Association between bleeding periodontal pockets and eczemas: Results of the Northern Finland Birth Cohort 1966.

Aim: To investigate whether the periodontal condition as measured by bleeding periodontal pockets is associated with atopic dermatitis, seborrheic dermatitis, and eczema nummulare.

Materials And Methods: The study population (n = 1871) was obtained from the 46-year follow-up study of the Northern Finland Birth Cohort 1966 study (NFBC1966). The periodontal condition was measured by the number of sites with bleeding periodontal pockets that were ≥4 mm deep.

Prevalence of oral mucosal normal variations and lesions in a middle-aged population: a Northern Finland Birth Cohort 1966 study.

Background: In this cross-sectional study we investigated the oral mucosal changes in a middle-aged Finnish population. We analyzed the prevalence of potentially malignant disorders and the influence of smoking, snuff and alcohol use on the mucosal changes.

Methods: Of the 12,068 members of the NFBC 1966, a total of 1961 participants (16.

Trypsin-2 enhances carcinoma invasion by processing tight junctions and activating ProMT1-MMP.

Enhanced proteolysis and altered tight junction (TJ) proteins associate with carcinoma invasion. We hypothesized that trypsin-2, a tumor-associated serine proteinase, induces tongue carcinoma invasion by activating pro-membrane type-1 matrix metalloproteinase (MT1-MMP) and disturbing the TJs. The effects of invasion were analyzed using trypsin-2 over-expressing human tongue squamous cell carcinoma cells (Try2-HSC-3) in vitro and in vivo.

Matrix metalloproteinase-8 concentration in shallow crevices associated with the extent of periodontal disease.

Objective: The aim of this study was to analyse the association between matrix metalloproteinase-8 (MMP-8) concentration in shallow, mostly non-bleeding gingival crevices, and the extent of periodontal disease.

Material And Methods: Plaque, bleeding on probing (BOP), probing pocket depth (PPD) and attachment level (AL) were assessed clinically in 48 patients with chronic periodontitis. MMP-8 concentrations in gingival crevicular fluid (GCF) from four shallow (PPD View Article and Find Full Text PDF

Intracellular co-localization of trypsin-2 and matrix metalloprotease-9: possible proteolytic cascade of trypsin-2, MMP-9 and enterokinase in carcinoma.

Tumor-associated trypsin-2 and matrix metalloprotease-9 (MMP-9) are associated with cancer, particularly with invasive squamous cell carcinomas. They require activation for catalytical competence via proteolytic cascades. One cascade is formed by enterokinase, trypsin-2 and MMP-9; enterokinase activates trypsinogen-2 to trypsin-2, which is an efficient proMMP-9 activator.

Collagen XVIII modulation is altered during progression of oral dysplasia and carcinoma.

Background: Collagen XVIII is a ubiquitous basement membrane (BM) component and a precursor of endostatin.

Methods: Using immunohistochemistry and in situ hybridization, we studied the expression and localization of collagen XVIII in different stages of normal oral wound healing, epithelial dysplasia and squamous cell carcinoma (SCC).

Results: In mild epithelial dysplasias collagen XVIII appeared as a continuous signal in the BM, whereas in severe epithelial dysplasias and in the invasive areas of oral SCCs collagen XVIII was absent.

Trypsins and their role in carcinoma growth.

There are more than 100 distinct types of cancer, and subtypes can be found within specific organs. Cancer progression is a complex multi-step process. These steps reflect alterations that drive the progressive transformation of normal cells into highly malignant ones.