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  • 1
    Electronic Resource
    Electronic Resource
    Presence of chondroid bone on rat mandibular condylar cartilage (1993)
    Springer
    Anatomy and embryology 187 (1993), S. 9-15 
    Details
    ISSN: 1432-0568
    Keywords: Chondroid bone ; Collagen ; Immunohistochemistry ; Mandibular condylar cartilage ; Secondary cartilage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Immunohistochemical techniques were used to examine the locations of type I and type II collagens in the the most anterior and the posterosuperior regions of the mandibular condylar cartilages of young and adult rats. Large ovoid and polygonal cells, which were morphologically different from any of the neighboring cells, e.g., mature or hypertrophied chondrocytes, osteoblasts, or fibroblasts, were observed at the most anterior margin of the young and adult condylar cartilages. In the extracellular matrix (ECM) of this area, an eosinophilic staining pattern similar to that in bone matrix was observed, while the peripheral ECM showed basophilic staining and very weak reactivity to Alcian blue. Immunohistochemical examination showed that the ECM was stained heavily and diffusely for type I collagen, while a staining for type II collagen was faint and limited to the peripheral ECM. Two different staining patterns for type II collagen could be recognized in the ECM: one pattern revealed a very faint and diffuse reaction while the other showed a weak rim-like reaction. These staining patterns were markedly different from those in the cartilaginous cell layer in the posterosuperior area of the condylar secondary cartilage, which showed faint staining for type I collagen and a much more intense staining for type II collagen. These observations reveal the presence of chondroid bone, a tissue intermediate between bone and cartilage tissues, in the mandibular condylar cartilage, and suggest the possibility of osteogenic transdifferentiation of mature chondrocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00208192
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  • 2
    Electronic Resource
    Electronic Resource
    Chondrocytes synthesize type I collagen and accumulate the protein in the matrix during development of rat tibial articular cartilage (1996)
    Springer
    Anatomy and embryology 194 (1996), S. 247-252 
    Details
    ISSN: 1432-0568
    Keywords: Articular cartilage ; Development ; Type I collagen ; In situ hybridization ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The present study was designed to investigate whether or not chondrocytes in articular cartilage express type I collagen in vivo under physiological conditions. Expressions of the gene and the phenotype of type I collagen were examined in rat tibial articular cartilage in the knee joint during development. Knee joints of Wistar rats at 1, 5, and 11 weeks postnatal were fixed in 4% paraformaldehyde with or without 0.5% glutaraldehyde and decalcified in 10% EDTA. After the specimens were embedded in paraffin and serial sections made, adjacent sections were processed for immunohistochemistry and in situ hybridization for type I collagen. The epiphysis of the tibia was composed of cartilage in week-1 rats. Formation of articular cartilage was in progress in week 5 as endochondral ossification proceeded and was completed in week 11. Anti-type I collagen antibody stained only the superficial area of the epiphysis in week 1, but the immunoreactivity was expanded into the deeper region of the articular cartilage with development in weeks 5 and 11. Hybridization signals for pro-alpha 1 (I) collagen were seen in some of chondrocytes in the epiphysis of the week-1 tibia. The most intense signals were identified in chondrocytes in week 5 and the signals appeared weaker in week 11. The present study demonstrated that chondrocytes synthesize type I collagen and accumulate the protein in the matrix during development of the articular cartilage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00187135
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  • 3
    Electronic Resource
    Electronic Resource
    Type X collagen is not localized in hypertrophic or calcified cartilage in the developing rat trachea (1998)
    Springer
    Anatomy and embryology 197 (1998), S. 399-403 
    Details
    ISSN: 1432-0568
    Keywords: Key words Immunohistochemistry ; Permanent cartilage ; Calcification ; von Kossa staining ; Endochondral ossification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Our previous studies have shown that rat tracheal chondrocytes become larger and hypertrophic, and that the cartilage matrix calcifies during development. Type X collagen is a short collagen molecule identified in hypertrophic and calcified cartilage in the growth plate of long bones during endochondral ossification. The present study was designed to investigate the distribution of type X collagen in rat tracheal cartilage during development before and after hypertrophization and calcification. Tracheas from postnatal Wistar rats, newborn, and at 4, 8 and 10 weeks were fixed along with hind limbs from newborn rats. Serial sections were made