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Infection and Immunity, October 2000, p. 5552-5558, Vol. 68, No. 10
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Regulation of Cathelicidin Gene Expression: Induction by Lipopolysaccharide, Interleukin-6, Retinoic Acid, and Salmonella enterica Serovar Typhimurium Infection

Hua Wu,1 Guolong Zhang,1 J. Ernest Minton,2 Christopher R. Ross,1 and Frank Blecha1,*

Departments of Anatomy and Physiology1 and Animal Sciences and Industry,2 Kansas State University, Manhattan, Kansas 66506

Received 11 April 2000/Accepted 10 July 2000

Cathelicidins are a family of antimicrobial peptides prominent in the host defense mechanisms of several mammalian species. In addition to their antimicrobial activities, these peptides have been implicated in wound healing, angiogenesis, and other innate immune mechanisms. To investigate the regulatory mechanisms of cathelicidin gene expression, we conducted in vitro experiments evaluating the bone marrow cell expression of two porcine cathelicidins, PR-39 and protegrin, and cloned and evaluated the promoter sequence of PR-39. In addition, we evaluated in vivo kinetics of cathelicidin gene expression in pigs during an infection with Salmonella enterica serovar Typhimurium. Lipopolysaccharide (LPS) increased PR-39 and protegrin mRNA expression, which was ameliorated by polymyxin B. Concentrations of PR-39 in supernatants from bone marrow cell cultures were increased 10-fold after LPS stimulation. Similarly, interleukin-6 (IL-6) and all-trans retinoic acid (RA) markedly induced cathelicidin gene expression. To verify the transcriptional activation of the PR-39 gene by these agents, we made a PR-39 promoter-luciferase construct containing the full-length PR-39 promoter driving luciferase gene expression and transiently transfected PK-15 epithelial cells. RA and IL-6 increased luciferase activity in PK-15 cells transfected with the PR-39 promoter-luciferase reporter. Similarly, Salmonella-challenged pigs showed increased expression of PR-39 and protegrin mRNA in bone marrow cells at 6 and 24 h postchallenge. Taken together, these findings show that bacterial products (LPS), IL-6, RA, and Salmonella infection enhance the expression of the cathelicidins, PR-39 and protegrin, in bone marrow progenitor cells, and we suggest that extrinsic modulation of this innate host defense mechanism may be possible.

* Corresponding author. Mailing address: Department of Anatomy and Physiology, College of Veterinary Medicine, VMS 228, 1600 Denison Ave., Kansas State University, Manhattan, KS 66506-5602. Phone: (785) 532-4537. Fax: (785) 532-4557. E-mail: blecha{at}vet.ksu.edu.

Infection and Immunity, October 2000, p. 5552-5558, Vol. 68, No. 10
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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