Abstract
Affinity-purified antibodies produced intense staining for type I collagen in alveolar bone matrix and predentine, and moderate staining in the dentine matrix, lamina propria, connective tissue invaginating into papillary layer of the enamel organ, dental sac and periodontal ligament. No staining occurred in oral epithelium, stellate reticulum, stratum intermedium, ameloblasts and odontoblasts. Fibronectin was distributed similarly except at the interface between the epithelial diaphragm and pre-odontoblasts where type I collagen was absent but fibronectin was present. In contrast, type III collagen showed strong staining in the periodontal ligament and lamina propria but no staining in bone matrix, predentine, dentine and at the interface between the epithelial diaphragm and pre-odontoblasts. The staining pattern for type III collagen was similar to that of type I and fibronectin in other tissues including endosteal reticular tissue, the connective tissue invaginating into papillary layer and the extracellular matrix of the pulp.
| Original language | English |
|---|---|
| Pages (from-to) | 273-279 |
| Number of pages | 7 |
| Journal | Archives of Oral Biology |
| Volume | 32 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - Jan 1 1987 |
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All Science Journal Classification (ASJC) codes
- Otorhinolaryngology
- Dentistry(all)
- Cell Biology
Cite this
Immunofluorescence localization of type I and type III collagen and fibronectin in mouse dental tissues in late development and during molar eruption. / Takita, K.; Ohsaki, Yasuyoshi; Nakata, M.; Kurisu, K.
In: Archives of Oral Biology, Vol. 32, No. 4, 01.01.1987, p. 273-279.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Immunofluorescence localization of type I and type III collagen and fibronectin in mouse dental tissues in late development and during molar eruption
AU - Takita, K.
AU - Ohsaki, Yasuyoshi
AU - Nakata, M.
AU - Kurisu, K.
PY - 1987/1/1
Y1 - 1987/1/1
N2 - Affinity-purified antibodies produced intense staining for type I collagen in alveolar bone matrix and predentine, and moderate staining in the dentine matrix, lamina propria, connective tissue invaginating into papillary layer of the enamel organ, dental sac and periodontal ligament. No staining occurred in oral epithelium, stellate reticulum, stratum intermedium, ameloblasts and odontoblasts. Fibronectin was distributed similarly except at the interface between the epithelial diaphragm and pre-odontoblasts where type I collagen was absent but fibronectin was present. In contrast, type III collagen showed strong staining in the periodontal ligament and lamina propria but no staining in bone matrix, predentine, dentine and at the interface between the epithelial diaphragm and pre-odontoblasts. The staining pattern for type III collagen was similar to that of type I and fibronectin in other tissues including endosteal reticular tissue, the connective tissue invaginating into papillary layer and the extracellular matrix of the pulp.
AB - Affinity-purified antibodies produced intense staining for type I collagen in alveolar bone matrix and predentine, and moderate staining in the dentine matrix, lamina propria, connective tissue invaginating into papillary layer of the enamel organ, dental sac and periodontal ligament. No staining occurred in oral epithelium, stellate reticulum, stratum intermedium, ameloblasts and odontoblasts. Fibronectin was distributed similarly except at the interface between the epithelial diaphragm and pre-odontoblasts where type I collagen was absent but fibronectin was present. In contrast, type III collagen showed strong staining in the periodontal ligament and lamina propria but no staining in bone matrix, predentine, dentine and at the interface between the epithelial diaphragm and pre-odontoblasts. The staining pattern for type III collagen was similar to that of type I and fibronectin in other tissues including endosteal reticular tissue, the connective tissue invaginating into papillary layer and the extracellular matrix of the pulp.
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U2 - 10.1016/0003-9969(87)90021-5
DO - 10.1016/0003-9969(87)90021-5
M3 - Article
VL - 32
SP - 273
EP - 279
JO - Archives of Oral Biology
JF - Archives of Oral Biology
SN - 0003-9969
IS - 4
ER -