Статті в журналах: "CD2BP2"

1

Guo, Xiaobo, Gang Li, Yufeng Zhao, and Bo Zhao. "TGFB Induced Factor Homeobox 2 Induces Deterioration of Bladder Carcinoma via Activating CD2 Cytoplasmic Tail Binding Protein 2." Journal of Biomedical Nanotechnology 19, no. 9 (September 1, 2023): 1670–76. http://dx.doi.org/10.1166/jbn.2023.3657.

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Bladder carcinoma is a complex and aggressive malignancy with limited treatment options. In this study, we aimed to investigate the expression pattern of TGIF2 in bladder carcinoma and its clinical significance, as well as its functional role and interaction with CD2BP2 in disease progression. Through quantitative reverse transcription-polymerase chain reaction (qRT-PCR) analysis, we found that TGIF2 was highly expressed in bladder carcinoma tissues compared to normal bladder mucosa. Furthermore, elevated TGIF2 levels were associated with advanced tumor stage and larger tumor size, indicating its potential as a prognostic marker in bladder carcinoma. Using knockdown models in bladder carcinoma cell lines (253j and J82), we observed that the inhibition of TGIF2 resulted in decreased proliferation and migration rates, suggesting a critical role of TGIF2 in promoting these malignant phenotypes. Additionally, our dual-luciferase reporter assay revealed a direct interaction between TGIF2 and CD2BP2, with CD2BP2 being upregulated in bladder carcinoma tissues and positively correlated with TGIF2 expression. Notably, the overexpression of CD2BP2 reversed the suppressed malignant phenotypes caused by TGIF2 knockdown. Collectively, our findings highlight the abundant expression of TGIF2 in bladder carcinoma tissues and its association with malignant characteristics. We demonstrate that TGIF2 promotes proliferative and metastatic capacities in bladder carcinoma by positively regulating CD2BP2. These insights provide a basis for further investigations into the potential of TGIF2 and CD2BP2 as therapeutic targets and prognostic markers in bladder carcinoma management.

2

Kofler, Michael, Kathrin Motzny, Michael Beyermann, and Christian Freund. "Novel Interaction Partners of the CD2BP2-GYF Domain." Journal of Biological Chemistry 280, no. 39 (July 6, 2005): 33397–402. http://dx.doi.org/10.1074/jbc.m503989200.

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3

Heinze, M., M. Kofler, and C. Freund. "Investigating the functional role of CD2BP2 in T cells." International Immunology 19, no. 11 (September 6, 2007): 1313–18. http://dx.doi.org/10.1093/intimm/dxm100.

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4

Albert, Gesa I., Christoph Schell, Karin M. Kirschner, Sebastian Schäfer, Ronald Naumann, Alexandra Müller, Oliver Kretz, et al. "The GYF domain protein CD2BP2 is critical for embryogenesis and podocyte function." Journal of Molecular Cell Biology 7, no. 5 (June 16, 2015): 402–14. http://dx.doi.org/10.1093/jmcb/mjv039.

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5

Nielsen, Tine K., Sunbin Liu, Reinhard Lührmann, and Ralf Ficner. "Structural Basis for the Bifunctionality of the U5 snRNP 52K Protein (CD2BP2)." Journal of Molecular Biology 369, no. 4 (June 2007): 902–8. http://dx.doi.org/10.1016/j.jmb.2007.03.077.

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6

Kofler, Michael, Katja Heuer, Tobias Zech, and Christian Freund. "Recognition Sequences for the GYF Domain Reveal a Possible Spliceosomal Function of CD2BP2." Journal of Biological Chemistry 279, no. 27 (April 22, 2004): 28292–97. http://dx.doi.org/10.1074/jbc.m402008200.

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7

Andujar-Sanchez, Montserrat, Eva S. Cobos, Irene Luque, and Jose C. Martinez. "Thermodynamic Impact of Embedded Water Molecules in the Unfolding of Human CD2BP2-GYF Domain." Journal of Physical Chemistry B 116, no. 24 (June 4, 2012): 7168–75. http://dx.doi.org/10.1021/jp303495b.

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8

Piotukh, K., and C. Freund. "A novel hSH3 domain scaffold engineered to bind folded domains in CD2BP2 and HIV capsid protein." Protein Engineering Design and Selection 25, no. 10 (September 17, 2012): 649–56. http://dx.doi.org/10.1093/protein/gzs062.

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9

Gan, Zhen, Bei Wang, Yishan Lu, Shuanghu Cai, Jia Cai, JiChang Jian, and Zaohe Wu. "Molecular characterization and expression of CD2BP2 in Nile tilapia (Oreochromis niloticus) in response to Streptococcus agalactiae stimulus." Gene 548, no. 1 (September 2014): 126–33. http://dx.doi.org/10.1016/j.gene.2014.07.032.

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10

Kang, Yuanyuan, Bhavita Patel, Kairong Cui, Keji Zhao, Yi Qiu, and Suming Huang. "A T-Cell Specific Element Activates the TAL1 Oncogene Via an Interchromosomal Interaction During Leukemogenesis." Blood 120, no. 21 (November 16, 2012): 3507. http://dx.doi.org/10.1182/blood.v120.21.3507.3507.

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Abstract Abstract 3507 T-cell acute lymphoblastic leukemia (T-ALL) is an aggressive malignant disease of thymocytes that mainly affects children and has very poor prognosis with high rates of relapse. A prominent feature observed in 60% of T-ALL childhood patients is the ectopic expression of a key hematopoietic transcription factor TAL1/SCL. Although several enhancers has been identified to play an important role in normal hematopoietic differentiation, the histone modification patterns and chromatin organization over the whole TAL1 locus reveled that none of them is active in T-ALL cell lines such as Jurkat and Rex cells. It remains currently unknown how TAL1 is activated in the majority of T-ALL patients lacking the TAL1 locus rearrangements. To understand the molecular mechanism underlying regulation of the TAL1 oncogene in leukemic T-cells, we employed circularized chromosome conformation capture (4C) methodology to identify new regulatory elements that activate TAL1 specifically in T-ALL leukemia. Using the TAL1 promoter 1a as the bait, we discovered that the TAL1 promoter 1a interacts with the TIL16 element (TAL1 interacting locus in chromosome 16) that is located at ∼15 Kb downstream of T-cell specific CD2BP2 gene in T-ALL cell line Jurkat, but not in erythroid progenitor K562 cells. The CD2BP2 protein is a cellular adapter protein that was originally identified as a binding partner of the T cell adhesion protein CD2 in the context of T cell signaling. The TIL16 element contains the bind sites for several transcription factors that are important for hematopoiesis such as C-Maf, Pax5, HoxA7 and USF2. The inter-chromosomal interaction between the TIL16 and the TAL1 promoter 1a was further confirmed by chromosome conformation capture (3C) assay in three TAL1 over-expressing T-ALL cell lines, Jurkat, REX and Molt4, but not in K562 cells. Recent genome wide study has correlates H3K4 mono- or dimethyl marks with distal enhancers while trimethyl H3K4 is enriched in promoters of active genes. To further test if the TIL16 acts as T-cell specific enhancer for TAL1 activation in T-ALL cells, we carried out ChIP-seq and ChIP analysis in CD4 T cells, Jurkat, and K562 cells. We found that the TIL16 element is specifically marked by H3K4me1 in Jurkat and CD4+ T-cells but not in K562 cells. The enrichment of H3K4me1 is correlated with the binding of c-Maf, a T-cell specific transcription factor. To further test whether the TIL16 element contributes to transcription activity, a DNA fragments containing the TIL16 element were cloneed into SV40 minimal promoter driven luciferase reporter and introduced into K562 and several T-ALL cell lines. Compared to the pGL3-SV40 vector that showed only minimal luciferase activity, the 1 Kb TIL element specifically activated transcription of the luciferase reporter in T-ALL cells, but not in erythroid progenitor K562 cells suggesting that the TIL16 element functions as a T-cell specific TAL1 enhancer. Thus, our data revealed a novel epigenetic mechanism by which the TAL1 oncogene is ectopically activated in T-cell leukemia. Disclosures: No relevant conflicts of interest to declare.

