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Advanced bioactive glue tethering Lubricin/PRG4 to promote integrated healing of avascular meniscus tears

Bioactive Materials 2023年第10期28卷 61-73页

作者： Solaiman Tarafder Jaskirti Ghataure david langford Rachel Brooke Ryunhyung Kim Samantha Lewis Eyen Julian Bensadoun Jeffrey T.Felix James L.Cook Chang H.Lee Regenerative Engineering Laboratory Columbia University Medical Center630 W.168 St.-VC12-212New YorkNY10032USA Thompson Laboratory for Regenerative Orthopaedics Missouri Orthopedic InstituteUniversity of Missouri1100 Virginia AvenueColumbi1MO65212USA

Meniscus injuries are extremely common with approximately one million patients undergoing surgical treatment annually in the U.S. alone, but no regenerative therapy exist. Previously, we showed that controlled applications of connective tissue growth factor (CTGF) and transforming growth factor beta 3 (TGFβ3) via fibrin-based bio-glue facilitate meniscus healing by inducing recruitment and stepwise differentiation of synovial mesenchymal stem/progenitor cells. Here, we first explored the potential of genipin, a natural crosslinker, to enhance fibrin-based glue’s mechanical and degradation properties. In parallel, we identified the harmful effects of lubricin on meniscus healing and investigated the mechanism of lubricin deposition on the injured meniscus surface. We found that the pre-deposition of hyaluronic acid (HA) on the torn meniscus surface mediates lubricin deposition. Then we implemented chemical modifications with heparin conjugation and CD44 on our bioactive glue to achieve strong initial bonding and integration of lubricin pre-coated meniscal tissues. Our data suggested that heparin conjugation significantly enhances lubricin-coated meniscal tissues. Similarly, CD44, exhibiting a strong binding affinity to lubricin and hyaluronic acid (HA), further improved the integrated healing of HA/lubricin pre-coated meniscus injuries. These findings may represent an important foundation for developing a translational bio-active glue guiding the regenerative healing of meniscus injuries.

关键词： Knee meniscus Bioactive glue Stem cell recruitment Lubricin

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第三个一千年

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1992年

作者：布赖恩·斯特布尔福特(Brian Stableford) 戴维·兰福特(david langford)

来源：南通市图书馆图书汇雅图书（南通市图书馆... 评论

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Helicobacter pylori arginase mutant colonizes arginase Ⅱ knockout mice

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World Journal of Gastroenterology 2011年第28期17卷 3300-3309页

作者： Songhee H Kim Melanie L langford Jean-Luc Boucher Traci L Testerman david J McGee Department of Microbiology and Immunology Louisiana State University Health Sciences Center-Shreveport University of Nebraska-Lincoln School of Biological SciencesLincoln Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques Université Paris Descartes

AIM: To investigate the role of host and bacterial arginases in the colonization of mice by Helicobacter pylori (***).METHODS: *** produces a very powerful urease that hydrolyzes urea to carbon dioxide and ammonium,which neutralizes *** is absolutely essential to *** pathogenesis;therefore,the urea substrate must be in ample supply for urease to work *** urea substrate is most likely provided by arginase activity,which hydrolyzes L-arginine to L-ornithine and *** work has demonstrated that *** arginase is surprisingly not required for colonization of wild-type ***,another in vivo source of the critical urea substrate must *** hypothesized that the urea source was provided by host arginase Ⅱ,since this enzyme is expressed in the stomach,and *** has previously been shown to induce the expression of murine gastric arginase Ⅱ.To test this hypothesis,wild-type and arginase (rocF) mutant *** strain SS1 were inoculated into arginase Ⅱ knockout ***: Surprisingly,both the wild-type and rocF mutant bacteria still colonized arginase Ⅱ knockout ***,feeding arginase Ⅱ knockout mice the host arginase inhibitor S-(2-boronoethyl)L-cysteine (BEC),while inhibiting > 50% of the host arginase Ⅰ?activity in several tissues,did not block the ability of the rocF mutant *** to *** contrast,BEC poorly inhibited *** arginase ***: The in vivo source for the essential urea utilized by *** urease is neither bacterial arginase nor host arginase Ⅱ;instead,either residual host arginase Ⅰ?or agmatinase is probably responsible.

关键词： Arginase Helicobacter pylori S-(2-boronoethyl)-L-cysteine Urease Mice

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