The inhibition of bone morphogenetic protein 1 attenuates endometriosis lesions in vivo and in vitro

2020 ◽  
Vol 302 (2) ◽  
pp. 415-422
Author(s):  
Xinyue Han ◽  
Feifei Hu ◽  
Fang Chen ◽  
Wei Wang
Keyword(s):  
Bone Morphogenetic Protein ◽  
Morphogenetic Protein ◽  
Bone Morphogenetic Protein 1

scholarly journals Use of Bmp1/Tll1 Doubly Homozygous Null Mice and Proteomics To Identify and Validate In Vivo Substrates of Bone Morphogenetic Protein 1/Tolloid-Like Metalloproteinases

2003 ◽  
Vol 23 (13) ◽  
pp. 4428-4438 ◽  
Author(s):  
William N. Pappano ◽  
Barry M. Steiglitz ◽  
Ian C. Scott ◽  
Douglas R. Keene ◽  
Daniel S. Greenspan
Keyword(s):  
Bone Morphogenetic Protein ◽  
Residual Activity ◽  
Functional Redundancy ◽  
Bmp Signaling ◽  
Null Mouse ◽  
Genetic Redundancy ◽  
Morphogenetic Protein ◽  
Bone Morphogenetic Protein 1

ABSTRACT Bone morphogenetic protein 1 (BMP-1) and mammalian Tolloid (mTLD), two proteinases encoded by Bmp1, provide procollagen C-proteinase (pCP) activity that converts procollagens I to III into the major fibrous components of mammalian extracellular matrix (ECM). Yet, although Bmp1 −/− mice have aberrant collagen fibrils, they have residual pCP activity, indicative of genetic redundancy. Mammals possess two additional proteinases structurally similar to BMP-1 and mTLD: the genetically distinct mammalian Tolloid-like 1 (mTLL-1) and mTLL-2. Mice lacking the mTLL-1 gene Tll1 are embryonic lethal but have pCP activity levels similar to those of the wild type, suggesting that mTLL-1 might not be an in vivo pCP. In vitro studies have shown BMP-1 and mTLL-1 capable of cleaving Chordin, an extracellular antagonist of BMP signaling, suggesting that these proteases might also serve to modulate BMP signaling and to coordinate the latter with ECM formation. However, in vivo evidence of roles for BMP-1 and mTLL-1 in BMP signaling in mammals is lacking. To remove functional redundancy obscuring the in vivo functions of BMP-1-related proteases in mammals, we here characterize Bmp1 Tll1 doubly null mouse embryos. Although these appear morphologically indistinguishable from Tll1 −/− embryos, biochemical analysis of cells derived from doubly null embryos shows functional redundancy removed to an extent enabling us to demonstrate that (i) products of Bmp1 and Tll1 are responsible for in vivo cleavage of Chordin in mammals and (ii) mTLL-1 is an in vivo pCP that provides residual activity observed in Bmp1 −/− embryos. Removal of functional redundancy also enabled use of Bmp1 −/− Tll1 −/− cells in a proteomics approach for identifying novel substrates of Bmp1 and Tll1 products.

scholarly journals Twisted Gastrulation Modulates Bone Morphogenetic Protein-induced Collagen II and X Expression in Chondrocytes in Vitro and in Vivo

2006 ◽  
Vol 281 (42) ◽  
pp. 31790-31800
Author(s):  
Martina Schmidl ◽  
Nadia Adam ◽  
Cordula Surmann-Schmitt ◽  
Takako Hattori ◽  
Michael Stock ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Twisted Gastrulation ◽  
Morphogenetic Protein ◽  
Collagen Ii

scholarly journals Surface Immobilization of TiO2 Nanotubes with Bone Morphogenetic Protein-2 Synergistically Enhances Initial Preosteoblast Adhesion and Osseointegration

2019 ◽  
Vol 2019 ◽  
pp. 1-12 ◽  
Author(s):  
Ying Li ◽  
Yunjia Song ◽  
Aobo Ma ◽  
Changyi Li
Keyword(s):  
Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 2 ◽  
Surface Immobilization ◽  
Implant Surface ◽  
Cytoskeleton Organization ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein ◽  
Collagen Type 1

Although titanium (Ti) alloys have been widely used as implant materials, the bioinertness of pristine Ti impairs their bioactivity and early osseointegration. In the present work, we prepared TiO2 nanotubes (TNT) layer on the titanium (Ti) surface by anodic oxidation. The anodized surface was functionalized with human bone morphogenetic protein-2 coating to form the hBMP-2/TNT surface. The release behavior of hBMP-2 on the hBMP-2/TNT surface displayed a controlled and sustained pattern, compared to that on the hBMP-2/Ti surface, which showed a rapid release. In vitro cellular activity tests demonstrated that both TNT and hBMP-2/Ti surfaces, particularly the hBMP-2/TNT surface, enhanced adhesion, proliferation, and differentiation of osteoblast cells. Increased cell adhesion, improved cytoskeleton organization, and immunofluorescence staining of vinculin were observed on the modified surfaces. The TNT, hBMP-2/Ti, and hBMP-2/TNT surfaces, especially the hBMP-2/TNT surface, further displayed an upregulated gene expression of adhesion and osteogenic markers vinculin, collagen type 1, osteopontin, and osteocalcin, compared to the pristine Ti surface. In vivo experiments using a rat model demonstrated that the TNT and hBMP-2/Ti surfaces, in particular the hBMP-2/TNT surface, improved osseointegration and showed a superior bone bonding ability compared to Ti. Our study revealed a synergistic role played by TiO2 nanotubes nanotopography and hBMP-2 in promoting initial osteoblast adhesion, proliferation, differentiation, and osseointegration, thus suggesting a promising method for better modifying the implant surface.

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