Age-related changes in the localization of glycosaminoglycans in condylar cartilage of the mandible in rats

Takahashi, Ichiro; Mizoguchi, Itaru; Sasano, Yasuyuki; Saitoh, S.; Ishida, Mamoru; Kagayama, Manabu; Mitani, Hideo

doi:10.1007/bf00185995

Cited by 18 publications

(19 citation statements)

References 24 publications

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“…According to previous reports, the localization of collagen types I, II and X and GAGs is a well-established marker for the degree of chondrogenic differentiation in primary cartilage (von der Mark et al, 1976;von der Mark, 1980;Silbermann et al, 1987;Takahashi et al, 1996b). The localization of both collagens and GAGs also reflects the morphological stage of chondrogenesis during the development of secondary cartilage (Mizoguchi et al, 1990;Ohashi et al 1997;Takahashi et al, 1996b). Although the extracellular collagenous components of primary cartilage show temporal changes during the developmental stage, secondary cartilage has an undifferentiated proliferative cell layer and a differentiating transitional cell layer that includes type I collagen as the ECM and osteo-chondro progenitor cells as a cell source for subsequent chondrogenesis.…”

Section: Discussion Experimental Proceduresmentioning

confidence: 99%

“…The majority of the experimental procedures were identical to those mentioned above for collagen immunohistochemistry and were described in our previous study (Takahashi et al, 1996b). The sections were incubated with chondroitinase ABC or chondroitinase ACII (Seikagakukogyo, Tokyo, Japan) in a moisture chamber for 60 min at 37°C, instead of hyaluronidase as described above.…”

Section: Immunohistochemical Staining For Gagsmentioning

confidence: 99%

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Compressive force promotes chondrogenic differentiation and hypertrophy in midpalatal suture cartilage in growing rats

et al. 2000

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Section: Discussion Experimental Proceduresmentioning

confidence: 99%

Section: Immunohistochemical Staining For Gagsmentioning

confidence: 99%

Compressive force promotes chondrogenic differentiation and hypertrophy in midpalatal suture cartilage in growing rats

et al. 2000

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“…Colocalization of GAGs and mineralization has been detected histologically in calcifying tissue, [12][13][14] and importantly there is accumulating evidence that the type of GAG in the matrix may exert tight control over mineralization, particularly during its initiation. 15,16 An early event in bone mineralization is release of membrane-bound matrix vesicles which act as the nidus for mineral nucleation by concentrating calcium and phosphate. Matrix vesicles bind GAGs, and this binding is increased in mineralization-competent hypertrophic chondrocyte-derived matrix vesicles, further suggesting that GAGs play a direct role in initiating physiological mineralization.…”

