An in situ hybridization and histochemical study of development and postnatal changes of mouse mandibular angular cartilage compared with condylar cartilage.
To investigate the origin and postnatal changes of mouse mandibular angular cartilage, in situ hybridization for cartilaginous marker proteins, histochemistry for alkaline phosphatase (ALP) and tartrate-resistant acid phosphatase (TRAP), and bromodeoxyuridine (BrDU) analyses were performed. Chondrocytes of the mandibular angular cartilage were derived from ALP-positive progenitor cells and first detected at embryonic day (E) 15.5. Newly formed chondrocytes rapidly differentiated into hypertrophic chondrocytes and hypertrophic cell zone rapidly extended in subsequent a few days. During this period, bone sialoprotein mRNA was more widely expressed than osteopontin mRNA in cartilage. Endochondral bone formation started at E 17.5 with the resorption of the bone collar by osteoclasts. These characteristics were consistent with those of the condylar cartilage, although developmental process was 0.5-1.5 day delayed relative to the condylar cartilage. During the postnatal period, contrast to the condylar cartilage, the angular cartilage constantly decreased in volume with advancing age. Reduction of proliferating activity estimated by BrDU incorporation accounts for this phenomenon. We demonstrate new structural features of the mandibular angular cartilage that may contribute to a coming research for the secondary cartilage.
Shibata
Shunichi
S
Maxillofacial Anatomy, Department of Maxillofacial Biology, Graduate School, Tokyo Medical and Dental University, Japan. S.Shibata.mfa@tmd.ac.jp
Fujimori
Tatsuya
T
Yamashita
Yasuo
Y
D053674:Aggrecans; D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry / Q000196:embryology* / Q000254:growth & development*; D049109:Cell Proliferation; D019902:Chondrocytes / Q000737:chemistry*; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis; D024043:Collagen Type II / Q000032:analysis; D024121:Collagen Type X / Q000032:analysis; D016326:Extracellular Matrix Proteins / Q000032:analysis; D006651:Histocytochemistry; D017403:In Situ Hybridization; D058574:Integrin-Binding Sialoprotein; D037181:Lectins, C-Type / Q000032:analysis; D008334:Mandible / Q000033:anatomy & histology*; D008335:Mandibular Condyle / Q000033:anatomy & histology; D051379:Mice; D008813:Mice, Inbred ICR; D053495:Osteopontin; D012333:RNA, Messenger / Q000032:analysis; D012795:Sialoglycoproteins / Q000032:analysis
C508320:Acan protein, mouse; D053674:Aggrecans; D011508:Chondroitin Sulfate Proteoglycans; D024043:Collagen Type II; D024121:Collagen Type X; D016326:Extracellular Matrix Proteins; C546872:Ibsp protein, mouse; D058574:Integrin-Binding Sialoprotein; D037181:Lectins, C-Type; D012333:RNA, Messenger; D012795:Sialoglycoproteins; C506896:Spp1 protein, mouse; D053495:Osteopontin