title: Expression of 72-kDa gelatinase (matrix metalloproteinase-2) in the developing mouse craniofacial complex.
abstract: Tissue remodelling is an important feature during embryogenesis. Although the matrix metalloproteinases are believed to participate in these processes, the relation between matrix metalloproteinases and tissue remodelling during craniofacial morphogenesis remains unclear. The purpose of the study was to look for the presence of enzymes involved in extracellular matrix degradation during craniofacial morphogenesis. Protein expression of the matrix metalloproteinase, 72-kDa gelatinase (matrix metalloproteinase-2, gelatinase A, 72-kDa type IV collagenase) was studied by gelatine zymography and by indirect immunofluorescence with conventional and confocal microscopy. In the anterior region of the developing mouse face, 72-kDa gelatinase was labelled mainly in the tips and peripheral regions of the nasal and facial prominences. Upon contact and fusion of the prominences, the staining was intensely localized to the zone of the fusion and the tips and peripheral regions of the nasal prominences and the maxilla. The labelling of 72-kDa gelatinase was also present in the peripheral regions of the mandible, second branchial arch, and the face around the developing eye. However, during lens vesicle formation, the staining of 72-kDa gelatinase was absent in the invaginated lens ectoderm. After the lens had completely detached from the surface ectoderm, the staining was resumed in the corneal epithelium and mesenchyme. Gelatine zymography was used to confirm the presence of active and latent 72-kDa gelatinase in the developing mouse craniofacial complex. Collectively, these data indicate that 72-kDa gelatinase may play a significant part in localized tissue remodelling during craniofacial morphogenesis and the aberrant expression or function of the enzyme could be involved in causing facial abnormalities.
authors.affiliation: Department of Odontology and Oral Pathology, Faculty of Dentistry, ChiangMai University, Thailand.
authors.forename: A
authors.initials: A
authors.lastname: Iamaroon
authors.forename: U M
authors.initials: UM
authors.lastname: Wallon
authors.forename: C M
authors.initials: CM
authors.lastname: Overall
authors.forename: V M
authors.initials: VM
authors.lastname: Diewert
mesh_terms: D000818:Animals; D001934:Branchial Region / Q000196:embryology / Q000201:enzymology; D004396:Coloring Agents; D003315:Cornea / Q000196:embryology / Q000201:enzymology; D004475:Ectoderm / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D004848:Epithelium / Q000196:embryology / Q000201:enzymology; D005109:Extracellular Matrix / Q000201:enzymology; D005123:Eye / Q000196:embryology / Q000201:enzymology; D005147:Facial Bones / Q000196:embryology* / Q000201:enzymology; D019084:Fluorescent Antibody Technique, Indirect; D018093:Gelatinases / Q000032:analysis / Q000235:genetics*; D015870:Gene Expression; D007908:Lens, Crystalline / Q000196:embryology / Q000201:enzymology; D008334:Mandible / Q000196:embryology; D020778:Matrix Metalloproteinase 2; D008437:Maxilla / Q000196:embryology / Q000201:enzymology; D008648:Mesoderm / Q000201:enzymology; D008666:Metalloendopeptidases / Q000032:analysis / Q000235:genetics*; D051379:Mice; D008815:Mice, Inbred Strains; D018613:Microscopy, Confocal; D009024:Morphogenesis / Q000235:genetics; D009666:Nose / Q000196:embryology / Q000201:enzymology; D012886:Skull / Q000196:embryology* / Q000201:enzymology
chemical_list: D004396:Coloring Agents; D018093:Gelatinases; D008666:Metalloendopeptidases; D020778:Matrix Metalloproteinase 2