The role of the SIBLING, Bone Sialoprotein in skeletal biology — Contribution of mouse experimental genetics

Bouleftour, Wafa; Juignet, Laura; Bouet, Guénaëlle; Granito, Renata Neves; Vanden‐Bossche, Arnaud; Laroche, Norbert; Aubin, Jane E.; Lafage-Proust, Marie-Hélène; Vico, Laurence; Malaval, Luc

doi:10.1016/j.matbio.2015.12.011

Cited by 75 publications

(59 citation statements)

References 109 publications

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“…BSP is usually situated in the ECMof bone and plays a role during remodeling of bone and during the formation of ectopic ossifications. 54,55 BSP was detectable in small amounts in all groups. It was mostly found close to the synovial membrane and in the superficial cartilage areas, as can be seen in the overview image ( Figure 9).…”

Section: Immunhistochemistry Of Bspmentioning

confidence: 84%

<p>Effects of losartan and atorvastatin on the development of early posttraumatic joint stiffness in a rat model</p>

Baranowski

Schlemmer

Förster

et al. 2019

DDDT

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Background After a trauma, exuberant tissue healing with fibrosis of the joint capsule can lead to posttraumatic joint stiffness (PTJS). Losartan and atorvastatin have both shown their antifibrotic effects in different organ systems. Objective The purpose of this study was the evaluation of the influence of losartan and atorvastatin on the early development of joint contracture. In addition to joint angles, the change in myofibroblast numbers and the distribution of bone sialoprotein (BSP) were assessed. Study design and methods In this randomized and blinded experimental study with 24 rats, losartan and atorvastatin were compared to a placebo. After an initial joint injury, rat knees were immobilized with a Kirschner wire. Rats received either losartan, atorvastatin or a placebo orally daily. After 14 days, joint angle measurements and histological assessments were performed. Results Losartan increased the length of the inferior joint capsule. Joint angle and other capsule length measurements did not reveal significant differences between both drugs and the placebo. At cellular level both losartan and atorvastatin reduced the total number of myofibroblasts (losartan: 191±77, atorvastatin: 98±58, placebo: 319±113 per counting field, p <0.01) and the percentage area of myofibroblasts (losartan: 2.8±1.8% [ p <0.05], atorvastatin: 2.5±1.7% [ p <0.01], vs control [6.4±4%], respectively). BSP was detectable in equivalent amounts in the joint capsules of all groups with only a trend toward a reduction of the BSP-stained area by atorvastatin. Conclusion Both atorvastatin and losartan reduced the number of myofibroblasts in the posterior knee joint capsule of rat knees 2 weeks after trauma and losartan increased the length of the inferior joint capsule. However, these changes at the cellular level did not translate an increase in range of motion of the rats´ knee joints during early contracture development.

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Section: Immunhistochemistry Of Bspmentioning

confidence: 84%

<p>Effects of losartan and atorvastatin on the development of early posttraumatic joint stiffness in a rat model</p>

Baranowski

Schlemmer

Förster

et al. 2019

DDDT

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“…Osteopontin is known to localize not only in bone, dentin, cementum, and the formative cells of these hard tissues, but also in a wide range of non‐mineralized tissues such as kidney, macrophages, and T‐lymphocytes (Mark et al, ; Miyazaki et al, ; Hosoya et al, ; Rittling and Singh, ). Bone sialoprotein is found in several types of tissues including bone, dentin, cementum, and cartilage, as well as in the formative cells thereof (Hosoya et al, ; Bouleftour et al, ). These non‐collagenous proteins have been reported to accumulate at the surface of cementum facing the root dentin (Kawaguchi et al, ).…”

Section: Introductionmentioning

confidence: 99%

Localization of RELM‐β/FIZZ2 Is Associated with Cementum Formation

Hosoya

Takahama

Nakamura

2017

The Anatomical Record

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Resistin-like molecule-β/found in inflammatory zone 2 (RELM-β/FIZZ2) is a cysteine-rich secretory protein that is localized in the epithelium of the gastrointestinal tract and lung alveoli. Previous reports have suggested that this protein regulates glucose metabolism and inflammation. In the present study, to analyze the involvement of RELM-β/FIZZ2 in tooth development, we immunohistochemically examined the localization of RELM-β/FIZZ2 in tooth germs of embryonic days (E) 15-20 and postnatal days (P) 7-42 rats. RELM-β/FIZZ2 was hardly detected in the tooth germ at the bud (E15) stage. However, at the cap (E17) and bell (E20) stages, this protein was detectable in the inner enamel epithelium; whereas cells in the other parts of the enamel organ including the outer enamel epithelium and stellate reticulum did not show the immunoreactivity. During the root formation stage (P14-28), cells in Hertwig's epithelial root sheath (HERS) localized RELM-β/FIZZ2. Intense immunoreactivity was also seen in the matrix of the root dentin facing the HERS and the dental follicle. This reactivity was not present on the more upwardly located dentin surface. In contrast, cementum matrix positive for osteopontin and bone sialoprotein was observed on the dentin instead of immunoreactivity for RELM-β/FIZZ2. Osterix-positive cells, indicating cementoblast progenitors, were also detected in the dental follicle near the matrix positive for RELM-β/FIZZ2. These results suggest that RELM-β/FIZZ2 secreted by the inner enamel epithelium was mainly localized in the matrix at the surface of the apical root dentin and might be involved in cementogenesis. Anat Rec, 2017. © 2017 Wiley Periodicals, Inc. Anat Rec, 300:1865-1874, 2017. © 2017 Wiley Periodicals, Inc.

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“…Osteopontin is typically involved in cell adhesion, tissue and extracellular remodeling, inflammation and immune-mediated events (Denhardt, 2002;Wai and Kuo, 2004;Rittling and Singh, 2015;Bouleftour et al, 2016). Despite substantial information about the actions of osteopontin in several tissues, an understanding of its function in male reproduction is far from complete.…”

Section: Proteins Involved In Acrosome Reaction and Fertilizationmentioning

confidence: 99%

Functional aspects of seminal plasma and sperm proteins and their potential as molecularmarkers of fertility

Moura

Memili

2016

Anim Reprod

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Molecular components of sperm and in the media surrounding them influence bull fertility. Given this concept, proteins of the seminal plasma modulate crucial functions and events of reproduction, such as sperm motility and capacitation, cell protection, acrosome reaction, fertilization and embryonic development. Sperm proteins are also important for successful fertilization, egg activation and embryo development. Empirical associations between seminal and sperm proteins and fertility in the bovine indicate that these proteins are potential molecular markers of the male reproductive status.

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The role of the SIBLING, Bone Sialoprotein in skeletal biology — Contribution of mouse experimental genetics

Cited by 75 publications

References 109 publications

<p>Effects of losartan and atorvastatin on the development of early posttraumatic joint stiffness in a rat model</p>

<p>Effects of losartan and atorvastatin on the development of early posttraumatic joint stiffness in a rat model</p>

Localization of RELM‐β/FIZZ2 Is Associated with Cementum Formation

Functional aspects of seminal plasma and sperm proteins and their potential as molecularmarkers of fertility

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