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Biomedical subjects

Barbara Janssens

Publications and source records attributed to Barbara Janssens.

9 recordsLinked to original sources
PubMed2026

Association of Social Support With Oral Health in Older Adults: A Systematic Review and Meta-Analysis.

BACKGROUND: Social support is an important determinant of health in later life, yet no study has synthesised the relevant evidence. This systematic review and meta-analysis aimed to synthesise evidence on the association between social support (functional, structural, and perceived dimensions) and oral health among older adults aged 75 years and over. METHODS: The review process, using a systematic approach and random-effects meta-analysis, was conducted in accordance with PRISMA guidelines. Searches were carried out in Medline, Embase, and CENTRAL up to November 2025. Eligible studies examined associations between social support and oral health, including dentition status, oral conditions, oral function, oral health behaviours, and oral health-related quality of life. Risk of bias was assessed using the Newcastle-Ottawa Scale. RESULTS: Forty studies were included. Meta-analyses showed that low functional support-defined as having fewer people to rely on-was associated with edentulism (OR 1.21, 95% CI: 1.15, 1.27) and non-regular dental service use (OR 1.20, 95% CI: 1.17, 1.23). Low structural support, in terms of living conditions, was associated with edentulism and lacking functional dentition (OR 1.34, 95% CI: 1.02, 1.75; and OR 1.41, 95% CI: 1.20, 1.67, respectively). The evidence on the associations between low social support and other oral health measures was sparse and heterogeneous. CONCLUSION: Poor social support was associated with poor dentition status and oral health behaviours among older adults aged 75 years and over. These findings underscore the importance of incorporating psychosocial factors into oral health assessment and care planning for this population. TRIAL REGISTRATION: PROSPERO; registration number: CRD420251231319.

Humans↗
PubMed2026

Association of Socioeconomic Factors With Oral Health in Older Adults: A Systematic Review and Meta-Analysis.

BACKGROUND: Oral diseases remain disproportionately prevalent among older adults. However, evidence on oral health inequalities among older adults remains dispersed across studies that have used different socioeconomic indicators and oral health measures and has not been synthesised. OBJECTIVE: To synthesise the evidence on the association between socioeconomic factors and oral health among older adults aged 75 years and older. METHODS: A systematic review and meta-analysis was conducted following PRISMA guidelines. The Medline, Embase, and CENTRAL databases were searched. Studies reporting socioeconomic factors (education, income, occupation, area-level deprivation, and multi-aspect socioeconomic position) and oral health (dentition status, dental caries, periodontal disease, dry mouth, oral function, oral health behaviours, and oral health-related quality of life (OHRQoL)) among older adults were included. Risk of bias was assessed using the Newcastle-Ottawa Scale. RESULTS: Sixty-eight studies were included. Meta-analyses showed that socioeconomic disadvantage in older adults was associated with: (1) poor dentition status: fewer natural teeth, higher prevalence of edentulism, and lacking a functional dentition; (2) more teeth with decay; (3) irregular dental attendance; and (4) poorer OHRQoL. Similar patterns were generally observed for periodontal disease, dry mouth, and oral function, although no meta-analysis could be performed due to limited evidence and heterogeneous oral health measures. CONCLUSION: Socioeconomic disadvantage was consistently associated with poor oral health in older adults. Associations were more pronounced for dentition status, reflecting the cumulative socioeconomic disadvantage over the life course. Socioeconomic factors should be considered to inform prevention, clinical decision-making and oral healthcare planning for the ageing population. TRIAL REGISTRATION: PROSPERO Registration CRD420251231319.

Aged↗
PubMed2006

Truncated isoform of mouse alphaT-catenin is testis-restricted in expression and function.

