Ultrastructural immunolocalization of laminin 332 (laminin 5) at dento-gingival interface in Macaca fuscata monkey

Abstract

Although laminin 332 (laminin 5), an extracellular matrix molecule involved in cell adhesion and migration, has been localized at the interface between the tooth enamel and junctional epithelium, its ultrastructural localization remains to be fully clarified. The purpose of the present study was to investigate the ultrastructural distribution of laminin 332 at the dento-gingival interface in Japanese monkey (Macaca fuscata) using pre- and post-embedding immunoelectron microscopy. Pre-embedding immunoelectron microscopy revealed a broad band of internal basal lamina together with supplementary lamina densa, and both showed immunolabeling for laminin 332. Immunoreaction products for laminin 332 were observed in the rough-surfaced endoplasmic reticulum of the junctional epithelial cells close to the tooth enamel. Post-embedding immunoelectron microscopy revealed an increase in the number of immunogold particles toward the coronal portion, resulting in a large accumulation of particles on the basal lamina, preferentially on the lamina densa. Concomitantly the dental cuticle at the dento-gingival interface was sporadically, but specifically, immunogold-labeled with anti-laminin 332 antibody. These data suggest that junctional epithelium actively produces laminin 332, and that the products accumulate at the dento-gingival interface during cell migration coronally towards the gingival sulcus.

Adenovirus-Mediated LAMA3 Transduction Enhances Hemidesmosome Formation and Periodontal Reattachment during Wound Healing

“…Our results revealed a strong immunoreactive band along the full length of the tooth–JE interface in the Ad-LAMA3 group, which was consistent with the IBL region. 45 , 46 …”

“…Our results revealed a strong immunoreactive band along the full length of the tooth-JE interface in the Ad-LAMA3 group, which was consistent with the IBL region. 45,46 Next, we explored if Ad-LAMA3 promoted HD formation. Scholars have shown that the interaction between integrin b4 and plectin has a crucial role in HD assembly.…”

Proteoglycans in the periodontium: A review with emphasis on specific distributions, functions, and potential applications

“…40,45 However, human research on severely inflamed junctional/pocket epithelium has elucidated that not only is syndecan-1 present in outer layers but also more highly expressed in areas close to teeth (Figure 6B). 46 Given that binding between syndecan-1 and laminin-5, a molecule in tooth-facing cells, 47 can prevent cellular migration and motility, 48 we hypothesize that further studies might focus on the potential function of syndecan-1 in epithelial reattachment, which is an ideal healing pattern for periodontitis. 13 Conversely, in healthy gingiva, syndecan-1 is pinpointed mainly in the suprabasal layer, 34,49 has been verified during gingival keratinocytes differentiation, 50 consistent with the finding that epithelial syndecan-1 is negatively correlated with the invasiveness of head and neck squamous cell carcinoma (including GSCC).…”

A Pilot Study of Antibody Drug Therapy to Regulate Cell Adhesion in Dental Implants

“…In the oral cavity, laminin-332 is also an important factor as it influences epithelial cell behavior in dental implant therapy and wound healing [15] [16] [17].…”