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Tian, J. J.

Publications and source records attributed to Tian, J. J..

2 recordsLinked to original sources

Bridging scale-up to transplantation: pluripotent stem cell-derived pancreatic islet encapsulation in emulsion-generated high concentration alginate beads

Pluripotent stem cell-derived pancreatic islet-like cell clusters (SC-islets) have emerged as potential cellular therapy for type 1 diabetes. While SC-islets can theoretically be produced in bioreactors to meet transplantation needs of many recipients per batch, biomanufacturing and translational challenges remain. SC-islet can be cultured in suspension using stirred tank or vertical wheel bioreactors, but these can impart hydrodynamic damage and lead to cellular agglomeration, particularly upon scale-up. We previously described a robust emulsion-based process to encapsulate murine pancreatic beta cells in high-concentration alginate beads which improved graft survival in allogeneic recipients. Here, we present a full pipeline for scalable microencapsulated SC-islet biomanufacturing with extended in vitro bioreactor culture leading into transplantation. We hypothesized that encapsulation would prevent cellular agglomeration, reduce mechanical stress, and preserve differentiation potential during scale-up. Encapsulation of Stage 6 SC-islets prevented cellular agglomeration during extended suspension culture (25 days) and increased cell recovery (91 +/- 3%) compared with non-encapsulated aggregates (60 +/- 10%). No significant differences in glucose-stimulated insulin secretion were observed with vs without microencapsulation. Stage 7 SC-islets matured in the bioreactor were transplanted either as encapsulated islets via the intraperitoneal route or as free SC-islets under the kidney capsule, where they displayed glucose-responsive human C-peptide secretion and remained functional in vivo for up to 98 days. Overall, this work establishes a scalable, robust, transplantation-ready encapsulation platform that supports SC-islet maturation and delivery, providing a generalizable strategy for scaling and transplanting encapsulated organoid systems.

bioengineering↗

IgG hexamers initiate acute lung injury

Antibodies can initiate lung injury in a variety of disease states such as autoimmunity, transfusion reactions, or after organ transplantation, but the key factors determining in vivo pathogenicity of injury-inducing antibodies are unclear. A previously overlooked step in complement activation by IgG antibodies has been elucidated involving interactions between IgG Fc domains that enable assembly of IgG hexamers, which can optimally activate the complement cascade. Here, we tested the in vivo relevance of IgG hexamers in a complement-dependent alloantibody model of acute lung injury. We used three approaches to block alloantibody hexamerization (antibody carbamylation, the K439E Fc mutation, or treatment with domain B from Staphylococcal protein A), all of which reduced acute lung injury. Conversely, Fc mutations promoting spontaneous hexamerization made a harmful alloantibody into a more potent inducer of acute lung injury and rendered an innocuous alloantibody pathogenic. Treatment with a recombinant Fc hexamer decoy therapeutic protected mice from lung injury, including in a model with transgenic human FCGR2A expression that exacerbated pathology. These results indicate a direct in vivo role of IgG hexamerization in initiating acute lung injury and the potential for therapeutics that inhibit or mimic hexamerization to treat antibody-mediated diseases. Brief summaryIgG antibodies can form hexamers. This study shows that hexamer assembly is an important event determining the ability of IgG to trigger acute lung injury. Graphical abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=141 SRC="FIGDIR/small/577129v1_ufig1.gif" ALT="Figure 1"> View larger version (59K): org.highwire.dtl.DTLVardef@15b0346org.highwire.dtl.DTLVardef@33f39eorg.highwire.dtl.DTLVardef@bf0f4dorg.highwire.dtl.DTLVardef@185b5bf_HPS_FORMAT_FIGEXP M_FIG C_FIG

immunology↗