Change of complement C1s synthesis during development of hamster cartilage

Toyoguchi, Toru; Yamaguchi, Kiichiro; Nakagawa, Kōichi; Fukusawa, Takeshi; Moriya, Hideshige; Sakiyama, Hisako

doi:10.1007/s004410050637

Cited by 17 publications

(14 citation statements)

References 20 publications

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“…In hamster articular cartilage, Cls is not detected by either immunostaining or in situ hybridization (Toyoguchi et al 1996). Consistent with these observations, normal human articular cartilage displayed no immunostaining with anti-Cls mAb PG11.…”

Section: Discussionsupporting

confidence: 81%

“…Degrading enzymes may play a major role in the cleaning mechanisms of cartilage. We have shown that Cls synthesis increases in accordance with chondrocyte differentiation both in vivo (Toyoguchi et al 1996) and in vitro (Nakagawa et al, 1997). Cls synthesized by chondrocytes as well as that delivered from the blood stream may participate in chondrocyte and matrix degradation.…”

Section: Introductionmentioning

confidence: 84%

“…Recently, however, we have demonstrated that Cls degrades type II collagen (Yamaguchi et al 1990), a major constituent of cartilage matrix and gelatin, and activates zymogen of matrix metalloproteinase 9 (MMP-9) (Sakiyama et al 1994). MMP-9 is known to be synthesized by chondrocytes in vivo (Toyoguchi et al 1996) and in vitro (Nakagawa et al, 1997), and colocalized with Cls at the primary ossification center of human femur (Sakiyama et al 1994). Therefore, Cls is thought to have a role in cartilage degradation.…”

Section: Introductionmentioning

confidence: 97%

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Complement Cls, a classical enzyme with novel functions at the endochondral ossification center: immunohistochemical staining of activated Cls with a neoantigen-specific antibody

Sakiyama¹,

Nakagawa²,

Kuriiwa³

et al. 1997

Cell and Tissue Research

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The secondary ossification center of 14- to 16-day-old hamster tibiae was examined immunohistochemically with active and inactive Cls-specific antibodies, RK5 and RK4, respectively. At the ossification center, chondrocytes differentiate from proliferating and hypertrophic to degenerating stages, and their site is occupied by the bone marrow. Cls was strongly immunostained in hypertrophic chondrocytes. In order to discover whether Cls is activated at a particular site, the cartilage was immunostained with RK5 and RK4. RK5 mainly reacted with degrading matrix around invading vessels. In contrast, RK4 strongly stained hypertrophic chondrocytes. Immunoelectron microscopy revealed Cls on degrading fragments of chondrocytes and fibers of cartilage matrix. Decorin, one of the major matrix proteoglycans, was dose and time dependently degraded by Cls. Type II collagen and type I gelatin were also degraded. Articular cartilage from patients with rheumatoid arthritis was positively immunostained (11/12 cases) with an anti-Cls monoclonal antibody (mAb) PG11, whereas normal articular cartilage (5/5 cases) was negative, suggesting Cls participation in the etiology of rheumatoid arthritis.

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Section: Discussionsupporting

confidence: 81%

Section: Introductionmentioning

confidence: 84%

Section: Introductionmentioning

confidence: 97%

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Complement Cls, a classical enzyme with novel functions at the endochondral ossification center: immunohistochemical staining of activated Cls with a neoantigen-specific antibody

Sakiyama¹,

Nakagawa²,

Kuriiwa³

et al. 1997

Cell and Tissue Research

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“…However, C1s gene expression has been found in most other tissues, including brain, kidney, stomach, and muscle (Kusumoto et al 1988;Sakiyama et al 1991), and in several types of cultured cells, such as monocytes (Bensa et al 1983), endothelial cells (Morris et al 1978), and fibroblasts (Kats and Strunk 1989). By immunostaining (Sakiyama et al 1991 and in situ hybridization (Toyoguchi et al 1996), we have shown that C1s is also synthesized by chondrocytes and that the synthesis increases in accordance with chondrocyte hypertrophy. Since C1s degrades types I, II, and IV collagen and gelatin (Sakiyama et al 1989;Yamaguchi et al 1990) and activates the zymogen of matrix metalloproteinase 9 , C1s is thought to participate in cartilage degradation.…”

