Expression of VLA-integrins and their related basement membrane ligands in gingiva from patients of various periodontitis categories.
Periodontitis is characterized by destruction of dento-gingival fibers and apical migration of the junctional epithelium. Tissue destruction may be associated with altered interactions between epithelium and connective tissue mediated by integrins localized in the basement membrane zone. We examined the expression of alpha2beta1, alpha3beta1, alpha4/alpha5/beta1, alpha6beta4 and their related extracellular matrix (ECM) ligands: laminin-1, laminin-5, and collagen type IV in untreated periodontitis sites of various categories. The expression and location of ECM proteins along the basement membrane were found to be similar between clinically healthy and periodontitis affected tissues. However, ECM proteins were more diffusely distributed in connective tissue (CT) of periodontitis tissues as streak-like/ fibrillar/granular stainings, particularly beneath the pocket epithelium (PE) and around the blood vessels. This may reflect an increase in inflammatory cell migration. The more widespread distribution of integrins alpha2beta1, alpha3beta1 in PE of periodontitis specimens may be related to disease activity and increased rate of keratinocyte proliferation and migration. Moreover, the weaker expression of alpha6beta4 in junctional epithelium (JE) of periodontitis affected tissues may be related to the epithelial detachment from the tooth surface. Clarification of expressions of integrins and their ligands in relation to known clinical disease susceptibility factors may provide information on the onset and progression mechanisms of periodontal disease destruction.
Gürses
N
N
Department of Periodontology, Faculty of Dentistry, University of Ege, Izmir, Turkey. guerses@dishekimligi.ege.edu.tr
Thorup
A K
AK
Reibel
J
J
Carter
W G
WG
Holmstrup
P
P
D000293:Adolescent; D000328:Adult; D015703:Antigens, CD / Q000032:analysis; D000954:Antigens, Surface / Q000032:analysis; D001485:Basement Membrane / Q000378:metabolism* / Q000473:pathology; D002352:Carrier Proteins / Q000032:analysis; D015815:Cell Adhesion Molecules / Q000032:analysis; D002648:Child; D003094:Collagen / Q000032:analysis; D003238:Connective Tissue / Q000378:metabolism / Q000473:pathology; D004846:Epithelial Attachment / Q000378:metabolism / Q000473:pathology; D000939:Epitopes / Q000032:analysis; D016326:Extracellular Matrix Proteins / Q000032:analysis*; D005881:Gingiva / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D039201:Integrin alpha3beta1; D039441:Integrin alpha4; D039161:Integrin alpha6beta4; D019012:Integrin beta1 / Q000032:analysis; D016023:Integrins / Q000032:analysis*; D015603:Keratinocytes / Q000378:metabolism / Q000473:pathology; D007797:Laminin / Q000032:analysis; D008024:Ligands; D008875:Middle Aged; D010518:Periodontitis / Q000378:metabolism* / Q000473:pathology; D038981:Receptors, Collagen; D017469:Receptors, Fibronectin / Q000032:analysis; D017474:Receptors, Laminin / Q000032:analysis; D016201:Receptors, Lymphocyte Homing / Q000032:analysis; D000097794:Kalinin
D015703:Antigens, CD; D000954:Antigens, Surface; D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; D003094:Collagen; D000939:Epitopes; D016326:Extracellular Matrix Proteins; D039201:Integrin alpha3beta1; D039441:Integrin alpha4; D039161:Integrin alpha6beta4; D019012:Integrin beta1; D016023:Integrins; D007797:Laminin; D008024:Ligands; D038981:Receptors, Collagen; D017469:Receptors, Fibronectin; D017474:Receptors, Laminin; D016201:Receptors, Lymphocyte Homing; D000097794:Kalinin