Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2023 Feb;88(2):638-649.
doi: 10.1111/1750-3841.16402. Epub 2022 Dec 28.

Involvement of MMP-9 in collagen degradation of sea bass (Lateolabrax japonicus): Cloning, expression, and characterization

Ru-Qing Yang  1 , Yu-Lei Chen  1   2 , Le-Chang Sun  1   2 , Wei Ou  1 , Hai-Yan Liu  1 , Ling-Jing Zhang  1   2 , Guang-Ming Liu  1   2 , Guanghua Zhao  3 , Min-Jie Cao  1   2
Affiliations

Involvement of MMP-9 in collagen degradation of sea bass (Lateolabrax japonicus): Cloning, expression, and characterization

Ru-Qing Yang et al. J Food Sci. 2023 Feb.

Abstract

Disintegration of intramuscular connective tissue is responsible for postmortem tenderization of fish muscles during chilled storage. Matrix metalloproteinase-9 (MMP-9) was reported to be involved in this process, whereas the mechanism has not been revealed. In the present study, purified type I and V collagens from the connective tissues of sea bass (Lateolabrax japonicus) muscles were first prepared. These two kinds of collagens comprise three polypeptide chains (α), forming a typical triple-helical domain as determined by circular dichroism. The complete coding region of MMP-9 containing an open reading frame of 2070 bp encoding 689 amino acid residues was then cloned. The recombinant MMP-9 catalytic domain (rcMMP-9) was expressed in Escherichia coli and exhibited high hydrolyzing activity toward gelatin. Besides, rcMMP-9 was effective in degrading type V collagen rather than type I collagen at 4°C. The enzymatic activity of rcMMP-9 was highly pH-dependent, and its enzymatic activity under neutral and basic conditions was higher than that under acidic conditions. Metal ion Ca2+ was necessary for the maintenance of rcMMP-9 activity, whereas Zn2+ inhibited its activity. Our present study indicated that MMP-9 is responsible for the disintegration of intramuscular connective tissues by cleaving type V collagen during postmortem tenderization of fish muscle. PRACTICAL APPLICATION: Elucidation the involvement of MMP-9 in collagen degradation will deliver a reference for the prevention of muscular protein decomposition during chilled storage of fish fillets.

Keywords: Lateolabrax japonicus; collagen; enzymatic activity; matrix metalloproteinase-9; softening.

PubMed Disclaimer

References

REFERENCES

    1. Amaral, R. A., Pinto, C. A., Lima, V., Tavares, J., Martins, A. P., Fidalgo, L. G., Silva, A. M., Gil, M. M., Teixeira, P., Barbosa, J., Barba, F. J., & Saraiva, J. A. (2021). Chemical-Based methodologies to extend the shelf life of fresh fish-A review. Foods, 10(10), 2300. https://doi.org/10.3390/foods10102300
    1. Appleby, T. C., Greenstein, A. E., Hung, M., Liclican, A., Velasquez, M., Villase Or, A. G., Wang, R., Wong, M. H., Liu, X., & Papalia, G. A. (2017). Biochemical characterization and structure determination of a potent, selective antibody inhibitor of human MMP9. Journal of Biological Chemistry, 292(16), 6810-6820. https://doi.org/10.1074/jbc.M116.760579
    1. Birk, D. E. (2001). Type V collagen: Heterotypic type I/V collagen interactions in the regulation of fibril assembly. Micron (Oxford, England: 1993), 32(3), 223-237.
    1. Bruggemann, D. A., & Lawson, M. A. (2005). The extracellular matrix of Gadus morhua muscle contains types III, V, VI and IV collagens in addition to type I. Journal of Fish Biology, 66(3), 810-821. https://doi.org/10.1111/j.0022-1112.2005.00650.x
    1. Chung, L. D., Dinakarpandian, D., Yoshida, N., Lauer-Fields, J. L., Fields, G. B., Visse, R., & Nagase, H. (2004). Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. EMBO Journal, 23(15), 3020-3030. https://doi.org/10.1038/sj.emboj.7600318

LinkOut - more resources