and adjacent sections were processed for von Kossa staining or immunohistochemistry for type X collagen. In addition, the immunoreactivity to type II collagen was examined as a control. The anti-type X collagen antibody stained hypertrophic and/or calcified cartilage in the newborn rat tibia. The immunoreaction for type X collagen was localized in the uncalcified peripheral region of tracheal cartilage in 4, 8 and 10-week-old rats. In contrast, the anti-type X collagen antibody did not show immunoreactivity to hypertrophic or calcified cartilage in the central region of the 10-week-old rat tracheal cartilage. The present study has suggested that type X collagen is not involved in hypertrophization of chondrocytes or calcification of the matrix in developing rat tracheal cartilage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004290050151
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  • 4
    Electronic Resource
    Electronic Resource
    Distribution of type I collagen, type II collagen and PNA binding glycoconjugates during chondrogenesis of three distinct embryonic cartilages (1992)
    Springer
    Anatomy and embryology 186 (1992), S. 205-213 
    Details
    ISSN: 1432-0568
    Keywords: Chondrogenesis ; Meckel's cartilage ; Limb bud ; Nasal septum ; Collagen ; PNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Previous studies of chondrogenesis have been focused on limb bud cartilage, whereas little is known about chondrogenic processes of other cartilages with different developmental fates. We hypothesize that cartilages with various developmental fates might show identical characteristics of chondrogenesis. The chondrogenic processes in the nasal septum, the mandible, and the limb bud of the mouse were examined by means of PNA-binding glycoconjugate, and types I and II collagen expression. Swiss-Webster mouse embryos of 11 days (E11) to 14 days (E14) gestation were fixed and processed for imniuno- and lectin histochemistry. The blastema of mesenchymal cell aggregates stained positively with anti-type I collagen, but very weakly with anti-type II collagen in all three models at E12, whereas PNA bound to the blastema in the limb bud but not in nasal septum or mandible. Types I and II collagens coexisted in cartilages at E13. Type II collagen was predominant in E14; type I collagen was confined to the peripheral region. The synchronized transitional expression of the collagen phenotypes in all three embryonic cartilages may be systemically regulated. The presence or absence of the PNA-binding glycoconjugates may be involved in characterizing the nature of the cartilages.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00174142
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  • 5
    Electronic Resource
    Electronic Resource
    Confocal microscopy of cementocytes and their lacunae and canaliculi in rat molars (1997)
    Springer
    Anatomy and embryology 195 (1997), S. 491-496 
    Details
    ISSN: 1432-0568
    Keywords: Key words Cementum and bone ; FITC-phalloidin ; Actin filaments ; Alizarin red ; Secondary calcification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The present study was designed to analyze the morphological characteristics of cementocytes and osteocytes. The maxillae of 10-week-old Wistar rats were used for observations. Non-decalcified ground sections stained vitally with fluorescence dyes and decalcified frozen sections stained with FITC-phalloidin were examined by confocal microscopy. Calcein and alizarin red stained the calcification front of bone, cementum, and dentin intensely. In addition, lacunae and canaliculi of cementocytes and osteocytes as well as dentinal canals were stained with the fluorescent dyes. The staining of lacunae and canaliculi was less intense than that of the calcification front of bone, cementum and dentin. The canaliculi of cementocytes and osteocytes were connected with the canaliculi extending from the calcification front of cementum and bone, respectively. The canalicular density was less in the cellular cementum than in the bone. Areas devoid of canaliculi were numerous in the cellular cementum, whereas areas devoid of canaliculi were scarce in the alveolar bone. Further, the lacunae of cementocytes showed various shapes, from oval to tubular, while the lacunae of osteocytes were invariably oval. The cell body and the cytoplasmic processes of cementocytes were positive for FITC-phalloidin within the extracellular matrix of cellular cementum, which was negative. The distribution of actin filaments in the osteocytes and the cementocytes was predominantly cortical and appeared to be closely associated with the cell membrane of the cell bodies and the cytoplasmic processes. Intense staining was seen at the proximal part of the cytoplasmic processes in both osteocytes and cementocytes, showing a punctuated structure of the cells that was more frequent in osteocytes than in cementocytes. The stress fiber known to be present in most of the cultured cells was not evident in the these cells in situ. The cells incorporated in the cementodentinal junction were strongly stained with FITC-phalloidin. The distribution pattern of the cytoplasmic processes stained with FITC-phalloidin was similar to that of the canaliculli stained vitally. The cytoplasmic processes of osteocytes and cementocytes were connected with those of cells lining the surface of bone and cementum. The present result – that lacunae and canaliculi of cementocytes were stained vitally with the fluorescence dyes – suggests that cementocytes may have a role in secondary calcification of cellular cementum. Further, the lower density of cytoplasmic processes in cementocytes than in osteocytes suggests a lack of complexity in the intercellular network within the cellular cementum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004290050068
