Target type: biologicalprocess
The change in morphology and behavior of a monocyte resulting from exposure to a cytokine, chemokine, cellular ligand, or soluble factor. [GOC:mgi_curators, ISBN:0781735149]
Monocyte activation is a crucial process in the innate immune response, involving a complex series of events triggered by various stimuli, such as pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). These stimuli bind to pattern recognition receptors (PRRs) expressed on the monocyte surface, initiating intracellular signaling cascades that lead to profound changes in monocyte function.
Upon activation, monocytes undergo a rapid transformation, becoming highly phagocytic and capable of releasing a diverse array of inflammatory mediators. This process involves the upregulation of cell surface receptors, including integrins and chemokine receptors, enabling monocytes to adhere to and migrate towards sites of infection or tissue injury.
The activation of monocytes also results in the production and release of a wide range of cytokines, including TNF-α, IL-1β, IL-6, and chemokines like CCL2 and CCL5. These cytokines act as signaling molecules that recruit other immune cells to the site of inflammation, modulate the adaptive immune response, and contribute to tissue repair.
Moreover, activated monocytes differentiate into macrophages and dendritic cells, specialized phagocytic cells that play vital roles in engulfing and destroying pathogens, presenting antigens to T lymphocytes, and initiating adaptive immune responses.
In summary, monocyte activation is a tightly regulated process that involves a complex interplay of signaling pathways, transcriptional changes, and functional modifications, leading to the production of inflammatory mediators, phagocytosis, and differentiation into macrophages and dendritic cells. These changes are essential for the effective clearance of pathogens and the initiation of adaptive immune responses.'
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| Protein | Definition | Taxonomy |
|---|---|---|
| Disintegrin and metalloproteinase domain-containing protein 9 | A disintegrin and metalloproteinase domain-containing protein 9 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q13443] | Homo sapiens (human) |
| Disintegrin and metalloproteinase domain-containing protein 10 | A disintegrin and metalloproteinase domain-containing protein 10 that is encoded in the genome of human. [PRO:WCB, UniProtKB:O14672] | Homo sapiens (human) |
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| ilomastat | CS 610: matrix metalloproteinase inhibitor; structure in first source ilomastat : An N-acyl-amino acid obtained by formal condensation of the carboxy group of (2R)-2-[2-(hydroxyamino)-2-oxoethyl]-4-methylpentanoic acid with the amino group of N-methyl-L-tryptophanamide. A cell permeable broad-spectrum matrix metalloproteinase (MMP) inhibitor | hydroxamic acid; L-tryptophan derivative; N-acyl-amino acid | anti-inflammatory agent; antibacterial agent; antineoplastic agent; EC 3.4.24.24 (gelatinase A) inhibitor; neuroprotective agent |
| pepstatin | pepstatin: inhibits the aspartic protease endothiapepsin | pentapeptide; secondary carboxamide | bacterial metabolite; EC 3.4.23.* (aspartic endopeptidase) inhibitor |
| bms-566394 | BMS-566394: structure in first source | ||
| incb3619 | INCB3619: ADAM inhibitor; structure in first source | ||
| grassystatin a | grassystatin A: isolated from a cyanobacterium, identified as Lyngbya cf.; structure in first source |