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An overview of human pluripotent stem cell applications for the understanding and treatment of blindness
Published in John Ravenscroft, The Routledge Handbook of Visual Impairment, 2019
Louise A. Rooney, Duncan E. Crombie, Grace E. Lidgerwood, Maciej Daniszewski, Alice Pébay
McCabe et al. (2015) described a two-step methodology for the generation of corneal endothelium from hESCs. First, neural crest and central nervous system progenitors were generated by the treatment of hESCs with SB431542 and Noggin. Following this, neural crest cells were differentiated to corneal epithelium by the addition of platelet-derived growth factor B (PDGFB), DKK2 and bFGF. This approach produces large quantities of corneal endothelial cells, similar to adult corneal endothelial cells, characterised by morphology, gene expression and protein expression. Other work has been undertaken to generate hPSC-derived corneal organoids for the investigation of cornea development and disease modelling (Foster et al., 2017). Through sequential differentiation protocols, retinal, and at later stages, corneal organoids were generated comprising the cell types of the cornea. This induction was achieved by forced aggregation of single cell dissociated iPSCs, followed by treatment with neural induction medium and later DMEM/F12 supplemented with B27, a neural cell culture supplement, fetal bovine serum (FBS) and retinoic acid to induce retinal maturation and corneal generation. The cornea organoids expressed markers of the epithelium (Keratin 14), stroma (Keratocan, Collagen types I and V, and Lumican) and endothelium (Collagen Type VIII Alpha Chain 1 and F11 Receptor (endothelial tight junction protein)) and notably extracellular matrix collagens and stromal matrix proteins. This work provides a platform to investigate corneal disease phenotypes, including interactions of different cell types, over long periods of time.
F11R/JAM-A: why do platelets express a molecule which is also present in tight junctions?
Published in Platelets, 2023
Piotr Kamola, Anna Babinska, Tomasz Przygodzki
In 1990, Kornecki et al. showed that certain antibodies which had the capability of activating human blood platelets were binding to a protein target which was not known at the time. The protein was named F11 receptor (F11R) after the name of the clone of these antibodies (F11).1 Platelet activation induced by binding of the antibodies to F11R was primarily shown to be dependent on the interaction of Fc fragment of F11 antibodies with FcγRII receptor present on blood platelets5 (Figure 1). In 1998, a similar protein was isolated during studies on tight junctions in epithelial and endothelial cell monolayers.2 The protein was recognized as an immunoglobulin and named after its function as Junctional Adhesion Molecule (JAM). In the wake of full sequencing of the protein, the homology of JAM-A and F11R was established.6,7 As an effect of this convergent discovery, the two names of the protein exist simultaneously in scientific publications. This status quo gained legitimacy by the decision of the Human Genome Nomenclature committee which has approved F11R as a symbol of the gene number AF207907, and the number BC021876 for the murine molecule, while JAM-A was mentioned as one of the alias symbols among others such as PAM-1, JCAM, JAM-1, JAMA, and CD321.
Helicobacter pylori PqqE is a new virulence factor that cleaves junctional adhesion molecule A and disrupts gastric epithelial integrity
Published in Gut Microbes, 2021
Miguel S. Marques, Ana C. Costa, Hugo Osório, Marta L. Pinto, Sandra Relvas, Mário Dinis-Ribeiro, Fátima Carneiro, Marina Leite, Ceu Figueiredo
Stable cell lines with either flJAM-A or sJAM-A were generated in CHO cells, which do not express JAM-A. The human flJAM-A open reading frame (Ultimate™ ORF Clone ID IOH12781_Homo sapiens F11 receptor) and the sJAM-A vector generated through the deletion of the region that encodes Ala285 to Val299 were obtained from Invitrogen. Both flJAM-A and sJAM-A were cloned into a pENTR™ Directional TOPO® Entry vector. After confirmation of the sequences of both vectors using the M13 primers (Supplementary Table S7), flJAM-A and sJAM-A sequences were cloned in the pEF6/myc-His A expression vector, using the Gateway® cloning technology according to the manufacturer’s instructions.