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  • 6
    Electronic Resource
    Electronic Resource
    Expression of major bone extracellular matrix proteins during embryonic osteogenesis in rat mandibles (2000)
    Springer
    Anatomy and embryology 202 (2000), S. 31-37 
    Details
    ISSN: 1432-0568
    Keywords: Key words Bone ; Calcification ; Type I collagen ; Noncollagenous proteins ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  It is not known how bone proteins appear in the matrix before and after calcification during embryonic osteogenesis. The present study was designed to investigate expressions of the five major bone extracellular matrix proteins – i.e. type I collagen, osteonectin, osteopontin, bone sialoprotein and osteocalcin – during osteogenesis in rat embryonic mandibles immunohistochemically, and their involvement in calcification demonstrated by von Kossa staining. Wistar rat embryos 14 to 18 days post coitum were used. Osteogenesis was not seen in 14-day rat embryonic mandibles. Type I collagen was localized in the uncalcifed bone matrix in 15-day mandibles, where no other bone proteins showed immunoreactivity. Osteonectin, osteopontin, bone sialoprotein and osteocalcin appeared almost simultaneously in the calcified bone matrix of 16-day mandibles and accumulated continuously in 18-day mandibles. The present study suggested that type I collagen constitutes the basic framework of the bone matrix upon which the noncollagenous proteins are oriented to lead to calcification, whereas the noncollagenous proteins are deposited simultaneously by osteoblasts and are involved in calcification cooperatively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00008242
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  • 7
    Electronic Resource
    Electronic Resource
    The process of calcification during development of the rat tracheal cartilage characterized by distribution of alkaline phosphatase activity and immunolocalization of types I and II collagens and glycosaminoglycans of proteoglycans (1993)
    Springer
    Anatomy and embryology 188 (1993), S. 31-39 
    Details
    ISSN: 1432-0568
    Keywords: Tracheal cartilage ; Development ; Calcification ; Alkaline phosphatase ; Collagen ; Proteoglycan
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The rat tracheal cartilage was shown to calcify during development. The process of calcification was characterized in terms of distribution of alkaline phosphatase (ALP) activity and alterations to immunolocalization of types I and II collagens and glycosaminoglycans of proteoglycans during the development of the tracheal cartilage, in comparison with calcification of the epiphyseal growth plate cartilage. ALP activity was not identified in the tracheal cartilage in the course of calcification, which therefore differed from that in the growth plate. The tracheal cartilage matrix was not resorbed or invaded by type I collagen during calcification. This suggests that no osteogenesis is involved in calcification of the cartilage. Immunoreactivity for type II collagen became weaker in the central region of the tracheal cartilage during development. No net loss of proteoglycans was identified with Alcian blue staining after calcification of the tracheal cartilage. Immunoreactivity for chondroitin 4-sulphate increased in the calcified tracheal cartilage, while reactivity for chondroitin 6-sulphate was weaker in the calcified area than in the surrounding uncalcified region of the tracheal cartilage. The alteration of the extracellular matrices during development may be involved in the calcification of the rat tracheal cartilage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00191449
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  • 8
    Electronic Resource
    Electronic Resource
    Immunohistochemical Localization of Type I Collagen, Fibronectin and Tenascin C During Embryonic Osteogenesis in the Dentary of Mandibles and Tibias in Rats (2000)
    Springer
