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Published on: August 20, 2016
A review on animal venom-based matrix metalloproteinase modulators and their therapeutic implications
Ansumaan Sharma1, Akshad Balde1, Rasool Abdul Nazeer1
1Biopharmaceuticals Lab, Department of Biotechnology, School of Bioengineering, SRM Institute of Science and Technology, Kattankulathur 603203, Tamil Nadu, India.
Abstract:
Matrix Metalloproteinases (MMPs) belong to a family of proteolytic enzymes that degrade extracellular matrix components, such as collagen, elastin, laminin, and fibronectin. They also play a part in tissue remodeling by cleaving and rejoining the tissue proteins. Cancer, neurodegenerative disorders, cardiovascular diseases, arthritis, and chronic inflammatory conditions are just some of the diseases that can start or get worse when different MMPs are not working properly. Venomous Animals such as honeybees, toads, snakes, spiders, scorpions, jellyfish, and sea anemones contain venom-secreting glands, which help them defend against predators and immobilize their prey. The molecules that come from animal venom are a complicated mix of bioactive molecules, such as peptides, enzymes, proteins, and small organic compounds that do a number of biological things. Venom-derived molecules have been found to modulate MMP. These venoms and their components target specific signaling pathways, modifying MMP expression levels to either induce inflammation or exhibit anti-inflammatory effects. In this review, we study and explore different MMPs, such as MMP1, MMP2, MMP3, MMP7, MMP8, and MMP9, and their roles in the progression of certain diseases. We also look at different types of molecules derived from marine and land animal venom that are used as MMP modulators. We look at how they work by targeting specific signaling pathways to change MMPs and how they might be used as a medicine to stop diseases by decreasing MMPs.

