» Articles » PMID: 23443633

Zymography Methods for Visualizing Hydrolytic Enzymes

Overview
Journal Nat Methods
Date 2013 Feb 28
PMID 23443633
Citations 113
Authors
Affiliations
Soon will be listed here.
Abstract

Zymography is a technique for studying hydrolytic enzymes on the basis of substrate degradation. It is a powerful, but often misinterpreted, tool yielding information on potential hydrolytic activities, enzyme forms and the locations of active enzymes. In this Review, zymography techniques are compared in terms of advantages, limitations and interpretations. With in gel zymography, enzyme forms are visualized according to their molecular weights. Proteolytic activities are localized in tissue sections with in situ zymography. In vivo zymography can pinpoint proteolytic activity to sites in an intact organism. Future development of novel substrate probes and improvement in detection and imaging methods will increase the applicability of zymography for (reverse) degradomics studies.

Citing Articles

The Influence of Bariatric Surgery on Matrix Metalloproteinase Plasma Levels in Patients with Type 2 Diabetes Mellitus.

Gentile J, Migliore R, Waisberg J, Junior M Biomolecules. 2025; 14(12.

PMID: 39766340 PMC: 11727344. DOI: 10.3390/biom14121633.


A simple and efficient "cell in situ collagen zymography" technique to evaluate cellular collagenase activities in thyroid cancer cell lines.

Savas E, Surer S, Sipahi M, Keles D, Oktay G Mol Biol Rep. 2024; 52(1):49.

PMID: 39673649 DOI: 10.1007/s11033-024-10158-8.


Human monocyte-derived macrophages shift subcellular metalloprotease activity depending on their activation state.

Bernaerts E, Ahmadzadeh K, De Visscher A, Malengier-Devlies B, HauBler D, Mitera T iScience. 2024; 27(11):111171.

PMID: 39569367 PMC: 11576389. DOI: 10.1016/j.isci.2024.111171.


Comparative proteomic analysis provides insights into wood formation in immature xylem at different ages in × .

Liu G, Zhang G, Wu Z, Lu W, Lin Y, Wang C Front Plant Sci. 2024; 15:1431164.

PMID: 39539291 PMC: 11557400. DOI: 10.3389/fpls.2024.1431164.


Spatial Measurement and Inhibition of Calpain Activity in Traumatic Brain Injury with an Activity-Based Nanotheranostic Platform.

Madias M, Stessman L, Warlof S, Kudryashev J, Kwon E ACS Nano. 2024; 18(37):25565-25576.

PMID: 39236689 PMC: 11411711. DOI: 10.1021/acsnano.4c06052.


References
1.
Kaijzel E, van der Pluijm G, Lowik C . Whole-body optical imaging in animal models to assess cancer development and progression. Clin Cancer Res. 2007; 13(12):3490-7. DOI: 10.1158/1078-0432.CCR-07-0402. View

2.
Kaberdin V, McDowall K . Expanding the use of zymography by the chemical linkage of small, defined substrates to the gel matrix. Genome Res. 2003; 13(8):1961-5. PMC: 403789. DOI: 10.1101/gr.1277303. View

3.
Margulies I, Hoyhtya M, Evans C, Stracke M, Liotta L, Stetler-Stevenson W . Urinary type IV collagenase: elevated levels are associated with bladder transitional cell carcinoma. Cancer Epidemiol Biomarkers Prev. 1992; 1(6):467-74. View

4.
Van den Steen P, Dubois B, Nelissen I, Rudd P, Dwek R, Opdenakker G . Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9). Crit Rev Biochem Mol Biol. 2003; 37(6):375-536. DOI: 10.1080/10409230290771546. View

5.
Kwon M, Kim H, Hahm D, Song J . Synthesis activity-based zymography for detection of lipases and esterases. Biotechnol Lett. 2010; 33(4):741-6. DOI: 10.1007/s10529-010-0485-4. View