11

LAGGERBAUER, B. "The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation." RNA 11, no. 5 (May 1, 2005): 598–608. http://dx.doi.org/10.1261/rna.2300805.

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12

Wang, Chris, Laura Wilson-Berry, Tim Schedl, and Dave Hansen. "TEG-1 CD2BP2 regulates stem cell proliferation and sex determination in the C. elegans germ line and physically interacts with the UAF-1 U2AF65 splicing factor." Developmental Dynamics 241, no. 3 (January 30, 2012): 505–21. http://dx.doi.org/10.1002/dvdy.23735.

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13

Nadler, M. J., P. A. McLean, B. G. Neel, and H. H. Wortis. "B cell antigen receptor-evoked calcium influx is enhanced in CD22-deficient B cell lines." Journal of Immunology 159, no. 9 (November 1, 1997): 4233–43. http://dx.doi.org/10.4049/jimmunol.159.9.4233.

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Abstract CD22 is a B cell membrane glycoprotein that, upon Ag receptor engagement, becomes rapidly tyrosyl phosphorylated and associates with several signaling molecules including Lyn, Syk, PLCgamma1, and the protein-tyrosine phosphatase, SHP-1. Two allelic forms of murine CD22 exist: CD22.1 is expressed in strains such as NZB and DBA/2, whereas CD22.2 is expressed in BALB/c and most other strains. WEHI-231 cells, which derive from a (BALB/c x NZB)F1 mouse, express one copy of each allele. Previous studies have proposed both positive and negative functions for CD22. We explored the role of CD22 in surface IgM Ag receptor signal transduction by examining signaling in three clonally independent WEHI-231 variants that have lost expression of the CD22.2 allele. This experimental design allowed us to assess the signaling functions of CD22 independent of its developmental role. These variants, which exhibit a 50% reduction of total surface CD22, are hyper-responsive to Ag receptor stimulation: several cellular proteins are hyperphosphorylated on tyrosyl residues and surface IgM-mediated calcium flux is markedly increased. Interestingly, the increased calcium response observed in CD22-deficient cells is due largely to enhanced calcium influx. Reconstitution of CD22 expression reduces these changes. The SHP-1/CD22 association is reduced in CD22-deficient cell lines and is restored by re-expression of CD22. Our results demonstrate that CD22 is a cell autonomous negative regulator of B cell Ag receptor signaling, and suggest that it regulates calcium entry via a mechanism downstream from or independent of calcium release from intracellular stores.

14

Aziz Muhammad, Hawzheen. "MOLECULAR DOCKING OF SELECTED CD22 INHIBITORS TARGETING HUMAN CD22 RECEPTOR ON B CELLS." Journal of Sulaimani Medical College 10, no. 3 (December 21, 2020): 355–69. http://dx.doi.org/10.17656/jsmc.10276.

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15

Li, Cong, Vesa Ruotsalainen, Karl Tryggvason, Andrey S. Shaw, and Jeffrey H. Miner. "CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere." American Journal of Physiology-Renal Physiology 279, no. 4 (October 1, 2000): F785—F792. http://dx.doi.org/10.1152/ajprenal.2000.279.4.f785.

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CD2-associated protein (CD2AP) is an adapter molecule that can bind to the cytoplasmic domain of nephrin, a component of the glomerular slit diaphragm. Mice lacking CD2AP exhibit a congenital nephrotic syndrome characterized by extensive foot process effacement, suggesting that CD2AP-nephrin interactions are critical to maintaining slit diaphragm function. We have examined the patterns of expression of both CD2AP and nephrin in developing mouse and human kidney. Both proteins were first detected in developing podocytes at the capillary loop stage of glomerulogenesis and eventually became concentrated near the glomerular basement membrane. CD2AP was also observed diffusely in collecting duct and apically in many cells of proximal and distal tubule. Kidneys from Cd2ap −/− mice initially exhibited normal nephrin localization, but as the mice aged and foot processes became effaced, nephrin disappeared. In laminin-β2 mutant mice exhibiting nephrotic syndrome, CD2AP in glomeruli was aberrantly localized in a primarily punctate pattern. Extensive extrarenal expression of CD2AP was observed in endothelial and epithelial cells, in many cases with a specific subcellular localization. Together, these results suggest that CD2AP is not only involved in maintaining the slit diaphragm but may also have a general role in maintaining specialized subcellular architecture. The severity of kidney disease in Cd2ap mutant mice may have eclipsed manifestation of defects in other tissues.

16

Monzo, Pascale, Nils C. Gauthier, Frédérique Keslair, Agnès Loubat, Christine M. Field, Yannick Le Marchand-Brustel, and Mireille Cormont. "Clues to CD2-associated Protein Involvement in Cytokinesis." Molecular Biology of the Cell 16, no. 6 (June 2005): 2891–902. http://dx.doi.org/10.1091/mbc.e04-09-0773.

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Cytokinesis requires membrane trafficking coupled to actin remodeling and involves a number of trafficking molecules. CD2-associated protein (CD2AP) has been implicated in dynamic actin remodeling and membrane trafficking that occurs during endocytosis leading to the degradative pathway. In this study, we present several arguments for its implication in cytokinesis. First, endogenous CD2AP was found concentrated in the narrow region of the midzone microtubules during anaphase and in the midbody during late telophase. Moreover, we found that CD2AP is a membrane- and not a microtubule-associated protein. Second, the overexpression of the first two Src homology 3 domains of CD2AP, which are responsible for this localization, led to a significant increase in the rate of cell multinucleation. Third, the CD2AP small interfering RNA interfered with the cell separation, indicating that CD2AP is required for HeLa cells cytokinesis. Fourth, using the yeast two-hybrid system, we found that CD2AP interacted with anillin, a specific cleavage furrow component, and the two proteins colocalized at the midbody. Both CD2AP and anillin were found phosphorylated early in mitosis and also CD2AP phosphorylation was coupled to its delocalization from membrane to cytosol. All these observations led us to propose CD2AP as a new player in cytokinesis.

17

Lehtonen, Sanna, Fang Zhao, and Eero Lehtonen. "CD2-associated protein directly interacts with the actin cytoskeleton." American Journal of Physiology-Renal Physiology 283, no. 4 (October 1, 2002): F734—F743. http://dx.doi.org/10.1152/ajprenal.00312.2001.

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CD2-associated protein (CD2AP) is an adapter protein associating with several membrane proteins, including nephrin, mutated in congenital nephrotic syndrome of the Finnish type, and polycystin-2, mutated in type 2 autosomal dominant polycystic kidney disease. Both proteins have critical roles in the maintenance of the integrity of the nephrons. Previous studies have suggested a role for CD2AP in the regulation of the organization of the actin cytoskeleton, but it has not been known whether the postulated association between CD2AP and actin is direct or mediated by other proteins. In this study, we address this question by using various cellular and biochemical approaches. We show that CD2AP and F-actin partially colocalize in cultured cells and that disruption of the actin cytoskeleton results in disorganization of endogenous CD2AP. Using cytoskeletal fractionation by differential centrifugation, we demonstrate that a proportion of CD2AP associates with the actin cytoskeleton. Furthermore, using pure actin and purified CD2AP fusion proteins in an F-actin coprecipitation assay, we show that CD2AP directly associates with filamentous actin and that this interaction is mediated by means of the COOH terminus of CD2AP. The present results suggest that CD2AP is involved in the regulation of the actin cytoskeleton and indicate that CD2AP may act as a direct adapter between the actin cytoskeleton and cell membrane proteins, such as nephrin and polycystin-2. Alterations in these interactions could explain some of the pathophysiological changes in congenital nephrotic syndrome and polycystic kidney disease.

18

Tsvetkov, Dmitry, Michael Hohmann, Yoland Marie Anistan, Marwan Mannaa, Christian Harteneck, Birgit Rudolph, and Maik Gollasch. "A CD2AP Mutation Associated with Focal Segmental Glomerulosclerosis in Young Adulthood." Clinical Medicine Insights: Case Reports 9 (January 2016): CCRep.S30867. http://dx.doi.org/10.4137/ccrep.s30867.

