Human CCL3(4-69) (C-C motif ligand 3(4-69); also known as MIP-1α(4-69)) is a 66-amino-acid N-terminally truncated CC chemokine that arises from proteolytic processing of full-length CCL3(1-69) during inflammation. It binds to the classical receptors CCR1, CCR3, and CCR5 with enhanced potency compared to the full-length form, mediating stronger chemotaxis of monocytes, T cells, NK cells, eosinophils, and immature dendritic cells to sites of inflammation or infection. Additional interactions include the atypical scavenger receptors ACKR1 and ACKR2, which internalize and degrade the ligand to regulate chemokine bioavailability and prevent excessive leukocyte recruitment. These interactions highlight CCL3(4-69)'s amplified role in acute inflammatory responses, HIV suppression, and hematopoietic stem cell inhibition. It is generated by enzymes such as CD26/dipeptidyl peptidase IV in activated tissues and contributes to processes such as antiviral defense, autoimmune diseases, and tumor progression.
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