Macrophage inflammatory protein
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chemokine (C-C motif) ligand 3 | |
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Identifiers | |
Symbol | CCL3 |
Alt. symbols | SCYA3, MIP-1α |
Entrez | 6348 |
HUGO | 10627 |
OMIM | 182283 |
PDB | 1B50 More structures |
RefSeq | NM_002983 |
UniProt | P10147 |
Other data | |
Locus | Chr. 17 q12 |
chemokine (C-C motif) ligand 4 | |
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Identifiers | |
Symbol | CCL4 |
Alt. symbols | SCYA4, MIP-1β, LAG1 |
Entrez | 6351 |
HUGO | 10630 |
OMIM | 182284 |
PDB | 1HUM More structures |
RefSeq | NM_002984 |
UniProt | P13236 |
Other data | |
Locus | Chr. 17 q21-q23 |
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1α and MIP-1β that are now officially named CCL3 and CCL4, respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins.[3] They are crucial for immune responses towards infection and inflammation.[4] They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-α from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.[5]
They are produced by many cells, particularly macrophages, dendritic cells, and lymphocytes.[6] MIP-1 are best known for their chemotactic and proinflammatory effects but can also promote homoeostasis.[6] Biophysical analyses and mathematical modelling has shown that MIP-1 reversibly forms a polydisperse distribution of rod-shaped polymers in solution. Polymerization buries receptor-binding sites of MIP-1, thus depolymerization mutations enhance MIP-1 to arrest monocytes onto activated human endothelium.[4]
See also
References
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External links
- Macrophage Inflammatory Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
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