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Blood, 15 June 2005, Vol. 105, No. 12, pp. 4561-4568.
Prepublished online as a Blood First Edition Paper on February 17, 2005; DOI 10.1182/blood-2004-12-4618.


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CHEMOKINES

Identification of carboxypeptidase N as an enzyme responsible for C-terminal cleavage of stromal cell-derived factor-1{alpha} in the circulation

David A. Davis, Kathleen E. Singer, Maria De La Luz Sierra, Masashi Narazaki, Fuquan Yang, Henry M. Fales, Robert Yarchoan, and Giovanna Tosato

From the HIV and AIDS Malignancy Branch, the Experimental Transplantation and Immunology Branch, National Cancer Institute, and the Laboratory of Biophysical Chemistry, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, MD.

The chemokine stromal-derived factor-1{alpha} (SDF-1{alpha}) is an essential regulator of hematopoiesis, lymphocyte homing, pre-B-cell growth, and angiogenesis. As SDF-1{alpha} is constitutively expressed in many tissues, chemokine function is mostly regulated by proteolytic degradation. Human serum cleaves the 68-amino acid chemokine, SDF-1{alpha}, at both termini. The enzyme or enzymes responsible for the removal of the carboxy-terminal lysine from SDF-1{alpha}, leading to significant reduction in biologic activity, have not been identified. Using a new biochemical assay for measuring the carboxy-terminal cleavage activity, we purified from serum and plasma a peptidase that specifically removes the carboxy-terminal lysine from SDF-1{alpha} and identified it as carboxypeptidase N (CPN, also known as kininase I, arginine carboxypeptidase, and anaphylotoxin inactivator). We demonstrate that SDF-1{alpha} in serum and plasma lacks the carboxy terminal lysine, and depletion of CPN from serum and plasma significantly reduces the SDF-1{alpha} carboxypeptidase activity. Purified CPN effectively and specifically removes the carboxy-terminal lysine from SDF-1{alpha} and significantly reduces the chemokine's biologic activity as a pre-B-cell growth factor and chemoattractant. Thus, in addition to its role as a regulator of the biologic activity of kinins and anaphylatoxins, CPN is an important regulator of the biologic activity of SDF-1{alpha} by reducing the chemokine-specific activity. (Blood. 2005;105:4561-4568)


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