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Related Concept Videos

Complement System01:27

Complement System

The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
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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...
Caspases01:24

Caspases

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.
Clot Retraction and Fibrinolysis01:16

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
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Cell Motility through Blebbing

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Blebbing Through the Matrix
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Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments
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A new cleavage site for elastase within the complement component 3.

Rolf Claesson1, Eleni Kanasi, Anders Johansson

  • 1Department of Odontology, Umeå University, Umeå, Sweden. rolf.claesson@odont.umu.se

APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica
|September 22, 2010
PubMed
Summary

This study identifies a novel cleavage site on complement C3 by the lysosomal enzyme elastase, generating previously undescribed fragments important for innate immunity research.

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Monitoring Neutrophil Elastase and Cathepsin G Activity in Human Sputum Samples

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Area of Science:

  • Biochemistry
  • Immunology
  • Proteomics

Background:

  • The complement system is crucial for innate immunity.
  • Lysosomal elastase is known to cleave complement C3.
  • Previous studies identified a specific elastase cleavage site on C3.

Purpose of the Study:

  • To investigate novel C3 cleavage fragments generated by elastase.
  • To characterize the proteolytic reaction between elastase and C3.
  • To identify new cleavage sites on the C3 molecule.

Main Methods:

  • Degradation of C3 with elastase or cathepsin G.
  • Immunoblotting using anti-C3c and anti-C3d antibodies.
  • SDS-PAGE protein separation and amino acid sequencing of fragments.

Main Results:

  • A previously undescribed elastase cleavage site was identified at alanine1350/lysine1351 on C3.
  • This cleavage produces a ~39 kDa fragment containing C3d.
  • This finding is distinct from the known cleavage site yielding a 34 kDa C3d fragment.

Conclusions:

  • Elastase generates novel C3 fragments through a distinct cleavage site.
  • These findings expand our understanding of C3 proteolysis in innate immunity.
  • The newly identified fragments may play a role in immune responses to pathogens.