Membrane-anchored serine proteases as regulators of epithelial function
1Proteases and Tissue Remodeling Section, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD, U.S.A.
Biochemical Society Transactions
|March 21, 2020
Summary
Membrane-anchored serine proteases (MASPs) regulate epithelial cell functions. This review highlights their roles in barrier formation, ion transport, and sensory perception, crucial for epithelial tissue health and disease.
Area of Science:
- Biochemistry
- Cell Biology
- Physiology
Background:
- Extracellular protein cleavage regulates cell behavior, involving hormones, growth factors, and matrix molecules.
- Mammalian genomes encode over 500 proteolytic enzymes, including membrane-anchored serine proteases (MASPs).
- MASPs are expressed on epithelial cells, mediating signal transduction and regulating epithelial development and function.
Purpose of the Study:
- To summarize the in vivo roles of MASPs in epithelial tissues.
- To highlight MASPs' involvement in key epithelial functions.
- To underscore the significance of MASPs in epithelial health and disease.
Main Methods:
- Minireview synthesizing current knowledge on MASPs.
- Focus on in vivo studies of MASP functions.
- Analysis of MASPs' roles in epithelial barrier, ion transport, and sensory perception.
Main Results:
- MASPs are crucial for regulating epithelial cell behavior through extracellular protein cleavage.
- MASPs play significant roles in maintaining epithelial barrier integrity.
- MASPs are involved in ion transport and sensory perception within epithelial tissues.
Conclusions:
- MASPs are vital regulators of epithelial tissue development, function, and disease.
- Understanding MASP functions is key to addressing epithelial-related pathologies.
- Further research into MASPs will illuminate their therapeutic potential.
Related Concept Videos
01:23Role of Matrix Metalloproteases in Degradation of ECM
3.1K
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...
3.1K
01:24Caspases
13.5K
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...
13.5K
01:13The Proteasome
1.5K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.5K
02:18The Proteasome
9.9K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
9.9K
01:17Role of ER in the Secretory Pathway
6.7K
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
6.7K
02:58Regulated Protein Degradation
8.6K
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
8.6K