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Full-Text Articles in Life Sciences
Acid Ceramidase Maintains The Chondrogenic Phenotype Of Expanded Primary Chondrocytes And Improves The Chondrogenic Differentiation Of Bone Marrow-Derived Mesenchymal Stem Cells, Calogera M. Simonaro, Sylvain Sachot, Yi Ge, Xingxuan He, Victor A. Deangelis, Efrat Eliyahu, Daniel J. Leong, Hui B. Sun, Jeffrey B. Mason, Mark E. Haskins, Dean W. Richardson, Edward H. Schuchman
Acid Ceramidase Maintains The Chondrogenic Phenotype Of Expanded Primary Chondrocytes And Improves The Chondrogenic Differentiation Of Bone Marrow-Derived Mesenchymal Stem Cells, Calogera M. Simonaro, Sylvain Sachot, Yi Ge, Xingxuan He, Victor A. Deangelis, Efrat Eliyahu, Daniel J. Leong, Hui B. Sun, Jeffrey B. Mason, Mark E. Haskins, Dean W. Richardson, Edward H. Schuchman
Animal, Dairy, and Veterinary Science Faculty Publications
Acid ceramidase is required to maintain the metabolic balance of several important bioactive lipids, including ceramide, sphingosine and sphingosine-1-phosphate. Here we show that addition of recombinant acid ceramidase (rAC) to primary chondrocyte culture media maintained low levels of ceramide and led to elevated sphingosine by 48 hours. Surprisingly, after three weeks of expansion the chondrogenic phenotype of these cells also was markedly improved, as assessed by a combination of histochemical staining (Alcian Blue and Safranin-O), western blotting (e.g., Sox9, aggrecan, collagen 2A1), and/or qPCR. The same effects were evident in rat, equine and human cells, and were observed in monolayer …
Physiological Level Production Of Antigen-Specific Human Immunoglobulin In Cloned Transchromosomic Cattle, A. Sano, H. Matsushita, H. Wu, J. Jiao, P. Kasinathan, E. J. Sullivan, Z. Wang, Y. Kuroiwa
Physiological Level Production Of Antigen-Specific Human Immunoglobulin In Cloned Transchromosomic Cattle, A. Sano, H. Matsushita, H. Wu, J. Jiao, P. Kasinathan, E. J. Sullivan, Z. Wang, Y. Kuroiwa
Animal, Dairy, and Veterinary Science Faculty Publications
Therapeutic human polyclonal antibodies (hpAbs) derived from pooled plasma from human donors are Food and Drug Administration approved biologics used in the treatment of a variety of human diseases. Powered by the natural diversity of immune response, hpAbs are effective in treating diseases caused by complex or quickly-evolving antigens such as viruses. We previously showed that transchromosomic (Tc) cattle carrying a human artificial chromosome (HAC) comprising the entire unrearranged human immunoglobulin heavy-chain (hIGH) and kappa-chain (hIGK) germline loci (named as κHAC) are capable of producing functional hpAbs when both of the bovine immunoglobulin mu heavy-chains, bIGHM and bIGHML1, are homozygously …