Section: Discussionmentioning

confidence: 99%

Mineral Surface in Calcified Plaque Is Like That of Bone

Duer

Friščić

Proudfoot

et al. 2008

ATVB

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Objectives-Cell biological studies demonstrate remarkable similarities between mineralization processes in bone and vasculature, but knowledge of the components acting to initiate mineralization in atherosclerosis is limited. The molecular level microenvironment at the organic-inorganic interface holds a record of the mechanisms controlling mineral nucleation. This study was undertaken to compare the poorly understood interface in mineralized plaque with that of bone, which is considerably better characterized. Methods and Results-Solid state nuclear magnetic resonance (SSNMR) spectroscopy provides powerful tools for studying the organic-inorganic interface in calcium phosphate biominerals. The rotational echo double resonance (REDOR) technique, applied to calcified human plaque, shows that this interface predominantly comprises sugars, most likely glycosaminoglycans (GAGs). In this respect, and in the pattern of secondary effects seen to protein (mainly collagen), calcified plaque strongly resembles bone. Conclusion-The similarity between biomineral formed under highly controlled (bone) and pathological (plaque) conditions suggests that the control mechanisms are more similar than previously thought, and may be adaptive. It is strong further evidence for regulation of plaque mineralization by osteo/chondrocytic vascular smooth muscle cells. Key Words: atherosclerosis Ⅲ biomineralization Ⅲ glycosaminoglycans Ⅲ nuclear magnetic resonance spectroscopy Ⅲ vascular calcification C alcification 1 is prevalent in numerous vascular pathologies and is associated with adverse clinical outcomes. Parallels have frequently been drawn between ectopic calcification processes in vessels and normal developmental osteogenesis. In fact vascular calcified material is by many criteria indistinguishable from bone, and its formation involves the participation of many cellular and molecular signaling processes underlying normal osteogenesis. 2 These include matrix vesicle release, expression of mineralizationregulating proteins by vascular smooth muscle cells (VSMCs) of the vessel wall, and the association of calcification with lipid and chronic inflammation, a hallmark of atherosclerosis. 3 Indeed vascular calcification is recognized as regulated biomineralization instead of merely passive precipitation. However questions are still unanswered concerning the mechanisms leading to the initiation of calcification in the vessel wall particularly as it occurs in different vascular environments (ie, media and intima), which do not mimic that of bone. Moreover, VSMCs can overexpress mineralization inhibitors such as matrix Gla protein (MGP) to effectively block mineralization. 4 Aspects of the molecular structure of mineralized tissues 5 can be studied by the solid state NMR (SSNMR) technique 13 C{ 31 P} rotational echo double resonance (REDOR). 6 13 C is a stable, nonradioactive, NMR-receptive isotope of carbon occurring naturally at about 1.1% abundance; similarly 31 P is a stable NMR-receptive isotope of phosphorus which however is natu...

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“…While mandibular condylar cartilage has been shown to have Wve distinct layers, primary cartilages, including growth plate and articular cartilage, is composed of four layers during the growth period (Luder et al 1988;Mizoguchi et al 1992). Primary cartilage cells express both type II collagen and aggrecan, cartilage-speciWc ECM components; however, cells in the upper two layers of mandibular condylar cartilage do not express either of these molecules (Mizoguchi et al 1992;Takahashi et al 1996;Shibata et al 2001). Proliferating cells in growth plate and articular cartilage are well-diVerentiated chondrocytes, but those in mandibular condylar cartilage are not (Mizoguchi et al 1992).…”

Section: Introductionmentioning

confidence: 99%

Comparison of age-dependent expression of aggrecan and ADAMTSs in mandibular condylar cartilage, tibial growth plate, and articular cartilage in rats

Takahashi

Onodera

Bae

et al. 2006

Histochem Cell Biol

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A disintegrin and metalloproteinase with thrombospondin motif (adamalysin-thrombospondins, ADAMTS) degrades aggrecan, one of the major extracellular matrix (ECM) components in cartilage. Mandibular condylar cartilage differs from primary cartilage, such as articular and growth plate cartilage, in its metabolism of ECM, proliferation, and differentiation. Mandibular condylar cartilage acts as both articular and growth plate cartilage in the growing period, while it remains as articular cartilage after growth. We hypothesized that functional and ECM differences between condylar and primary cartilages give rise to differences in gene expression patterns and levels of aggrecan and ADAMTS-1, -4, and -5 during growth and aging. We employed in situ hybridization and semiquantitative RT-PCR to identify mRNA expression for these molecules in condylar cartilage and primary cartilages during growth and aging. All of the ADAMTSs presented characteristic, age-dependent expression patterns and levels among the cartilages tested in this study. ADAMTS-5 mainly contributed to ECM metabolism in growth plate and condylar cartilage during growth. ADAMTS-1 and ADAMTS-4 may be involved in ECM turn over in articular cartilage. The results of the present study reveal that ECM metabolism and expression of related proteolytic enzymes in primary and secondary cartilages may be differentially regulated during growth and aging.

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Age-related changes in the localization of glycosaminoglycans in condylar cartilage of the mandible in rats

Cited by 18 publications

References 24 publications

Compressive force promotes chondrogenic differentiation and hypertrophy in midpalatal suture cartilage in growing rats

Compressive force promotes chondrogenic differentiation and hypertrophy in midpalatal suture cartilage in growing rats

Mineral Surface in Calcified Plaque Is Like That of Bone

Comparison of age-dependent expression of aggrecan and ADAMTSs in mandibular condylar cartilage, tibial growth plate, and articular cartilage in rats

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