Chemoattractant protein-1, amino acid sequence

Figure 1. Amino acid sequence of human Monocyte Chemoattractant Protein-1 (2,3).

The first diemokine, PF-4, was identified in 1977 [3] but it was not for almost a decade that other members of the family started to emerge, with the discovery of the proinflammatory chemokines IP-10 was identified in 1985 as a protein showing homology to PF4 [4], while IL-8 and the MI P-1 proteins were isolated in the late 1980s as active protein from tissues or culture supernatants. The neutrophil chemoattractant, IL-8, was purified from culture supernatant of stimulated blood monocytes [5] and the monocyte chemoattractants MIP-la and MIP-ip were purified from LPS-stimulated mouse macrophages [6]. The primary amino acid sequence of these chemokines rapidly led to the identification of the highly conserved four-cysteine motif described above and also allowed their classification into the two principal subclasses. The number of chemokines then grew rapidly... 

All of the CXC ligand proteins are active as chemoattractant factors. As mentioned earlier, the first chemokine identified was CXCLS, which has now been extensively characterized and will thus be used as a representative for this discussion on chemokine structures and functions. The amino-acid alignment of all the human CXC chemokines shown in Fig. 2 is therefore arranged with respect to CXCLS, and references to specific sections of CXCLs will be numbered according to the CXCLS primary sequence. 

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