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Caspases

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.

Apoptosis

Apoptosis

Apoptosis is a combination of two Greek words, 'apo' and 'ptosis,' meaning separation and falling off, respectively. Hippocrates used this word to describe gangrene, which was caused due to bandaging of fractured bones. Apoptosis was distinguished from necrosis in 1970 when John Kerr reported observations of morphological changes occurring during apoptosis. During one experiment, he observed that the disruption of blood supply to the liver tissue resulted in a size reduction of the tissue.

The Intrinsic Apoptotic Pathway

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...

The Extrinsic Apoptotic Pathway

The Extrinsic Apoptotic Pathway

The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...

Role of Matrix Metalloproteases in Degradation of ECM

Role 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...

Cellular Injury V: Apoptosis and Autophagy

Cellular Injury V: Apoptosis and Autophagy

Cells respond to damage and stress through highly coordinated processes that decide whether they survive or undergo controlled self-destruction. Two major pathways involved in this regulation are apoptosis, a type of programmed cell death, and autophagy, a survival mechanism that helps cells adapt to adverse conditions.ApoptosisApoptosis removes aged or injured cells to maintain tissue balance. During this process, the cell shrinks, chromatin condenses and fragments, and membrane-bound...

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Visualization of Inflammatory Caspases Induced Proximity in Human Monocyte-Derived Macrophages

Visualization of Inflammatory Caspases Induced Proximity in Human Monocyte-Derived Macrophages

Published on: April 6, 2022

Are metacaspases caspases?

Dominique Vercammen¹, Wim Declercq, Peter Vandenabeele

¹Department of Plant Systems Biology, Flanders Institute for Biotechnology, 9052 Gent, Belgium.

The Journal of Cell Biology

|October 31, 2007

Summary

This summary is machine-generated.

Metacaspases, found in plants and fungi, do not perform apoptosis like animal caspases. These distinct cysteine peptidases, including paracaspases, have functions beyond cell death.

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Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Caspases are key regulators of apoptosis in animals.
Metacaspases were discovered in plants, fungi, and protozoa, initially thought to be homologous to caspases.
Evidence suggests metacaspases lack direct caspase activity and are not responsible for observed caspaselike activities in plant and fungal cell death.

Purpose of the Study:

To broaden the understanding of metacaspase and paracaspase functions beyond apoptosis and cell death.
To propose a new classification for metacaspases and paracaspases within the cysteine peptidase clan CD.
To differentiate metacaspases and paracaspases from metazoan caspases.

Main Methods:

Comparative analysis of peptidase families.
Structural and mechanistic feature comparison.
Literature review and re-evaluation of existing data.

Main Results:

Metacaspases exhibit distinct biochemical properties compared to caspases.
Metacaspases and paracaspases show structural and mechanistic similarities to caspases but represent a separate family.
These peptidases belong to the cysteine peptidase clan CD.

Conclusions:

Metacaspases and paracaspases are not direct functional homologs of animal caspases in apoptosis.
Metacaspases and paracaspases possess unique biological roles independent of apoptosis.
A reclassification of metacaspases and paracaspases as distinct members of clan CD cysteine peptidases is proposed.