Macrophage inflammatory protein

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chemokine (C-C motif) ligand 3
1b53.png
Human Mip-1α dimer D26A mutant. PDB 1b53. [1] Disulfide bonds highlighted.
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
1hum.png
Human Mip-1β dimer. PDB 1hum.[2] Disulfide bonds highlighted.
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


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