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Mutations in CD2-associated protein (CD2AP) have been identified in patients with focal segmental glomerulosclerosis (FSGS); however, reports of CD2AP mutations remain scarce. We performed Sanger sequencing in a patient with steroid-resistant FSGS and identified a heterozygous CD2AP mutation (p.T374A, c.1120 A > G). Our patient displayed mild cognitive decline, a phenotypic characteristic not previously associated with CD2AP-associated FSGS. His proteinuria was remarkably reduced by treatment with cyclosporine A. Our findings expand the genetic spectrum of CD2AP-associated disorders and broaden the associated phenotype with the co-occurrence of cognitive decline. Our case shows that cyclosporin A is a treatment option for CD2AP-associated nephropathy.

19

Tossidou, Irini, Beina Teng, Kirstin Worthmann, Janina Müller-Deile, Tilman Jobst-Schwan, Christian Kardinal, Patricia Schroder, et al. "Tyrosine Phosphorylation of CD2AP Affects Stability of the Slit Diaphragm Complex." Journal of the American Society of Nephrology 30, no. 7 (June 24, 2019): 1220–37. http://dx.doi.org/10.1681/asn.2018080860.

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BackgroundCD2-associated protein (CD2AP), a slit diaphragm–associated scaffolding protein involved in survival and regulation of the cytoskeleton in podocytes, is considered a “stabilizer” of the slit diaphragm complex that connects the slit diaphragm protein nephrin to the cytoskeleton of the cell. Tyrosine phosphorylation of slit diaphragm molecules can influence their surface expression, but it is unknown whether tyrosine phosphorylation events of CD2AP are also physiologically relevant to slit diaphragm stability.MethodsWe used isoelectric focusing, western blot analysis, and immunofluorescence to investigate phosphorylation of CD2AP, and phospho-CD2AP antibodies and site-directed mutagenesis to define the specific phosphorylated tyrosine residues. We used cross-species rescue experiments in Cd2apKD zebrafish and in Drosophila cindrRNAi mutants to define the physiologic relevance of CD2AP phosphorylation of the tyrosine residues.ResultsWe found that VEGF-A stimulation can induce a tyrosine phosphorylation response in CD2AP in podocytes, and that these phosphorylation events have an important effect on slit diaphragm protein localization and functionality in vivo. We demonstrated that tyrosine in position Y10 of the SH3–1 domain of CD2AP is indispensable for CD2AP function in vivo. We found that the binding affinity of nephrin to CD2AP is significantly enhanced in the absence of Y10; however, unexpectedly, this increased affinity leads not to stabilization but to functional impairment of the glomerular filtration barrier.ConclusionsOur findings provide insight into CD2AP and its phosphorylation in the context of slit diaphragm functionality, and indicate a fine-tuned affinity balance of CD2AP and nephrin that is influenced by receptor tyrosine kinase stimulation.

20

Welsch, Thilo, Nicole Endlich, Gökmen Gökce, Elena Doroshenko, Jeremy C. Simpson, Wilhelm Kriz, Andrey S. Shaw, and Karlhans Endlich. "Association of CD2AP with dynamic actin on vesicles in podocytes." American Journal of Physiology-Renal Physiology 289, no. 5 (November 2005): F1134—F1143. http://dx.doi.org/10.1152/ajprenal.00178.2005.

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The docking protein CD2AP (CD2-associated protein) serves a nonredundant function in podocytes as CD2AP knockout mice die of renal failure at the age of 6–7 wk. Furthermore, haploinsufficiency due to mutation of the CD2AP gene is associated with focal segmental glomerulosclerosis in humans. Although CD2AP has been shown to interact with proteins regulating actin polymerization, with proteins of the slit diaphragm, and with the endocytic machinery, its critical function in podocytes remains unclear. In conditionally immortalized mouse podocytes, we demonstrate that CD2AP colocalizes with cortactin and F-actin in spots of ≤0.5-μm diameter. Confocal time-lapse microscopy in living podocytes expressing GFP-CD2AP or GFP-actin revealed that spots are motile, possess a limited lifetime, and are frequently associated with vesicles. A significant portion of spot-associated vesicles belongs to a later endosomal-sorting compartment, characterized by delayed uptake of fluorescent dextran (10 kDa) and by colocalization with Rab4, but not Rab5 and AP-2. Rapid accumulation of microinjected G-actin in spots and abrogation of spot motility by jasplakinolide demonstrate that spot movements depend on actin polymerization. Furthermore, a high turnover (half-time < 10 s) of CD2AP in spots was demonstrated by FRAP (fluorescence recovery after photobleaching). Our results demonstrate that CD2AP is associated with dynamic actin in a specific late endosomal compartment in podocytes, suggesting that CD2AP might be crucially involved in endosomal sorting and/or trafficking via regulation of actin assembly on vesicles.

21

Kurilla, Anita, Loretta László, Tamás Takács, Álmos Tilajka, Laura Lukács, Julianna Novák, Rita Pancsa, László Buday, and Virág Vas. "Studying the Association of TKS4 and CD2AP Scaffold Proteins and Their Implications in the Partial Epithelial–Mesenchymal Transition (EMT) Process." International Journal of Molecular Sciences 24, no. 20 (October 13, 2023): 15136. http://dx.doi.org/10.3390/ijms242015136.

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Colon cancer is a leading cause of death worldwide. Identification of new molecular factors governing the invasiveness of colon cancer holds promise in developing screening and targeted therapeutic methods. The Tyrosine Kinase Substrate with four SH3 domains (TKS4) and the CD2-associated protein (CD2AP) have previously been linked to dynamic actin assembly related processes and cancer cell migration, although their co-instructive role during tumor formation remained unknown. Therefore, this study was designed to investigate the TKS4-CD2AP interaction and study the interdependent effect of TKS4/CD2AP on oncogenic events. We identified CD2AP as a novel TKS4 interacting partner via co-immunoprecipitation-mass spectrometry methods. The interaction was validated via Western blot (WB), immunocytochemistry (ICC) and proximity ligation assay (PLA). The binding motif of CD2AP was explored via peptide microarray. To uncover the possible cooperative effects of TKS4 and CD2AP in cell movement and in epithelial-mesenchymal transition (EMT), we performed gene silencing and overexpressing experiments. Our results showed that TKS4 and CD2AP form a scaffolding protein complex and that they can regulate migration and EMT-related pathways in HCT116 colon cancer cells. This is the first study demonstrating the TKS4-CD2AP protein–protein interaction in vitro, their co-localization in intact cells, and their potential interdependent effects on partial-EMT in colon cancer.

22

Fox, Mark A., Andrés E. Goeta, Andrew K. Hughes, John M. Malget, and Ken Wade. "Halogenation of Tris(amido)tantalacarboranes with Dihalomethanes CH2X2 (X = Cl, Br)." Collection of Czechoslovak Chemical Communications 67, no. 6 (2002): 791–807. http://dx.doi.org/10.1135/cccc20020791.

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Slow reactions of isomeric metallacarboranes of general formulae [(NMe2)3TaC2B9H11] (3 isomers) and [(NMe2)3TaC2B9H10Me] (3 isomers) with CD2Cl2 afford quantitative yields of monochloro complexes [Cl(NMe2)2TaC2B9H11] and [Cl(NMe2)2TaC2B9H10Me]. Exposure to CD2Cl2 for months leads to solutions containing about 70% of the dichlorides in three cases. More prolonged exposure of these and the other monochlorides leads to a mixture of boron-substituted complexes. Hydrolysis of [3,3,3-(NMe2)3-3,1,2-TaC2B9H11] by moist toluene results in the formation of the oxo-bridged complex 3,3'-[3,3-(NMe2)2-3,1,2-TaC2B9H11]2(μ-O), characterised by single-crystal X-ray crystallography. The limited solubility of the latter complex in CD2Cl2 eliminates the presence of this compound in the reaction of [3,3,3-(NMe2)3-3,1,2-TaC2B9H11] with CD2Cl2. The reaction of [2,2,2-(NMe2)3-2,1,12-TaC2B9H11] with CH2Br2 in C6D6 quantitatively yields the monobromide [2-Br-2,2-(NMe2)2-2,1,12-TaC2B9H11]. Prolonged reaction with CH2Br2 leads directly to isomeric boron-substituted complexes with no evidence for dibromides. The influence on 11B, 13C and 1H NMR chemical shifts of replacing an amide group in [(NMe2)3TaC2B9H11] with chloride to give [Cl(NMe2)2TaC2B9H11] is also discussed.

