Related Experiment Video
Updated: Jul 13, 2026
07:32
Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
Published on: March 30, 2022
Control of matrix metalloproteinase catalytic activity
Hyun-Jeong Ra1, William C Parks
1Center for Lung Biology, University of Washington, Seattle, WA 98109, USA.
Summary
Matrix metalloproteinases (MMPs) are proteases with diverse roles in health and disease. This review explores known and potential mechanisms for activating proMMPs, crucial for regulating their function.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Matrix metalloproteinases (MMPs) are proteases initially known for degrading extracellular matrix proteins.
- MMPs also activate effector proteins and shed cell-surface proteins, impacting homeostasis and immunity.
- Dysregulated MMP activity contributes to diseases like cancer, fibrosis, and inflammation.
Purpose of the Study:
- To review the diverse functions of MMPs beyond matrix degradation.
- To discuss the critical step of proMMP activation in regulating MMP proteolysis.
- To explore established and potential mechanisms of proMMP activation.
Main Methods:
- Literature review of studies on MMP function and activation.
- Analysis of known proMMP activation pathways.
- Identification of potential proMMP activation mechanisms.
Main Results:
- MMPs exhibit broad substrate specificity, acting on various extracellular proteins.
- MMPs are involved in essential physiological processes like wound healing and immunity.
- MMPs play significant roles in pathological conditions including tumor progression and chronic inflammation.
- ProMMP activation is a key regulatory step, yet mechanisms remain largely unknown for most MMPs.
Conclusions:
- MMPs are crucial regulators of both physiological and pathological processes.
- Understanding proMMP activation is vital for therapeutic interventions.
- Further research is needed to elucidate the diverse mechanisms of proMMP activation.
Related Concept Videos
01:23Role of Matrix Metalloproteases in Degradation of ECM
Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
A...
01:20The JAK-STAT Signaling Pathway
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
01:19Allosteric Proteins-ATCase
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
01:24Caspases
Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
01:19Translocation of Proteins into the Mitochondria
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
01:22Amplifying Signals via Enzymatic Cascade
When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...