Novel specific human and mouse stromelysin-1 (MMP-3) and stromelysin-2 (MMP-10) antibodies for biochemical and immunohistochemical analyses.


Journal

Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society
ISSN: 1524-475X
Titre abrégé: Wound Repair Regen
Pays: United States
ID NLM: 9310939

Informations de publication

Date de publication:
07 2019
Historique:
received: 16 09 2018
revised: 24 01 2019
accepted: 07 02 2019
pubmed: 15 2 2019
medline: 25 2 2020
entrez: 15 2 2019
Statut: ppublish

Résumé

Matrix metalloproteinases (MMP) are a family of more than 25 zinc-dependent enzymes that are centrally involved in cellular migration, tissue remodeling, cancer invasion and metastasis. Besides degrading extracellular matrix proteins, MMPs are crucial for growth factor and cytokine release and activation. At the same time, they can inactivate inflammatory mediators and enzymes themselves through protein degradation. Subclasses of MMPs include collagenases, gelatinases, stromelysins, membrane-bound MMPs, and others. With regard to the stromelysin subfamily, three members exist, e.g., stromelysin-1 (MMP-3), stromelysin-2 (MMP-10), and stromelysin-3 (MMP-11). MMP-3, and MMP-10 share extensive similarities at the amino acid level that made it difficult to develop specific antibodies distinguishing between MMP-3 and MMP-10. Scrutinizing published data on and performing different analyses with detection of both stromelysins with commercially available or lab-made antibodies showed ambiguous results with regard to specificity of antibodies used to date. We developed new specific antibodies against the most divergent parts of the active forms of both proteins. We assessed the specificity of our novel specific anti-human and anti-mouse MMP-3 and MMP-10 antibodies in cell lysates and different human and murine skin tissues. Tests analyzing specificity of the novel antibodies included Western immunoblotting, immunofluorescence, and immunohistochemistry on paraffin sections. Analyses demonstrated specific detection of respective protein for human or mouse samples except for the anti-human MMP-3 antibody. The aim of this summary was to call attention the MMP research community to distinguish clearly between both enzymes. Our new specific anti-mouse MMP-3 and both MMP-10 antibodies allow us to address this detection problem and to enable comparative studies between both stromelysins with regard to their respective location and function in the tissue.

Identifiants

pubmed: 30761682
doi: 10.1111/wrr.12704
doi:

Substances chimiques

Antibodies 0
Matrix Metalloproteinase 3 EC 3.4.24.17
Matrix Metalloproteinase 10 EC 3.4.24.22

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

309-323

Informations de copyright

© 2019 by the Wound Healing Society.

Auteurs

Ursula Mirastschijski (U)

Wound Repair Unit, Centre for Biomolecular Interactions Bremen, Department of Biology and Biochemistry, University of Bremen, Bremen, Germany.

Nilima Dinesh (N)

Wound Repair Unit, Centre for Biomolecular Interactions Bremen, Department of Biology and Biochemistry, University of Bremen, Bremen, Germany.

Sudarson Baskaran (S)

Wound Repair Unit, Centre for Biomolecular Interactions Bremen, Department of Biology and Biochemistry, University of Bremen, Bremen, Germany.

Dirk Wedekind (D)

Hannover Medical School, Institute for Laboratory Animal Science, Hannover, Germany.

Jelena Gavrilovic (J)

School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.

Megan Y Murray (MY)

School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.

Damon Bevan (D)

School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.

Sørge Kelm (S)

Wound Repair Unit, Centre for Biomolecular Interactions Bremen, Department of Biology and Biochemistry, University of Bremen, Bremen, Germany.

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Classifications MeSH