23

Welsch, T., N. Endlich, W. Kriz, and K. Endlich. "CD2AP and p130Cas localize to different F-actin structures in podocytes." American Journal of Physiology-Renal Physiology 281, no. 4 (October 1, 2001): F769—F777. http://dx.doi.org/10.1152/ajprenal.2001.281.4.f769.

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Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms. CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas. In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes. In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes. In addition, p130Cas was strongly expressed in mesangial cells. Immunoelectron microscopy demonstrated that CD2AP was present in podocyte foot processes without a prevailing localization. In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends. In contrast, CD2AP colocalized with F-actin at the leading edge of lamellipodia and in small spots, which were unevenly distributed in the cytoplasm. The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly. Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1. Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions. Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.

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Furusawa, Kotaro, Toshiyuki Takasugi, Yung-Wen Chiu, Yukiko Hori, Taisuke Tomita, Mitsunori Fukuda, and Shin-ichi Hisanaga. "CD2-associated protein (CD2AP) overexpression accelerates amyloid precursor protein (APP) transfer from early endosomes to the lysosomal degradation pathway." Journal of Biological Chemistry 294, no. 28 (May 28, 2019): 10886–99. http://dx.doi.org/10.1074/jbc.ra118.005385.

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A hallmark of Alzheimer's disease (AD) pathology is the appearance of senile plaques, which are composed of β-amyloid (Aβ) peptides. Aβ is produced by sequential cleavages of amyloid precursor protein (APP) by β- and γ-secretases. These cleavages take place in endosomes during intracellular trafficking of APP through the endocytic and recycling pathways. Genome-wide association studies have identified several risk factors for late-onset AD, one of which is CD2-associated protein (CD2AP), an adaptor molecule that regulates membrane trafficking. Although CD2AP's involvement in APP trafficking has recently been reported, how APP trafficking is regulated remains unclear. We sought to address this question by investigating the effect of CD2AP overexpression or knockdown on the intracellular APP distribution and degradation of APP in cultured COS-7 and HEK293 cells. We found that overexpression of CD2AP increases the localization of APP to Rab7-positive late endosomes, and decreases its localization to Rab5-positive early endosomes. CD2AP overexpression accelerated the onset of APP degradation without affecting its degradation rate. Furthermore, nutrient starvation increased the localization of APP to Rab7-positive late endosomes, and CD2AP overexpression stimulated starvation-induced lysosomal APP degradation. Moreover, the effect of CD2AP on the degradation of APP was confirmed by CD2AP overexpression and knockdown in primary cortical neurons from mice. We conclude that CD2AP accelerates the transfer of APP from early to late endosomes. This transfer in localization stimulates APP degradation by reducing the amount of time before degradation initiation. Taken together, these results may explain why impaired CD2AP function is a risk factor for AD.

25

Kisiel, Zbigniew, Lech Pszczółkowski, Laura B. Favero, and Walther Caminati. "Rotational Spectrum of CD2I2." Journal of Molecular Spectroscopy 189, no. 2 (June 1998): 283–90. http://dx.doi.org/10.1006/jmsp.1998.7556.

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26

Grunkemeyer, James A., Christopher Kwoh, Tobias B. Huber, and Andrey S. Shaw. "CD2-associated Protein (CD2AP) Expression in Podocytes Rescues Lethality of CD2AP Deficiency." Journal of Biological Chemistry 280, no. 33 (June 10, 2005): 29677–81. http://dx.doi.org/10.1074/jbc.m504004200.

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Yuan, Huaiping, Emiko Takeuchi, and David J. Salant. "Podocyte slit-diaphragm protein nephrin is linked to the actin cytoskeleton." American Journal of Physiology-Renal Physiology 282, no. 4 (April 1, 2002): F585—F591. http://dx.doi.org/10.1152/ajprenal.00290.2001.

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Nephrin is an Ig-like transmembrane protein. It is a major component of the podocyte slit diaphragm and is essential for maintaining normal glomerular permeability. CD2-associated protein (CD2AP) is also necessary for normal glomerular permeability and is a putative nephrin adapter molecule. Here, we document that nephrin and CD2AP are linked to the actin cytoskeleton. As detected by Western blot analysis, nephrin and CD2AP were both insoluble when cell membranes from normal rat glomeruli were extracted with 0.5% Triton X-100 (TX-100) at 4°C in the presence of divalent cations, but they were solubilized when the extraction included potassium iodide (KI) to depolymerize F-actin. In addition, a small fraction of the solubilized nephrin and CD2AP was recovered in the low-density fractions of OptiPrep flotation gradients, which indicates that a portion of nephrin, possibly associated with CD2AP, resides in a cholesterol- or sphingolipid-rich region of the plasma membrane. Immunofluorescent staining of unfixed sections of normal rat kidney for nephrin, CD2AP, and F-actin was unaltered by treatment with TX-100 but was greatly diminished by addition of KI. Nephrin staining was slightly reduced by cholesterol depletion with methyl-β-cyclodextrin in the presence of TX-100 but was nearly absent after addition of KI. These results document that nephrin anchors the slit diaphragm to the actin cytoskeleton, possibly by linkage to CD2AP, and that nephrin traverses a relatively cholesterol-poor region of the podocyte plasma membrane. In addition, a small pool of actin-associated nephrin and CD2AP resides in lipid rafts, possibly in the cholesterol-rich apical region of the podocyte-foot processes.

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Tang, Vivian W., and William M. Brieher. "FSGS3/CD2AP is a barbed-end capping protein that stabilizes actin and strengthens adherens junctions." Journal of Cell Biology 203, no. 5 (December 9, 2013): 815–33. http://dx.doi.org/10.1083/jcb.201304143.

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By combining in vitro reconstitution biochemistry with a cross-linking approach, we have identified focal segmental glomerulosclerosis 3/CD2-associated protein (FSGS3/CD2AP) as a novel actin barbed-end capping protein responsible for actin stability at the adherens junction. FSGS3/CD2AP colocalizes with E-cadherin and α-actinin-4 at the apical junction in polarized Madin-Darby canine kidney (MDCK) cells. Knockdown of FSGS3/CD2AP compromised actin stability and decreased actin accumulation at the adherens junction. Using a novel apparatus to apply mechanical stress to cell–cell junctions, we showed that knockdown of FSGS3/CD2AP compromised adhesive strength, resulting in tearing between cells and disruption of barrier function. Our results reveal a novel function of FSGS3/CD2AP and a previously unrecognized role of barbed-end capping in junctional actin dynamics. Our study underscores the complexity of actin regulation at cell–cell contacts that involves actin activators, inhibitors, and stabilizers to control adhesive strength, epithelial behavior, and permeability barrier integrity.

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Yu-Shengyou and Yu Li. "Dexamethasone Inhibits Podocyte Apoptosis by Stabilizing the PI3K/Akt Signal Pathway." BioMed Research International 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/326986.

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Corticosteroids like dexamethasone (DEX) are well-established treatments for the glomerular disease that sustain renal function, at least in part, by protecting podocytes from apoptotic death. In this study, we found that PAN causes abnormal expression of the PI3K-binding protein CD2AP, reducing PI3K/Akt signaling and promoting podocyte apoptosis. In contrast, DEX restores CD2AP-PI3K-Akt-GSK3βsignaling, which promotes the activity of antiapoptotic proteins and inhibits the activity of proapoptotic proteins. In addition, we also found that CD2AP was aberrantly colocalized with p85. Normal CD2AP mRNA expression and subcellular protein distribution were maintained in the PAN + DEX group, and DEX coapplication also reduced CD2AP-p85 colocalization. PAN evoked a concentration-dependent decrease in p-Akt and p-GSK3βexpressions, with p-Akt expression reaching a nadir at 15 min and p-GSK3βexpression at 30 min. DEX treatment induced a concentration-dependent reversal of PAN-induced p-Akt and p-GSK3βdownregulation. The PI3K inhibitor LY294002 blocked p-Akt and p-GSK3βexpressions in podocytes. Cells treated with PAN exhibited a significantly higher apoptosis rate than untreated or vehicle-treated cells. Furthermore, LY294002 exacerbated PAN-induced apoptosis. DEX cotreatment caused a significant concentration-dependent decrease in PAN-induced apoptosis. These results strongly suggest that DEX protects podocytes by stabilizing the expression and subcellular distribution of CD2AP and by maintaining the expression of phosphor-activated Akt and GSK3β.