    Journal of molecular histology 32 (2000), S. 591-598 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Type I collagen, fibronectin and tenascin C play an important role in regulating early osteoblast differentiation, but the temporal and spatial relationship of their localization during embryonic osteogenesis in vivo is not known. The present study was designed to localize these three molecules in the dentary of mandibles and tibias in rat embryos using immunohistochemistry. Serial paraffin sections were cut and adjacent sections were processed for von Kossa staining or immunohistochemistry for type I collagen, fibronectin and tenascin C. In the dentary, tenascin C was localized within and around the mesenchymal cell condensation in embryos at 14 days in utero. The bone matrix at 15 days showed immunoreactivity for both type I collagen and fibronectin. The immunoreactivity of type I collagen was persistent, whereas that of fibronectin decreased with age of embryos. In tibias, tenascin C was localized in the perichondral mesenchymal tissue at 17 days. Immunoreactivity for type I collagen was persistent in the bone matrix, whereas the tibial bone showed little immunoreactivity for fibronectin at any embryonic age examined. The present study demonstrated characteristic localization of type I collagen, fibronectin and tenascin C during embryonic osteogenesis in the dentary of mandibles and tibias.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026720003564
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  • 9
    Electronic Resource
    Electronic Resource
    Subperiosteal lmplantation of octacalcium phosphate (OCP) stimulates both chondrogenesis and osteogenesis in the tibia, but only osteogenesis in the parietal bone of a rat (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 242 (1995), S. 40-46 
    Details
    ISSN: 0003-276X
    Keywords: Octacalcium phosphate ; Implantation ; Long bone ; Calvarium ; Osteogenesis ; Chondrogenesis ; Type I collagen ; Type II collagen ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Background: It is not known whether long bones and calvaria have distinct biological characteristics. Octacalcium phosphate (OCP), which is a precursor phase of the hydroxyapatite, has been reported to stimulate bone formation if implanted in the subperiosteal region of mouse calvaria. The present study was designed to investigate how the long bone and the calvarium respond to OCP implantation and to compare their biological characteristics.Methods: The synthetic OCP was implanted into the subperiosteal region of rat tibiae and parietal bones being mixed with bovine type I collagen treated by pepsin (Atelocollagen). The biological response was examined histologically and immunohistochemically for collagen matrix phenotypes of types I and II to identify bone and cartilage formation.Results: Both chondrogenesis and osteogenesis were initiated in the tibia 1 week after implantation of OCP and most of the cartilage was replaced by bone at week 2. However, the parietal bone did not show osteogenesis responding to OCP implantation until week 3, and no cartilage formation was associated with the osteogenesis.Conclusions: The present study demonstrated the distinct characteristics of biological response to OCP implantation between the long bone and the calvarium in terms of whether or not cartilage formation is involved in the stimulated osteogenesis by OCP, and in terms of timing of the stimulated chondrogenesis and/or osteogenesis, i.e., the parietal bone takes more time to respond to OCP implantation than the tibia. © 1995 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092420106
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  • 10
    Electronic Resource
    Electronic Resource
    Effects of lateral pterygoid muscle hyperactivity on differentiation of mandibular condyles in rats (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 241 (1995), S. 328-336 
    Details
    ISSN: 0003-276X
    Keywords: Mandibular condylar cartilage ; Lateral pterygoid muscle ; Electrical stimulation ; Biomechanical force ; Type I collagen ; Type II collagen ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Background: The effects of biomechanical stress on the growth and development of the mandibular condyle have been studied by many investigators. However, the role of the lateral pterygoid muscle in this development is not clear.Methods: Hyperfunction of the lateral pterygoid muscles of male 3-weekold Sprague-Dawley rats was induced by electrical stimulation, and the responses of the mandibular condyles were compared to control tissues by a double-fluorescent staining technique using polyclonal antibodies against type I and type II collagen. Electrical stimulation consisted of repeated application (5 seconds on/5 seconds off) of a Hz current for up to 7 days.Results: In the first 2 days, cartilaginous tissues rich in type II collagen disappeared in the anterior and posterior areas, which were loaded by tensional force due to direct and indirect attachment of the lateral pterygoid muscles. Tissues in these areas were replaced by intramembranous bone that was reactive for type I collagen at 7 days. By the end of the experiment, the trabecula of the condyle was remodled more perpendicularly, thus resisting the compressive force due to hyperfunction of the lateral pterygoid muscles.Conclusions: These results suggest that the activity of the lateral pterygoid muscle might play a significant role in the differentiation of progenitor cells and in the maturation and calcification of chondrocytes in mandibular condyles. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092410306
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