Mechanical Strain Increases Expression of Type XII Collagen in Murine Osteoblastic MC3T3-E1 Cells

Arai, Katsuhiko; Nagashima, Yuko; Takemoto, Taeko; Nishiyama, Toshio

doi:10.1247/csf.08025

Cited by 24 publications

(21 citation statements)

References 27 publications

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“…Transcriptional regulators of this region have not been identified. Interestingly, a different enhancer region appears to be required for activation of the murine Col12a1 gene by cyclic strain in osteoblasts, namely an AP1 site binding c-Jun and JunD after strain (Arai et al, 2008). Thus, static versus cyclic tensile strain seem to regulate the collagen XII gene via distinct signaling pathways.…”

Section: Expression: Regulation By Growth Factors and Mechanical Stressmentioning

confidence: 99%

Collagen XII: Protecting bone and muscle integrity by organizing collagen fibrils

Chiquet

Birk

Bönnemann

et al. 2014

The International Journal of Biochemistry & Cell Biology

129

105

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Collagen XII, largest member of the fibril-associated collagens with interrupted triple helix (FACIT) family, assembles from three identical α-chains encoded by the COL12A1 gene. The molecule consists of three threadlike N-terminal noncollagenous NC3 domains, joined by disulfide bonds and a short interrupted collagen triple helix towards the C-terminus. Splice variants differ considerably in size and properties: "small" collagen XIIB (220 kDa subunit) is similar to collagen XIV, whereas collagen XIIA (350 kDa) has a much larger NC3 domain carrying glycosaminoglycan chains. Collagen XII binds to collagen I-containing fibrils via its collagenous domain, whereas its large noncollagenous arms interact with other matrix proteins such as tenascin-X. In dense connective tissues and bone, collagen XII is thought to regulate organization and mechanical properties of collagen fibril bundles. Accordingly, recent findings show that collagen XII mutations cause Ehlers-Danlos/myopathy overlap syndrome associated with skeletal abnormalities and muscle weakness in mice and humans.

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Section: Expression: Regulation By Growth Factors and Mechanical Stressmentioning

confidence: 99%

Collagen XII: Protecting bone and muscle integrity by organizing collagen fibrils

Chiquet

Birk

Bönnemann

et al. 2014

The International Journal of Biochemistry & Cell Biology

129

105

View full text Add to dashboard Cite

show abstract

“…The expression and alternative splicing of type XII collagen is known to be regulated by mechanical loading in various cell, such as fibroblasts [139,140], trabecular meshwork cells [141], vascular endothelial cells [142] and osteoblasts [143], as well as PDL-derived cells [20,138]. The promoter activity of type XII collagen is directly stimulated by mechanical loading, thus suggesting the conservation of a stress-response element [143,144].…”

Section: Other Types Of Collagenmentioning

confidence: 99%

“…The promoter activity of type XII collagen is directly stimulated by mechanical loading, thus suggesting the conservation of a stress-response element [143,144]. Upregulation of type XII collagen occurs during orthodontic tooth movement in the cells on the tension side, where there is an abundance of mature collagen fibers [138].…”

Section: Other Types Of Collagenmentioning

confidence: 99%

Mechano-regulation of collagen biosynthesis in periodontal ligament

Kaku

Yamauchi

2014

Journal of Prosthodontic Research

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Purpose Periodontal ligament (PDL) plays critical roles in the development and maintenance of periodontium such as tooth eruption and dissipation of masticatory force. The mechanical properties of PDL are mainly derived from fibrillar type I collagen, the most abundant extracellular component. Study selection The biosynthesis of type I collagen is a long, complex process including a number of intra- and extracellular post-translational modifications. The final modification step is the formation of covalent intra- and intermolecular cross-links that provide collagen fibrils with stability and connectivity. Results It is now clear that collagen post-translational modifications are regulated by groups of specific enzymes and associated molecules in a tissue-specific manner; and these modifications appear to change in response to mechanical force. Conclusions This review focuses on the effect of mechanical loading on collagen biosynthesis and fibrillogenesis in PDL with emphasis on the post-translational modifications of collagens, which is an important molecular aspect to understand in the field of prosthetic dentistry.

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“…It was reported that the Col12a1 gene could be directly stimulated by mechanical forces in fibroblasts 13,14 and endothelial cells 15 as well as osteoblasts. 16 In the chicken, collagen XII is expressed in interfacial regions of the cornea, Bowman membrane, and DM until hatching, suggesting a major role in the integration of different corneal layers. 17 Collagen XIV expression is homogeneous during stromal development and decreases in the mature stroma, suggesting a major role for collagen XIV during initial stages of fibrillogenesis and early stromal development and compaction.…”

mentioning

confidence: 99%

Abnormal Corneal Endothelial Maturation in Collagen XII and XIV Null Mice

Hemmavanh

Koch

Birk

et al. 2013

Invest. Ophthalmol. Vis. Sci.

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PURPOSE. Maturation of the endothelium and the adjacent matrix was characterized in wildtype (WT) mice. The influence of FACIT collagen XII and XIV deficiency on the morphology, maturation, and function of the corneal endothelium was examined.METHODS. Analysis of the endothelium and Descemet's membrane (DM) was performed using transmission electron microscopy at postnatal day (P)4, P14, and P30 in WT, Col12a1 À/À , Col14a1, and Col12a1 À/À /Col14a1 À/À mice. Endothelial junctions were analyzed using ZO-1. The presence of endothelial-stromal communications was evaluated with phalloidin staining as well as electron microscopy. Finally, corneal thickness was assessed. RESULTS.A thin DM, clefts between endothelial cells and DM, and large ''vacuole-like'' structures were present in the endothelial cells of WT mice at P4 but not noted at P30. The endothelia of Col12a1À/À , and compound Col12a1À/À in the P30 cornea maintained the vacuole-like structures seen at P4. A mature endothelial junction pattern was delayed in the null corneas. Expression of ZO-1 in WT endothelia at P14 was diffuse and localized to the basolateral and apical cell membrane. At P30, staining was localized to intercellular junctions. ZO-1 reactivity was patchy in Col12a1À/À , and compound Col12a1 À/À /Col14a1 À/À corneas at P14 and P30. Stromal thickness was increased in P30 null corneas. Endothelial cell processes were demonstrated penetrating the DM and into the underlying stroma, throughout the entire endothelial layer in the P4 cornea.CONCLUSIONS. Collagen XII and XIV null mice demonstrate delayed endothelial maturation. The structural alterations suggest functional changes in endothelial function resulting in increased corneal thickness. Endothelial-stromal interactions suggest a pathway for signal transduction.

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Mechanical Strain Increases Expression of Type XII Collagen in Murine Osteoblastic MC3T3-E1 Cells

Cited by 24 publications

References 27 publications

Collagen XII: Protecting bone and muscle integrity by organizing collagen fibrils

Collagen XII: Protecting bone and muscle integrity by organizing collagen fibrils

Mechano-regulation of collagen biosynthesis in periodontal ligament

Abnormal Corneal Endothelial Maturation in Collagen XII and XIV Null Mice

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