Human beta-defensin-1: an antimicrobial peptide of urogenital tissues.
Open Access
- 15 April 1998
- journal article
- Published by American Society for Clinical Investigation in Journal of Clinical Investigation
- Vol. 101 (8), 1633-1642
- https://doi.org/10.1172/jci1861
Abstract
Antimicrobial peptides are widely distributed mediators of innate host defense in animals and plants. A 36 amino acid antimicrobial peptide belonging to the defensin family, and named human beta-defensin-1 (HBD-1), was purified recently from hemodialysate fluid, but its tissue sources were not identified. By Northern blotting, we found the highest concentrations of HBD-1 mRNA in the kidney and the female reproductive tract. In situ hybridization localized the HBD-1 mRNA in the epithelial layers of the loops of Henle, distal tubules, and the collecting ducts of the kidney and the epithelial layers of the vagina, ectocervix, endocervix, uterus, and fallopian tubes in the female reproductive tract. Using a novel technique designed to detect cationic peptides in urine, we recovered several forms of HBD-1 ranging in length from 36 to 47 amino acid (aa) residues and differing from each other by amino terminal truncation. The total concentration of HBD-1 forms in voided urine was estimated at 10-100 microg/liter, with individual variations in the total amount of HBD-1 peptides and the relative proportion of HBD-1 forms. Multiple forms of HBD-1 (size 36-47 aa) were also found in the blood plasma, bound to carrier macromolecules that released the peptide under acid conditions, and in vaginal mucosal secretions (39, 40, and 44 aa). By immunostaining, HBD-1 was located in the kidney within the lumen of the loops of Henle, but no intracellular storage sites were identified in renal or female reproductive tissues. Recombinant HBD-1 forms (36, 39, and 42 aa) and natural HBD-1 forms were antimicrobial to laboratory and clinical strains of Escherichia coli at micromolar concentrations. HBD-1 activity was not changed appreciably by low pH, but was inhibited by high salt conditions. Some of the HBD-1 peptides retained their activity against E. coli in unconcentrated (low conductance) urine, and the 36 aa form was microbicidal even in normal (high conductance) urine. Production of HBD-1 in the urogenital tract could contribute to local antimicrobial defense.This publication has 38 references indexed in Scilit:
- The Human β-Defensin-1 and α-Defensins Are Encoded by Adjacent Genes: Two Peptide Families with Differing Disulfide Topology Share a Common AncestryGenomics, 1997
- Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA.Proceedings of the National Academy of Sciences, 1991
- Ultrasensitive assays for endogenous antimicrobial polypeptidesJournal of Immunological Methods, 1991
- A novel mouse gene family coding for cationic, cysteine-rich peptides. Regulation in small intestine and cells of myeloid origin.Journal of Biological Chemistry, 1990
- Preliminary observations on lactoferrin secretion in human vaginal mucus: Variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with Neisseria gonorrhoeaeAmerican Journal of Obstetrics and Gynecology, 1987
- Defensins. Natural peptide antibiotics of human neutrophils.Journal of Clinical Investigation, 1985
- Hybridization of nucleic acids immobilized on solid supportsAnalytical Biochemistry, 1984
- Renal tubular processing of small peptide hormones.1982
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979
- A Bactericidal Effect for Human LactoferrinScience, 1977