The distribution of type I, III, IV and V collagen in 35 gliomas and 20 meningiomas was studied by indirect immunofluorescence staining. In addition, the presence of fibronectin (FN) and laminin (LN) is also reported. In gliomas expression of type IV collagen and LN was found in the vessel walls and associated with the endothelial glomerulus-like proliferations. FN and type V collagens were located in proliferating vessel walls in a pattern corresponding both to the basement membrane and the perivascular matrix around the vessels. In the extracellular matrix of grade III and IV gliomas occasional faint intercellular fluorescence was also observed with both FN and type V collagen. Type I and III collagens were localised in the vessel walls and in the perivascular connective sheet. Glioma cells did not express any of the antigens investigated. In meningiomas, type IV and V collagens, LN and FN were found in vessel walls, whorls formations and psammoma bodies. These stainings support the hypothesis of a vascular origin of these psammoma bodies which were only found in syncytial and transitional meningiomas. Both type I and III collagens were detected in the perivascular connective tissue. In general, meningioma cells and extracellular matrix did not express any of these molecules, except in transitional meningiomas where occasional fluorescence was observed in extracellular matrix with type V collagen and FN.

The gene expression and protein distribution of matrix metalloproteinase (MMP) -2, -9, membrane type-1 MMP (MT1-MMP), as well as of TIMP-1, -2, and -3 were analyzed during mouse molar development. Immunohistochemical data demonstrated that all the MMPs investigated were expressed in the dental epithelium and mesenchyme. In contrast, gene and protein expression analysis for TIMPs showed that they were differentially expressed. TIMP-1 was expressed in the dental epithelium and mesenchyme between E13 and E16 and was transiently up-regulated at E14, the cap stage. TIMP-1 expression was also detected in differentiating odontoblasts. TIMP-2 RNA transcripts were found in the peridental and dental mesenchyme, odontoblasts, and ameloblasts. Protein analysis revealed high expression on the lingual side of the dental epithelium and underlying mesenchyme together with transient expression in the enamel knot at E14 and expression in the gingival tissue and enamel matrix postnatally. TIMP-3 RNA transcripts were found in discrete regions of the dental epithelium, including at high levels in the cervical loop at E16. Expression was also detected in preodontoblasts at E16 and transiently during ameloblast differentiation. Analysis of the protein distribution revealed a lower level of TIMP-3 on the lingual side of the dental epithelium at E14. MT1-MMP was expressed in the dental mesenchyme between E13 and E16, at relatively high levels in the cervical loop at E14, and in the odontoblasts and ameloblasts. The distinct temporospatial distribution patterns of the TIMPs suggest that these inhibitors play several intrinsic roles during tooth development. Developmental Dynamics 228:105-112, 2003.

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