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Volume 272, Number 20, Issue of May 16, 1997 pp. 13088-13093
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Identification of CRAMP, a Cathelin-related Antimicrobial Peptide Expressed in the Embryonic and Adult Mouse

(Received for publication, January 22, 1997, and in revised form, March 13, 1997)

Richard L. Gallo Dagger § , Katherine J. Kim § , Merton Bernfield § , Christine A. Kozak par , Margherita Zanetti **Dagger Dagger , Laura Merluzzi ** and Renato Gennaro **

From the Dagger  Joint Program in Neonatology, Children's Hospital, Boston, the § Department of Dermatology, Harvard Medical School, Boston, Massachusetts 02115, the par  National Institutes of Health, Bethesda, Maryland 20892, the ** Departimento di Scienze e Tecnologie Biomediche, University of Udine, Udine 1-33100, and the Dagger Dagger  National Laboratory Consorzio Interuniversitario Biotechnologie, Area Science Park, I-34012 Trieste, Italy

Cathelicidins are the precursors of potent antimicrobial peptides that have been identified in several mammalian species. Prior work has suggested that members of this gene family can participate in host defense through their antimicrobial effects and activate mesenchymal cells during wound repair. To permit further study of these proteins a reverse transcriptase-polymerase chain reaction approach was used to identify potential mouse homologs. A full-length 562-base pair cDNA clone was obtained encoding an NH2-terminal prepro domain homologous to other cathelicidins and a unique COOH-terminal peptide. This gene, named Cramp for cathelin-related antimicrobial peptide, was mapped to chromosome 9 at a region of conserved synteny to which genes for cathelicidins have been mapped in pig and man. Northern blot analysis detected a 1-kilobase transcript that was expressed in adult bone marrow and during embryogenesis as early as E12, the earliest stage of blood development. Reverse transcriptase-polymerase chain reaction also detected CRAMP expression in adult testis, spleen, stomach, and intestine but not in brain, liver, heart, or skeletal muscle. To evaluate further the expression and function of CRAMP, a peptide corresponding to the predicted COOH-terminal region was synthesized. CD spectral analysis showed that CRAMP will form an amphipathic alpha -helix similar to other antimicrobial peptides. Functional studies showed CRAMP to be a potent antibiotic against Gram-negative bacteria by inhibiting growth of a variety of bacterial strains (minimum inhibitory concentrations 0.5-8.0 µM) and by permeabilizing the inner membrane of Escherichia coli directly at 1 µM. Antiserum against CRAMP revealed abundant expression in myeloid precursors and neutrophils. Thus, CRAMP represents the first antibiotic peptide found in cells of myeloid lineage in the mouse. These data suggest that inflammatory cells in the mouse can use a nonoxidative mechanism for microbial killing and permit use of the mouse to study the role such peptides play in host defense and wound repair.


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