AlphaT-catenin is a recently identified member of the alpha-catenin family of cell-cell adhesion molecules. For decades it was thought that alpha-catenins mediate solid cell-cell adhesion by linking the cadherin-mediated cell-cell adhesion complex with the actin cytoskeleton. However, the roles of alpha-catenins in this classical adhesion model have been questioned recently. AlphaT-catenin has a restricted expression pattern, in contrast to the ubiquitously expressed alphaE-catenin. High levels of alphaT-catenin were detected in heart and testis. Northern and Western blot experiments indicated that besides the standard full-length alphaT-catenin transcript, smaller alternative transcripts are expressed in testis. We report the cloning of two alternative transcripts of the mouse alphaT-catenin gene (transcript-B and -X), both of which are expressed in a testis-restricted manner from two putative alternative promoters. Alternative transcript-X encodes a smaller protein, isoform-X, which lacks the amino-terminal beta-catenin binding domain of the standard mouse alphaT-catenin protein, and is therefore unable to restore cell-cell adhesion in an alpha-catenin-negative colon carcinoma cell line. Immunohistochemical analysis showed specific localization of the alphaT-catenin isoform-X in the differentiating germ cells. In contrast to the standard full-length alphaT-catenin protein, this shortened isoform-X can bind to l-afadin, an important component of the nectin/afadin/ponsin adhesion complex that reportedly is essential for spermatogenesis.

Animals↗
PubMed2004

Alpha-catenin is required for IGF-I-induced cellular migration but not invasion in human colonic cancer cells.

The mechanisms by which growth factors cooperate with cell adhesion molecules to modulate epithelial cell motility remain poorly understood. Here, we investigated the role of the E-cadherin/catenin complex in insulin-like growth factor (IGF-I)-dependent cell migration and invasion. We used variants of the HCT-8 colon cancer family that differ in their expression of alphaE-catenin, an intracellular molecule that links the E-cadherin/catenin complex to the actin cytoskeleton. Migration was determined using a monolayer wound model and cell invasion by the penetration of the cells into type-I collagen gels. We showed that alpha-catenin-deficient cells were not able to migrate in cohort upon IGF-I stimulation. Transfection of these cells with alpha-catenin isoforms (alphaN- or alphaT-catenin) restored migratory response IGF-I. These results suggest that alpha-catenins are involved in the signal issued from the E-cadherin/catenin complex to regulate IGF-I-stimulated migration. In contrast, IGF-I promoted invasion of both alpha-catenin-deficient and alpha-catenin-expressing cells, indicating that alpha-catenin did not participate in the regulation of IGF-I-induced invasion. Inhibition of E-cadherin function by treatment with MB-2 monoclonal antibodies inhibited both IGF-I-dependent cell migration and invasion. Taken together, our results indicate that functional alpha-catenin is essential for migration but not for invasion, while E-cadherin is involved in both phenomena.

Antibodies, Monoclonal↗
PubMed2004

Differential downregulation of alphaT-catenin expression in placenta: trophoblast cell type-dependent imprinting of the CTNNA3 gene.

The alphaE-catenin is a well-known invasion suppressor. A recently described novel alpha-catenin, i.e. alphaT-catenin (CTNNA3), shows related functions being necessary for the formation of cell-cell adhesion complexes. We recently demonstrated that the 10q21.3 region containing the CTNNA3 gene shows a parent-of-origin effect and that transcription of the CTNNA3 gene is downregulated in placental tissues of complete androgenetic origin. As this suggests that the CTNNA3 gene is subject to imprinting, we performed allele-specific RT-PCR on early placenta tissues using informative heterozygous samples. This was supplemented by immunostaining for alphaT-catenin, p57KIP2 and low molecular weight cytokeratin in tissues of a partial hydatidiform mole. As shown here we demonstrate that the CTNNA3 gene is subject to imprinting with preferential expression of the maternal allele in first trimester placental tissues. Imprinting, however, is trophoblast cell type-dependent: expression in extravillus trophoblast is biallelic; expression in villus cytotrophoblast is from the maternal allele only. Expression of alphaT-catenin is lost in villus syncytiotrophoblast as well as in extravillus trophoblast following epithelial-mesenchymal transition. The trophoblast cell type-dependent imprinting of CTNNA3 is identical to p57KIP2 imprinting with respect to trophoblast cell type (villus) and parental origin of the expressed allele (maternal). This suggests that gene dosage compensation of CTNNA3 and p57KIP2 in the placenta shares a conserved regulatory mechanism that correlates with an early step in trophoblast determination, i.e. differentiation into villus or extravillus trophoblast.

