Cathelicidin-related anti-microbial peptide (CRAMP) is the mouse homologue of the human LL-37 anti-microbial peptide. CRAMP possesses potent anti-bacterial activity against Gram-positive and Gram-negative bacterial strains with no haemolytic activity. As well as displaying direct anti-microbial activity, CRAMP also binds to lipopolysaccharide (LPS) to neutralise its activity. CRAMP is encoded for by the Cramp gene which is highly expressed in bone marrow and up-regulated by infectious and inflammatory signals, CRAMP is secreted by cells such as neutrophils epithelial cells and macrophages. This peptide represents the mature, extended, form of CRAMP, longer than the 34 amino acid peptide originally isolated from the bone marrow of mice. CRAMP (1-39) has enhanced anti-microbial activity compared to CRAMP (6-39).
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