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Karataeva, F. Kh, I. Z. Rakhmatullin, N. F. Galiullina, and V. V. Klochkov. "Structure and Intramolecular Mobility of Some Derivatives of Bis(thio)phosphorylated Amides in CCL4, CD2CL2, and CD3CN Solutions." Uchenye Zapiski Kazanskogo Universiteta. Seriya Estestvennye Nauki 165, no. 1 (2023): 149–57. http://dx.doi.org/10.26907/2542-064x.2023.1.149-157.

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The structure and intramolecular mobility of some derivatives of bis(thio)phosphorylated amides in CCl4, CD2Cl2, and CD3CN solutions were examined by 1H and 31P NMR spectroscopy. A comparative analysis of the temperature-dependent 1H and 31P NMR spectra of the studied compounds with symmetric and asymmetric substitution at phosphorus atoms was carried out. Various intramolecular processes were identified – rotation around C-N bonds, conformational transformations of molecules, tautomerism, and phosphorylotropic rearrangement with the formation of various conformational forms. It was shown that a dynamic equilibrium of several forms is reached, with the amide (phosphazo-) form having a clear advantage.

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Rollins-Raval, Marian A., Kimberly Fuhrer, Teresa Marafioti, and Christine G. Roth. "ALDH, CA I, and CD2AP." American Journal of Clinical Pathology 137, no. 1 (January 2012): 30–38. http://dx.doi.org/10.1309/ajcp0qfq0ftszcpw.

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Gelmez, Metin Yusuf, Kaya Köksalan, Suzan Çınar, Nevin Hatipoğlu, Taner Coşkuner, Zehra Topkarcı, Selda Hançerli Törün та ін. "IFN-γR1 (CD119) ve IL-12Rβ1 (CD212) Eksikliğinin Akan Hücre Ölçer ile Analizi". Mikrobiyoloji Bulteni 57, № 1 (9 січня 2023): 83–96. http://dx.doi.org/10.5578/mb.20239907.

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Belland, P., and M. Fourrier. "Submillimeter emission lines from CD2Cl2 optically pumped lasers." International Journal of Infrared and Millimeter Waves 7, no. 8 (August 1986): 1251–56. http://dx.doi.org/10.1007/bf01011103.

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34

Shah, Nirali N., Maureen Megan O'Brien, Constance Yuan, Lingyun Ji, Xinxin Xu, Susan R. Rheingold, Deepa Bhojwani, et al. "Evaluation of CD22 modulation as a mechanism of resistance to inotuzumab ozogamicin (InO): Results from central CD22 testing on the Children’s Oncology Group (COG) phase II trial of INO in children and young adults with CD22+ B-acute lymphoblastic leukemia (B-ALL)." Journal of Clinical Oncology 38, no. 15_suppl (May 20, 2020): 10519. http://dx.doi.org/10.1200/jco.2020.38.15_suppl.10519.

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10519 Background: The COG AALL1621 phase 2 trial evaluated the efficacy of InO in children and young adults with relapsed/refractory CD22+ B-cell ALL. We report results of central surface CD22 expression on ALL and impact on response. Methods: Optional central CD22 testing was performed on bone marrow and/or peripheral blood at the NCI flow cytometry (FC) laboratory pre/post cycle 1. Percentage of blasts with CD22+ expression (CD22%) was measured by multiparameter FC and the BD Biosciences QuantiBRITE system quantified the CD22 site density by measuring CD22 antibody bound per cell (ABC). Comparison of ABC and CD22% between subgroups was based on Wilcoxon rank sum test or signed rank test as appropriate. Post-treatment CD22 assessments could only be performed on those with residual ALL. Results: Amongst 48 patients, 28 (58.3%) achieved a complete response (CR) or CR with incomplete count recovery. The median CD22 ABC, pre and post-cycle 1, was 2688 (range, 290-10715, n = 33) and 1098 (184-6822, n = 15) respectively. Amongst 27 subjects with paired pre/post samples, median pre-treatment CD22 ABC was lower in those with residual ALL (n = 13) than in those without residual ALL (ABC 1005 (290-8848) vs ABC 4123 (762-10715), p = 0.003). Baseline CD22% ranged more widely in those with residual ALL, median 99% (40-100%) vs. 99% (92.9-100%, no residual ALL) p = 0.025; and significant decreases in CD22% were seen compared to baseline in those with residual ALL, with median post-treatment CD22% 82% (1.4%-100%), p = 0.007. Amongst 3 subjects with baseline partial CD22% (40%, 79% and 83% partial CD22+ populations), post-cycle 1 evaluations revealed emergence of predominantly CD22 negative populations (6.5%, 34% and 48% CD22+, respectively), precluding eradication of minimal residual disease. Amongst those with KMT2A rearrangement, 2 of 4 had partial CD22 expression and 4 of 4 had low ABC ( < 1500). Conclusions: Baseline CD22 expression, specifically low CD22 ABC and partial CD22% were significantly associated with response to treatment, emerging as potential biomarkers for poor InO response. This is particularly relevant to patients with KMT2Arearrangement who may be predisposed to CD22 partial positivity and low ABC. Evolution of CD22 negative/dim disease post-therapy suggests CD22 modulation is a mechanism of resistance to InO. Response to InO monotherapy may be limited in those with baseline CD22 negative/dim populations. Clinical trial information: NCT02981628.

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Engel, P., Y. Nojima, D. Rothstein, L. J. Zhou, G. L. Wilson, J. H. Kehrl, and T. F. Tedder. "The same epitope on CD22 of B lymphocytes mediates the adhesion of erythrocytes, T and B lymphocytes, neutrophils, and monocytes." Journal of Immunology 150, no. 11 (June 1, 1993): 4719–32. http://dx.doi.org/10.4049/jimmunol.150.11.4719.

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Abstract CD22 is a B lineage-restricted member of the Ig superfamily that serves as an adhesion receptor expressed by mature B lymphocytes. In this study, the ability of different cell types to attach to COS cells transiently transfected with a full-length CD22 cDNA (COS-CD22) was examined to determine the cellular distribution of the ligand for CD22. T and B lymphocytes, monocytes, erythrocytes, and neutrophils formed specific rosettes with COS-CD22 cells at 4 degrees C. A panel of 33 new mAb directed against CD22 were developed to examine the regions of CD22 that mediate adhesion. Four of these mAb, HB22-7, -22, -23, and -33 (at 1 to 5 micrograms/ml) specifically blocked adhesion (75 to 95%) of all cell types to COS-CD22 cells. Each of these mAb cross-blocked each other's binding, suggesting that ligand binding occurs through a single region of CD22. These mAb also identify a region of CD22 distinct from those defined by previously described CD22 mAb. CD22-mediated adhesion of cell lines to COS-CD22 cells was independent of CD45RO and CDw75 expression, and it was not inhibited by mAb against known integrins. Although alpha-2,6-linked sialic acid expressed on the surface of COS cells did not serve as a ligand for CD22, the CD22 ligand may contain a critical sialic acid determinant, as neuraminidase treatment of all target cells eliminated CD22-mediated adhesion. CD22-mediated adhesion was Ca2+/Mg2+ independent, again suggesting that integrins were not involved. An inhibitory substance for CD22-mediated adhesion was found to be present in FCS and some ascites fluid. Analysis of CD22 mRNA and protein revealed that although multiple mRNA splice variants of CD22 mRNA can be detected, only a single protein isoform was detected on the cell surface. Therefore, although the identity of the CD22 ligands remains incompletely characterized, it is possible that a single major ligand is expressed by RBC and leukocytes, which binds to a single region of CD22.

