title: Associations between mast cells and laminin in oral lichen planus.
abstract: Mast cell numbers are increased significantly in oral lichen planus (OLP). In other inflammatory conditions, mast cells frequently adhere to extracellular matrix proteins such as laminin. The aim of this study, therefore, was to determine whether the distribution of mast cells in OLP is related topographically to laminin in vascular and epithelial basement membranes. Monoclonal antibodies for tryptase, laminin and the alpha6beta1 CD49f laminin-binding integrin were used to identify mast cells, basement membranes (blood vessels and basal epithelium) and the "classical" laminin adhesion receptor, respectively. A double-labelling immunoperoxidase technique was employed to examine and compare mast cell-laminin relationships in OLP (n=19) and normal buccal mucosa (NBM, n=13). In both OLP and NBM, the majority of mast cells were located close to vascular basement membranes. Quantitative studies revealed that the number of mast cells associated with the laminin of vascular basement membranes (distance <1 microm) was two-fold and three-fold higher, respectively, in the superficial and deep layers in OLP compared with NBM (P<0.001). The frequency distribution of mast cells associated with basal epithelium was not statistically different in both groups (P>0.05). The association of mast cells with laminin may be an important determinant of mast cell density in OLP During OLP lesion formation and progression, the preferential distribution of mast cells in the immediate perivascular region provides an ideal situation for mast cell-derived mediators to influence the vascular endothelium.
authors.affiliation: Oral Biology & Pathology, School of Dentistry, The University of Queensland, Australia.
authors.forename: Z Z
authors.initials: ZZ
authors.lastname: Zhao
authors.forename: N W
authors.initials: NW
authors.lastname: Savage
authors.forename: L J
authors.initials: LJ
authors.lastname: Walsh
mesh_terms: D043925:Angiogenesis Inducing Agents / Q000737:chemistry; D000911:Antibodies, Monoclonal; D001485:Basement Membrane / Q000473:pathology; D001808:Blood Vessels / Q000473:pathology; D002448:Cell Adhesion; D002452:Cell Count; D016009:Chi-Square Distribution; D053818:Chymases; D018450:Disease Progression; D004848:Epithelium / Q000473:pathology; D005109:Extracellular Matrix / Q000473:pathology; D006801:Humans; D007124:Immunoenzyme Techniques; D018836:Inflammation Mediators / Q000737:chemistry; D039121:Integrin alpha6beta1; D019012:Integrin beta1 / Q000648:ultrastructure; D016023:Integrins / Q000648:ultrastructure; D007797:Laminin / Q000648:ultrastructure*; D017676:Lichen Planus, Oral / Q000473:pathology*; D008407:Mast Cells / Q000473:pathology*; D017474:Receptors, Laminin / Q000648:ultrastructure; D012697:Serine Endopeptidases / Q000648:ultrastructure; D053802:Tryptases
chemical_list: D043925:Angiogenesis Inducing Agents; D000911:Antibodies, Monoclonal; D018836:Inflammation Mediators; D039121:Integrin alpha6beta1; D019012:Integrin beta1; D016023:Integrins; D007797:Laminin; D017474:Receptors, Laminin; D012697:Serine Endopeptidases; C083294:chymase 2; D053818:Chymases; D053802:Tryptases