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Objective: The purpose of this study was to isolate and to identify an antimicrobial peptide, human alpha-defensin-1 (HNP-1) in jaw cyst fluid., Study Design: We collected jaw cyst fluid from 22 patients with various jaw cysts and analyzed the peptide components of them by reversed-phase high-performance liquid chromatography (HPLC). HNP-1 in the jaw cyst fluid was identified by the amino acid sequence and the molecular weight. The concentration of HNP-1 in the fluid of various jaw cysts was quantified by HPLC., Results: HNP-1 in the jaw cyst fluid was isolated, purified, and identified. The concentrations of HNP-1 in the jaw cyst fluid ranged from 27.0 to 3725.4 microg/mL., Conclusion: HNP-1 was detected in the fluid of various types of jaw cysts.

The purpose of this study was the immunohistochemical localization and distribution of HNP-1 in the submandibular glands of patients with oral carcinomas. Tissue sections were embedded in paraffin, and HNP-1 was immunostained by the streptavidin-biotin coupled peroxidase method. Striated duct cells in the submandibular glands were stained with anti-defensin antibody. Neutrophils and capillary intimal cells were also stained. Defensins (HNPs) are peptides that occur in neutrophils and protect against bacteria and tumor cells. Human alpha-defensin-1 (HNP-1) is such a peptide, possessing both antimicrobial and cytotoxic activities. The presence of HNP-1 in striated duct cells in the submandibular glands of oral cancer patients, suggests a likely role in tumor immunity, for this peptide.

We aimed to immunohistochemically study the localization of defensin (HNPs), a family of peptides with antimicrobial and cytotoxic activity, in oral tumor tissue. Therefore, tissue sections were embedded in paraffin, and defensin was immunostained by the streptavidin-biotin coupled peroxidase method. Langerhans cells were confirmed by indirect immunostaining with anti-S-100 protein polyclonal antibody. Melanocytes were stained with Fontana-Masson's stain. Neutrophils and intimal cells were stained by anti-defensin antibody. Langerhans cells in normal epithelium or dysplasic epithelium adjacent to squamous cell carcinoma and precancerous lesion were also stained. Defensins (HNPs) are nonspecific peptides that occur in neutrophils and protect against bacteria, fungi, and tumor cells. Since defensins are also found in epithelial Langerhans cells adjacent to tumor tissue, these peptides most likely have a role in tumor immunity.

Objective: The purpose of this study was to investigate the presence of an antimicrobial peptide, human defensin-1, in the saliva of patients with oral inflammation., Study Design: Whole saliva samples were collected from patients with oral inflammation and from healthy volunteers. Human defensin-1 in saliva was isolated and purified by reversed-phase high-performance liquid chromatography. The amino acid sequence and molecular weight of defensin-1 were determined. The concentration of defensin-1 in saliva was quantified by high-performance liquid chromatography. Serum C-reactive protein concentration was measured by particle-enhanced turbidimetric immunoassay., Results: The salivary defensin-1 concentration was significantly higher in patients with oral inflammation than in healthy volunteers; furthermore, in patients with oral inflammation, the concentration was significantly higher before treatment than after treatment. In the patients with oral inflammation, there was a strong positive correlation between salivary defensin-1 concentration and serum C-reactive protein concentration., Conclusions: The findings suggest that defensin-1 in saliva may be a convenient marker of inflammation associated with oral disease.

Objectives and Design: A preceding paper has noted a detection of defensin-1 (HNP-1), a peptide with antimicrobial and cytotoxic properties, in the saliva of patients with oral squamous cell carcinoma. The present study deals with the presence of HNP-1 in the saliva of patients with various oral diseases., Methods: Whole saliva samples were obtained from the patients. HNP-1 in the saliva was isolated and purified by HPLC and the amino acid sequence of the peptide was determined. The molecular weight of HNP-1 was measured by mass spectrometry. The concentration of HNP-1 in saliva was determined by comparing the height of eluted HNP-1 with that of a synthetic HNP-1 standard., Results: The concentrations of HNP-1 in the saliva of patients with oral lichen planus (n = 5), leukoplakia (n = 4), and glossitis associated with iron deficiency (n = 4) were 8.3 +/- 4.3 micrograms ml-1, 13.2 +/- 7.9 micrograms ml-1, and 11.4 +/- 4.9 micrograms ml-1, (mean +/- s.d.), respectively. These concentrations were significantly higher than those in healthy subjects (0.8 microgram ml-1) (P < 0.01). In contrast, salivary HNP-1 concentrations in patients with glossodynia (n = 4) and oral discomfort (n = 4) were similar to those in healthy subjects., Conclusions: Since HNP-1 is a non-specific defensive peptide present in neutrophils, it may play an important role in the protection against diseases such as oral lichen planus, leukoplakia, and glossitis associated with iron deficiency.

The saliva of patients with oral squamous cell carcinoma was subjected to reversed-phase HPLC, and a peak (P 14) was eluted with a linear gradient of acetonitrile. The molecular weight of P14 was 3,442 daltons by mass spectrometry. The results of amino acid sequencing by Edman degradation and homology studies indicated that P14 was consistent with a peptide, human alpha-defensin 1 (HNP-1) which belongs to the defensin family. The concentration of HNP-1 in the saliva of 6 squamous cell carcinoma patients before surgery and 11 after surgery was 12.3 +/- 8.6 and 6.5 +/- 5.9 micrograms/ml (mean +/- S.D.), respectively. In contrast, minimal amounts of HNP-1 were found in the saliva of adenocarcinoma patients and healthy volunteers. The concentration of salivary HNP-1 correlated positively with serum squamous cell carcinoma related antigen (SCC-Ag)level (r = 0.879, p < 0.01).

We examined a patient with cleidocranial dysplasia (CCD) and cleft lip and found a new stop codon mutation in CBFA1. This mutation was a heterozygous C-to-T transition in exon 3 of CBFA1. This nucleotide change converts a CAA codon to a TAA (stop) codon at amino acid position Gln195 in the runt domain of CBFA1. [ABSTRACT FROM AUTHOR]