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Fujimoto, Manabu, Maki Odaka, Minoru Hasegawa, and Kazuhiko Takehara. "Autoantibody-mediated regulation on B cell responses by functional anti-CD22 autoantibodies in patients with systemic sclerosis (137.42)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 137.42. http://dx.doi.org/10.4049/jimmunol.182.supp.137.42.

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Abstract Objectives. Studies have demonstrated that B cells play important roles in systemic sclerosis (SSc), especially through the gCD19/CD22 autoimmune loop h. In this study, we examined the presence and functional property of circulating autoantibodies reacting with CD22. Methods. Serum samples from 10 tight skin (TSK/+) mice and 50 SSc patients were assessed for anti-CD22 autoantibodies by enzyme-linked immunosorbent assays using recombinant mouse or human CD22. The association between anti-CD22 antibodies and clinical features was also investigated in SSc patients. Furthermore, the influence of SSc serum including anti-CD22 autoantibodies for CD22 tyrosine phosphorylation was examined by western blotting using phospho-tyrosine specific antibodies reacting with four major tyrosine motifs of CD22 cytoplasmic domain. Results. Anti-CD22 autoantibodies were positive in 80% of TSK/+ mice and in 22% of SSc patients. Patients positive for anti-CD22 antibodies showed significantly higher modified Rodnan skin thickness score compared with patients negative for anti-CD22 antibodies. Furthermore, anti-CD22 antibodies from patients' sera were capable of reducing phosphorylation of all four CD22 tyrosine motifs, while sera negative for anti-CD22 antibodies did not affect CD22 phosphorylation. Conclusions. A subset of SSc patients possessed autoantibodies reacting with a major inhibitory B cell response regulator, CD22. Since these antibodies can interfere CD22-mediated suppression onto B cell activation in vitro, SSc B cells produce functional autoantibodies that can enhance their own activation. This unique regulation may contribute to the autoimmune aspect of SSc.

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Xie, Dong, Rong Deng, Jakub Baudys, Pam Chan, Randy Dere, Allen Ebens, Paul Fielder, et al. "Pharmacokinetics of Anti-CD22 Antibody Conjugates with Uncleavable and Cleavable Linkers in Rats." Blood 110, no. 11 (November 16, 2007): 2361. http://dx.doi.org/10.1182/blood.v110.11.2361.2361.

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Abstract CD22 is a B cell specific antigen and is expressed in Non-Hodgkin lymphoma (NHL) with limited expression on normal tissues. Currently, we are evaluating anti-CD22 antibody drug conjugates (anti-CD22 ADC) consisting of a humanized monoclonal IgG antibody conjugated to mitotic inhibitors such as DM1 (a maytansinoid), Monomethylauristatin F (MMAF), or Monomethylauristatin E (MMAE). The antibody binds to human and cynomolgus monkey CD22, but does not bind to rodent CD22. The cytotoxic drugs were conjugated to the antibody via uncleavable linkers (MCC-DM1, MC-MMAF) or cleavable linkers (SPP-DM1, vc-MMAE). These conjugates have demonstrated anti-tumor activity in mouse xenograft models of human B-cell tumors. This study was to assess and to compare the antigen-independent pharmacokinetics of anti-CD22 ADCs with uncleavable linkers (anti-CD22-MCC-DM1 and anti-CD22-MC-MMAF) and cleavable linkers (anti-CD22-SPP-DM1 and anti-CD22-vc-MMAE) in rats, and to support a pilot rat safety study. Following a single IV dose, the anti-CD22 ADCs exhibited a biphasic disposition profile. The conjugates with cleavable linkers had faster clearance compared to those with uncleavable linkers (59.4 mL/day/kg for anti-CD22-SPP-DM1 vs. 18.0 mL/day/kg for anti-CD22-MCC-DM1). The faster clearance for anti-CD22 ADCs with cleavable linker has also been observed with other ADCs (different target). In addition, it was found that free DM1 in plasma that was deconjugated from anti-CD22-SPP-DM1 had ∼70 fold higher exposure compared with that from anti-CD22-MCC-DM1 (area under curve (AUC) for free DM1 in plasma: 562 day*ng/mL for anti-CD22-SPP-DM1 vs. 8.18 day*ng/mL for anti-CD22-MCC-DM1). Furthermore, anti-CD22-SPP-DM1 had a different DM1 release profile compared with anti-CD22-MCC-DM1 when incubated with human plasma in vitro. Maximum concentrations of free DM1 were reached at ∼6 hr and ∼24 hr for anti-CD22-SPP-DM1 and anti-CD22-MCC-DM1, respectively. These observations were consistent with the safety findings in rats: anti-CD22-SPP-DM1 had greater toxicity (body weight loss, renal toxicity) compared with anti-CD22-MCC-DM1. The data described here indicate that the anti-CD22 ADCs with uncleavable linkers are cleared slower than, and have a better safety profile than the conjugates with cleavable linkers.

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Yang, Hailin, and Ellis L. Reinherz. "CD2BP1 Modulates CD2-Dependent T Cell Activation via Linkage to Protein Tyrosine Phosphatase (PTP)-PEST." Journal of Immunology 176, no. 10 (May 2, 2006): 5898–907. http://dx.doi.org/10.4049/jimmunol.176.10.5898.

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Wu, Guozhen. "Global topological approach to highly excited vibration: a case study of H2O, CH2Br2 and CD2Br2." Chemical Physics Letters 270, no. 5-6 (May 1997): 453–63. http://dx.doi.org/10.1016/s0009-2614(97)00401-6.

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Carvalho, Jerusa Martins, Marlon Knabben de Souza, Valéria Buccheri, Cláudia Viviane Rubens, José Kerbauy, and José Salvador Rodrigues de Oliveira. "CD34-positive cells and their subpopulations characterized by flow cytometry analyses on the bone marrow of healthy allogenic donors." Sao Paulo Medical Journal 127, no. 1 (January 2009): 12–18. http://dx.doi.org/10.1590/s1516-31802009000100004.

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CONTEXT AND OBJECTIVE: Counting and separating hematopoietic stem cells from different sources has importance for research and clinical assays. Our aims here were to characterize and quantify hematopoietic cell populations in marrow donors and to evaluate CD34 expression and relate this to engraftment. DESIGN AND SETTING: Cross-sectional study on hematopoietic stem cell assays, using flow cytometry on donor bone marrow samples, for allogenic transplantation patients at two hospitals in São Paulo. METHODS: Immunophenotyping of marrow cells was performed in accordance with positive findings of CD34FITC, CD117PE, CD38PE, CD7FITC, CD33PE, CD10FITC, CD19PE, CD14FITC, CD13PE, CD11cPE, CD15FITIC, CD22PE, CD61FITC and CD56PE monoclonal antibodies in CD45PerCP+ cells, searching for differentiation and maturation regions. CD34+ sorting cells were analyzed for CD38 and CD117. Rh-123 retention was done before and after sorting. Antigen expression and CD34+ cells were correlated with engraftment. RESULTS: In region R1, 0.1% to 2.8% of cells were CD34+/CD45+ and 1.1%, CD34+/CD45-. The main coexpressions of CD45+ cells were CD38, CD22, CD19 and CD56 in R2 and CD33, CD11c, CD14, CD15 and CD61 in R3 and R4. After sorting, 2.2x10(6) CD34+ cells were equivalent to 4.9% of total cells. Coexpression of CD34+/CD38+ and CD34+/CD117+ occurred in 94.9% and 82% of events, respectively. There was a positive relationship between CD34+ cells and engraftment. More than 80% of marrow cells expressed high Rh-123. CD34+ cell sorting showed that cells in regions of more differentiated lineages retained Rh-123 more intensively than in primitive lineage regions. CONCLUSION: We advocate that true stem cells are CD34+/CD45-/CD38-/low-Rh-123 accumulations.

