suggest that MMPs and their inhibitors may contribute to the formation of airways and alveoli in fetal lung development and that activated MMP-2 of alveolar epithelial cells may function to provide an extremely wide alveolar surface.

APA, Harvard, Vancouver, ISO, and other styles

49

Goussev, Staci, Jung-Yu C. Hsu, Yong Lin, Tjoson Tjoa, Nino Maida, Zena Werb, and Linda J. Noble-Haeusslein. "Differential temporal expression of matrix metalloproteinases after spinal cord injury: relationship to revascularization and wound healing." Journal of Neurosurgery: Spine 99, no. 2 (September 2003): 188–97. http://dx.doi.org/10.3171/spi.2003.99.2.0188.

Full text

Abstract:

Object. Matrix metalloproteinases (MMPs), particularly MMP-9/gelatinase B, promote early inflammation and barrier disruption after spinal cord injury (SCI). Early blockade of MMPs after injury provides neuroprotection and improves motor outcome. There is recent evidence, however, that MMP-9 and MMP-2/gelatinase A participate in later wound healing in the injured cord. The authors therefore examined the activity of these gelatinases during revascularization and glial scar formation in the contused murine spinal cord. Methods. Gelatinase activity was evaluated using gelatin zymography 24 hours after a mild, moderate, or severe contusion injury. The active form of MMP-2 was not detected, whereas MMP-9 activity was evident in all SCI groups and rose with increasing injury severity. The temporal expression of gelatinases was then examined using gelatin zymography after a moderate SCI. The active form of MMP-9 was most prominent at 1 day, extended through the early period of revascularization, and returned to control by 14 days. The active form of MMP-2 appeared at 7 days postinjury and remained elevated compared with that documented in sham-treated mice for at least 21 days. Increased MMP-2 activity coincided with both revascularization and glial scar formation. Using in situ zymography, gelatinolytic activity was detected in the meninges, vascular elements, glia, and macrophage-like cells in the injured cord. Results of immunolabeling confirmed the presence of gelatinase in vessels during revascularization and in reactive astrocytes associated with glial scar formation. Conclusions. These findings suggest that although MMP-9 and -2 exhibit overlapping expression during revascularization, the former is associated with acute injury responses and the latter with formation of a glial scar.

APA, Harvard, Vancouver, ISO, and other styles

50

Schellenberger, Eyk, Akvile Haeckel, Lena Schoenzart, Franziska Appler, Joerg Schnorr, Matthias Taupitz, and Bernd Hamm. "Combined in Situ Zymography, Immunofluorescence, and Staining of Iron Oxide Particles in Paraffin-Embedded, Zinc-Fixed Tissue Sections." Molecular Imaging 11, no. 5 (September 2012): 7290.2011.00055. http://dx.doi.org/10.2310/7290.2011.00055.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!