Cytoskeletal Proteins↗
PubMed2004

Mediterranean views on epithelial polarity.

Developmental and cell biologists viewed polarity through each other's eyes at the EMBO workshop on Epithelial Polarity in Development and Disease, March 27-31 2004, in Carry-le-Rouet, France, a small village west of Marseille on the rocky Mediterranean coast. The presentations highlighted our growing understanding, not only of the molecular mechanisms underlying polarity and the conservation of polarity complexes from worms to mammals, but also the diverse roles that epithelial polarity has during development.

Animals↗
PubMed2004

Alpha-T-catenin is expressed in human brain and interacts with the Wnt signaling pathway but is not responsible for linkage to chromosome 10 in Alzheimer's disease.

The gene encoding alpha-T-catenin, CTNNA3, is positioned within a region on chromosome 10, showing strong evidence of linkage to Alzheimer's disease (AD), and is therefore a good positional candidate gene for this disorder. We have demonstrated that alpha-T-catenin is expressed in human brain, and like other alpha-catenins, it inhibits Wnt signaling and is therefore also a functional candidate. We initially genotyped two single-nucleotide polymorphisms (SNPs) in the gene, in four independent samples comprising over 1200 cases and controls but failed to detect an association with either SNP. Similarly, we found no evidence for association between CTNNA3 and AD in a sample of subjects showing linkage to chromosome 10, nor were these SNPs associated with Abeta deposition in brain. To comprehensively screen the gene, we genotyped 30 additional SNPs in a subset of the cases and controls (n > 700). None of these SNPs was associated with disease. Although an excellent candidate, we conclude that CTNNA3 is unlikely to account for the AD susceptibility locus on chromosome 10.

Aged↗
PubMed2002

Assessment of the CTNNA3 gene encoding human alpha T-catenin regarding its involvement in dilated cardiomyopathy.

Alpha T-catenin is a novel member of the alpha-catenin family, which shows most abundant expression in cardiomyocytes and in peritubular myoid cells of the testis, pointing to a specific function for alpha T-catenin in particular muscle tissues. Like other alpha-catenins, alpha T-catenin provides an indispensable link between the cadherin-based cell-cell adhesion complex and the cytoskeleton, to mediate cell-cell adhesion. By isolating genomic clones, combined with database sequence analysis, we have been able to determine the structure of the CTNNA3 and Ctnna3 genes, encoding human and mouse alpha T-catenin, respectively. The positions of the exon-exon boundaries are completely conserved in CTNNA3, Ctnna3, and the alpha N-catenin encoding CTNNA2 gene. They overlap largely with the boundaries of the CTNNA1 and CTNNAL1 genes encoding alpha E-catenin and alpha-catulin, respectively. This emphasizes that these alpha-catenin genes evolved from the same ancestor gene. Nevertheless, the introns of CTNNA3 and Ctnna3 are remarkably large (often more than 100 kb) compared with introns of other CTNNA genes. The CTNNA3 gene was mapped to chromosome band 10q21 by both fluorescence in situ hybridization and polymerase-chain-reaction-based hybrid mapping. This region encodes a gene for autosomal dominant familial dilated cardiomyopathy (DCM), a common cause of morbidity and mortality. As alpha T-catenin is highly expressed in healthy heart tissue, we have considered CTNNA3 as a candidate disease gene in a family showing DCM linkage to the 10q21-q23 locus. Mutation screening of all 18 exons of the CTNNA3 gene in this family has, however, not detected any DCM-linked CTNNA3 mutations.

Amino Acid Sequence↗