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Huber, Tobias B., Björn Hartleben, Jeong Kim, Miriam Schmidts, Bernhard Schermer, Alexander Keil, Lotti Egger, et al. "Nephrin and CD2AP Associate with Phosphoinositide 3-OH Kinase and Stimulate AKT-Dependent Signaling." Molecular and Cellular Biology 23, no. 14 (July 15, 2003): 4917–28. http://dx.doi.org/10.1128/mcb.23.14.4917-4928.2003.

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ABSTRACT Mutations of NPHS1 or NPHS2, the genes encoding nephrin and podocin, as well as the targeted disruption of CD2-associated protein (CD2AP), lead to heavy proteinuria, suggesting that all three proteins are essential for the integrity of glomerular podocytes, the visceral glomerular epithelial cells of the kidney. It has been speculated that these proteins participate in common signaling pathways; however, it has remained unclear which signaling proteins are actually recruited by the slit diaphragm protein complex in vivo. We demonstrate that both nephrin and CD2AP interact with the p85 regulatory subunit of phosphoinositide 3-OH kinase (PI3K) in vivo, recruit PI3K to the plasma membrane, and, together with podocin, stimulate PI3K-dependent AKT signaling in podocytes. Using two-dimensional gel analysis in combination with a phosphoserine-specific antiserum, we demonstrate that the nephrin-induced AKT mediates phosphorylation of several target proteins in podocytes. One such target is Bad; its phosphorylation and inactivation by 14-3-3 protects podocytes against detachment-induced cell death, suggesting that the nephrin-CD2AP-mediated AKT activity can regulate complex biological programs. Our findings reveal a novel role for the slit diaphragm proteins nephrin, CD2AP, and podocin and demonstrate that these three proteins, in addition to their structural functions, initiate PI3K/AKT-dependent signal transduction in glomerular podocytes.

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Yates, Bonnie, Haneen Shalabi, Dalia Salem, Cynthia Delbrook, Constance M. Yuan, Maryalice Stetler-Stevenson, Terry J. Fry, and Nirali N. Shah. "Sequential CD22 Targeting Impacts CD22 CAR-T Cell Response." Blood 132, Supplement 1 (November 29, 2018): 282. http://dx.doi.org/10.1182/blood-2018-99-119621.

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Abstract Background: With advances in immunotherapeutic approaches and the recognition of antigen modulation as a mechanism of relapse, it is imperative to understand the impact of sequential targeting strategies and the role it may have on outcomes of future therapies to optimize timing of therapeutic interventions. We previously reported on the safety, feasibility, and efficacy on our phase I dose escalation anti-CD22 CAR protocol (clinicaltrials.gov/NCT02315612).1 Based on our initial experience, we identified CD22 loss or diminution of CD22 as a risk factor for relapse following CD22 directed CAR therapy. With development of other CD22 directed therapies, we retrospectively analyzed impact of prior CD22 targeted therapy on response to CD22 CAR in our ongoing clinical trial. Design: Children and young adults with relapsed/refractory CD22+ hematologic malignancies eligible for our phase I dose escalation anti-CD22 CAR protocol were enrolled on study (Clinicaltrials.gov NCT02315612). All had bone marrow evaluations at baseline, prior to lympho-depleting chemotherapy (Fludarabine 25 mg/m2 x 3 days and Cyclophosphamide 900 mg/m2 x 1 day) and again at day 28 (+/- 4 days) post-CAR infusion. We retrospectively analyzed the impact of prior CD22 directed therapy on outcomes following CD22 CAR and specifically looked at the variables of CD22 antigen expression prior to CAR infusion (% positive and antigen density) and compared responses to CD22 CAR for those who did and did not receive prior CD22 targeted therapy. Results: From December 2014 to July 2018, 43 subjects with ALL were treated. All had active bone marrow involvement at baseline, the majority with an M2 marrow (>5% blasts) or higher disease burden. 34 had a prior transplant and 26 were previously treated with CD19 CAR. Fourteen subjects had received prior CD22 directed therapy, including CD22 CAR elsewhere (n=2) or inotuzumab ozagamicin (Ino) (n=13). Subjects received a median of 3 doses of Ino (3-6 doses) and the median time from last Ino exposure was 2 months (range 1-20 months). Median CD22 antigen expression on bone marrow leukemic blasts prior to planned lymphodepletion for those who had received prior CD22 therapy compared to those who did not was 2527 (882-9079) vs 3929 (846-13452), respectively (one-tailed p=0.05, Figure 1). (Figure 1). Complete remission (CR) rates following CAR-T infusion for those who had prior CD22 directed therapy compared to those who did not was 57% and 71%, respectively with MRD negativity by flow cytometry achieved in only 5/8 (62.5%) patients versus 18/20 (90%) respectively and residual disease in those not achieving MRD negativity was CD22 dim. Both subjects who had received prior CD22 CAR elsewhere were non-responders to our construct with a first-infusion, however one subject converted to a CR with an intensified lymphodepletion and a second infusion. Two subjects who had received prior Ino were noted to have partial CD22 expression on at least one time point (69-89% positivity) prior to enrollment. One of these patients with pre-existing CD22 partial positivity (69% positivity) had evidence for CAR-T cell expansion but had residual low CD22 expressing disease at restaging. Notably, another subject who received 6 doses of Ino prior to receiving CD22 CAR T-cells and had uniformly CD22+ disease at enrollment, emerged with CD22 negative disease following CD22 CAR. Durability of remission also significantly differed amongst the two groups. Median time to relapse in patients who received prior CD22 directed therapy was 2 months (range 2-5 months) versus 6 months (range 2-13 months) for those who did not receive prior CD22 targeted therapy, with the majority relapsing with CD22 negative disease. Conclusion: Sequential targeting of CD19 has anecdotally increased the possibility of CD19 negative relapses, and our data provide evidence for a similar phenomenon with sequential targeting of CD22. Most notably, CD22 expression in patients who had received prior CD22 targeted therapies was lower compared to those who did not. This may have ultimately contributed to both of the observed findings of decreased response rates and decreased durability of remission, the majority of whom relapsed with CD22 negative disease following sequential targeting. This observation contributes to the increasing fund of knowledge regarding optimization of targeted therapies. Disclosures No relevant conflicts of interest to declare.

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Zastrow, Alexi, David J. Friedman, Sydney B. Crotts, Matthew Rajcula, Brady Hammer, Mai Elissa, and Virginia Smith Shapiro. "Understanding the role of CD22 on Macrophage and Dendritic Cell Function." Journal of Immunology 210, no. 1_Supplement (May 1, 2023): 72.08. http://dx.doi.org/10.4049/jimmunol.210.supp.72.08.

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Abstract At the terminal position of many glycan chains are unique sugars known as sialic acids. Sialic acids bind sialic acid immunoglobin-like lectins (Siglecs). Our lab is interested in the role of CD22 (Siglec-2), which binds to α2,6-linked sialic acid generated by ST6GalI. CD22 can associate with itself or other molecules on the same cells in a “cis” configuration or bind in “trans” with ligands on other cells. CD22 contains four ITIMs within its cytoplasmic tail and is primarily known to function as an inhibitory co-receptor of the B cell receptor (BCR). CD22-ligand interactions restrain CD22 and BCR association which dampens BCR signaling. While CD22 is usually characterized as a B cell specific protein, we found that CD22 is highly expressed in hybrid macrophages (CD11b+ CD11c+ F4/80+) and expression decreases with activation, implying that CD22 may modulate myeloid cell responses. Using novel macrophage and dendritic cell-specific CD22 cKO mouse models, we will explore how CD22 impacts myeloid cell activation. We propose that CD22 impacts myeloid cell function and modulating this interaction may improve immune responses.

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Sherbina, N. V., P. S. Linsley, S. Myrdal, L. S. Grosmaire, J. A. Ledbetter, and G. L. Schieven. "Intracellular CD22 rapidly moves to the cell surface in a tyrosine kinase-dependent manner following antigen receptor stimulation." Journal of Immunology 157, no. 10 (November 15, 1996): 4390–98. http://dx.doi.org/10.4049/jimmunol.157.10.4390.