Section: Introductionmentioning

confidence: 86%

Coordinated change between complement C1s production and chondrocyte differentiation in vitro

Nakagawa¹,

Sakiyama²,

Fukazawa³

et al. 1997

Cell and Tissue Research

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In vitro synthesis of the first component of complement C1s was examined by using hamster epiphyseal chondrocytes (HAC) and human chondrosarcoma cell line HCS-2/8. Hamster and human C1s produced by the cells were quantified by immunoblotting and sandwich enzyme-linked immunosorbent assay (ELISA), respectively. It was possible to measure active and inactive C1s by sandwich ELISA, when we used anti-human C1s monoclonal antibodies, M241 recognizing only active C1s, and M365 and M81 recognizing both active and inactive C1s. Approximately 40% of C1s secreted from HCS-2/8 was found to be activated in the culture medium, whereas C1s from HAC was not. C1s production increased in accordance with chondrocyte differentiation induced by ascorbic acid. In contrast, transforming growth factor-beta1 and basic fibroblast growth factor, which inhibited differentiation, suppressed C1s production. These results confirmed our previous observation showing that C1s synthesis increased with differentiation into hypertrophic chondrocytes in vivo.

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“…Although osteoimmunology is gaining interest, not much is known about the role of the complement system in the growth plate 40. The complement system, and more specifically C1, seems to contribute to the turnover of cartilage into bone during endochondral ossification because several studies have shown that C1 is present in epiphyseal cartilage41 and ossification centers 42. How these systems affect chondrocyte proliferation and hypertrophy and facilitate differences in longitudinal growth and final height remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

Growth plate expression profiling: Large and small breed dogs provide new insights in endochondral bone formation

Teunissen

Riemers

Leenen

et al. 2017

Journal Orthopaedic Research

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The difference in the adult height of mammals, and hence in endochondral bone formation, is not yet fully understood and may serve to identify targets for bone and cartilage regeneration. In line with this hypothesis, the intra‐species disparity between the adult height of Great Danes and Miniature Poodles was investigated at a transcriptional level. Microarray analysis of the growth plate of five Great Danes and five Miniature Poodles revealed 2,981 unique genes that were differentially expressed, including many genes with an unknown role in skeletal development. A signaling pathway impact analysis indicated activation of the cell cycle, extracellular matrix receptor interaction and the tight junction pathway, and inhibition of pathways associated with inflammation and the complement cascade. In additional validation steps, the gene expression profile of the separate growth plate zones for both dog breeds were determined. Given that the BMP signaling is known for its crucial role in skeletal development and fracture healing, and BMP‐2 is used in orthopaedic and spine procedures for bone augmentation, further investigations concentrated on the BMP pathway.The canonical BMP‐2 and BMP‐6 signaling pathway was activated in the Great Danes compared to Miniature Poodles. In conclusion, investigating the differential expression of genes involved in endochondral bone formation in small and large breed dogs, could be a game changing strategy to provide new insights in growth plate development and identify new targets for bone and cartilage regeneration. © 2017 The Authors. Journal of Orthopaedic Research® published by Wiley Periodicals, Inc. on behalf of the Orthopaedic Research Society. J Orthop Res 36:138–148, 2018.

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Change of complement C1s synthesis during development of hamster cartilage

Cited by 17 publications

References 20 publications

Complement Cls, a classical enzyme with novel functions at the endochondral ossification center: immunohistochemical staining of activated Cls with a neoantigen-specific antibody

Complement Cls, a classical enzyme with novel functions at the endochondral ossification center: immunohistochemical staining of activated Cls with a neoantigen-specific antibody

Coordinated change between complement C1s production and chondrocyte differentiation in vitro

Growth plate expression profiling: Large and small breed dogs provide new insights in endochondral bone formation

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