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Abstract CD22 is a key accessory molecule for Ag receptor signaling in B cells that becomes tyrosine phosphorylated in the signaling process. CD22 associates with sIg and strongly amplifies sIg-induced signals. During B cell development, CD22 is initially expressed intracellularly, with surface expression appearing with IgD expression. We used confocal laser-scanning microscopy and flow cytometry to analyze CD22 translocation responses to signaling events. Cross-linking surface IgM (sIgM) induced rapid movement of CD22 to the cell surface in both Ramos and Daudi B cells, with a 50 to 100% increase in surface expression observed within 5 min of stimulation. The increase in CD22 surface expression was specific in that CD19 expression was not affected. Both cell surface and intracellular CD22 were directed toward the site of sIgM stimulation. Treatment with the phosphotyrosine phosphatase inhibitor bis(maltolato)oxovanadium(IV) also increased CD22 surface expression. The tyrosine kinase inhibitor tyrphostin A10 inhibited CD22 movement at concentrations that inhibited tyrosine phosphorylation of CD22 and other cellular proteins. In contrast to the B cell lines, mature peripheral blood B cells contained very little intracellular CD22 and showed no significant increase in surface expression following sIgM stimulation. The rapid directed movement of intracellular CD22 provides a new mechanism to dynamically regulate Ag receptor signaling, as well as CD22-mediated adhesion.

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Jin, Lei, Paul A. McLean, Benjamin G. Neel, and Henry H. Wortis. "Sialic Acid Binding Domains of CD22 Are Required For Negative Regulation of B Cell Receptor Signaling." Journal of Experimental Medicine 195, no. 9 (April 29, 2002): 1199–205. http://dx.doi.org/10.1084/jem.20011796.

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CD22, a negative regulator of B cell antigen receptor signaling, binds glycoconjugates terminating in α2, 6 sialic acid. The physiological ligand(s) for CD22 remain unknown. We asked whether the sialic acid binding domains are necessary for CD22 to function as a negative regulator. We generated two mutants that lack sialic acid binding activity and expressed them in a novel CD22−/− murine B cell line. Anti-IgM activated B cells expressing either CD22 mutant had greater Ca2+ responses than cells expressing wild-type CD22. Each variant also had reduced CD22 tyrosine phosphorylation and Src homology 2 domain–containing protein tyrosine phosphatase-1 association. These data suggest that the α2, 6 sialic acid ligand binding activity of CD22 is critical for its negative regulatory functions.

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Poe, Jonathan C., Evgueni I. Kountikov, and Thomas F. Tedder. "BCR-induced cell death of B cells from CD22 deficient mice is mediated by a novel ssRNA-directed endonuclease (136.33)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 136.33. http://dx.doi.org/10.4049/jimmunol.182.supp.136.33.

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Abstract B cells from CD22 deficient mice backcrossed onto a C57BL/6 genetic background (B6 CD22-/-) undergo B cell antigen receptor (BCR)-induced apoptosis. By contrast, B cells from parental inbred CD22-/- mice on a mixed B6x129 genetic background (B6/129 CD22-/-) survive and proliferate normally following BCR ligation. Through an extensive reverse genetic screen, a single locus was identified as being responsible for the proliferation defect of B6 CD22-/- B cells. In B6 CD22-/- mice this locus was homozygous for B6 germline DNA (locusB6), and in B6/129 CD22-/- mice this region was homozygous for 129 germline DNA (locus129). In locusB6 CD22-/- B cells, a novel single-stranded RNA (ssRNA)-directed endonuclease was specifically overexpressed compared to locus129 CD22-/- B cells, suggesting a direct role in BCR-induced cell death. Targeted disruption of the endonuclease gene in locusB6 CD22-/- mice restored BCR-mediated B cell survival and proliferation to normal levels. These results identify a novel ssRNA-directed endonuclease as a potent inhibitor of B cell survival when expressed following antigen receptor stimulation. This research was supported by NIH grant R01CA096547.

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Pezzutto, A., P. S. Rabinovitch, B. Dörken, G. Moldenhauer, and E. A. Clark. "Role of the CD22 human B cell antigen in B cell triggering by anti-immunoglobulin." Journal of Immunology 140, no. 6 (March 15, 1988): 1791–95. http://dx.doi.org/10.4049/jimmunol.140.6.1791.

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Abstract As B cells mature during ontogeny the CD22 human differentiation Ag is exported from the cytoplasm onto the membrane. Surface expression is lost in terminal differentiation and after activation. In tonsils, CD22 is expressed on the surface of 60 to 80% of the dense B cells. Some IgM+ dense cells, however, and buoyant in vivo activated B cells are CD22-. This differential expression of CD22 and the finding that an anti-CD22 mAb augmented anti-Ig induced B cell proliferation suggested that CD22 may play a role in B cell activation. In this study we have found that CD22+ but not CD22- B cells could be triggered by anti-IgM or anti-IgD to have increased free intracellular calcium ([Ca2+]i). The presence of CD22 rather than of IgD seems to determine the ability of B cells to respond to anti-Ig with a [Ca2+]i flux. Also the proliferative response to anti-Ig or anti-Ig + B cell growth factor was restricted to the CD22+ population. Anti-CD22 mAb, although not inducing [Ca2+]i on their own after binding to B cells, did augment [Ca2+]i fluxes by anti-Ig when cross-linked. Together these results suggest that CD22 may regulate triggering of B cells through surface Ig perhaps by acting as a "bridge" to transmit an early signal into the cytoplasm.

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Boue, DR, and TW LeBien. "Expression and structure of CD22 in acute leukemia." Blood 71, no. 5 (May 1, 1988): 1480–86. http://dx.doi.org/10.1182/blood.v71.5.1480.1480.

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Abstract The purpose of this study was to examine the expression and structure of CD22 in B cell precursor acute lymphoblastic leukemia (BCP-ALL), acute myeloid leukemia (AML), and T cell acute lymphoblastic leukemia (T-ALL). By using immunofluorescence microscopy and flow cytometry we observed that CD22 is expressed not only in the cytoplasm (as previously reported) but also on the cell surface of virtually all (15/16) BCP-ALL examined. CD22 that was biosynthetically labeled with 35S-cysteine and immunoprecipitated from the uncommon cytoplasmic CD22- positive/surface CD22-negative BCP-ALL cells was analyzed by single- dimension sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Our results indicated that the cytoplasmic form of CD22 comigrated with 125I/lactoperoxidase-labeled surface CD22. Therefore, cytoplasmic CD22 is probably a pool of fully processed glycoprotein. We also observed unusual cases of AML (approximately 20%) that expressed cytoplasmic CD22 based on immunofluorescent staining; however, biosynthetic labeling and immunoprecipitation revealed an apparently cross-reactive protein(s) of approximately 250 to 300 kd in AML cells. No T-ALL cell lines examined expressed either cytoplasmic or surface CD22. Thus, cytoplasmic and surface expression of bona fide CD22 appears restricted to B cells, which suggests that this molecule subserves a function unique to B cells.

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Boue, DR, and TW LeBien. "Expression and structure of CD22 in acute leukemia." Blood 71, no. 5 (May 1, 1988): 1480–86. http://dx.doi.org/10.1182/blood.v71.5.1480.bloodjournal7151480.

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The purpose of this study was to examine the expression and structure of CD22 in B cell precursor acute lymphoblastic leukemia (BCP-ALL), acute myeloid leukemia (AML), and T cell acute lymphoblastic leukemia (T-ALL). By using immunofluorescence microscopy and flow cytometry we observed that CD22 is expressed not only in the cytoplasm (as previously reported) but also on the cell surface of virtually all (15/16) BCP-ALL examined. CD22 that was biosynthetically labeled with 35S-cysteine and immunoprecipitated from the uncommon cytoplasmic CD22- positive/surface CD22-negative BCP-ALL cells was analyzed by single- dimension sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Our results indicated that the cytoplasmic form of CD22 comigrated with 125I/lactoperoxidase-labeled surface CD22. Therefore, cytoplasmic CD22 is probably a pool of fully processed glycoprotein. We also observed unusual cases of AML (approximately 20%) that expressed cytoplasmic CD22 based on immunofluorescent staining; however, biosynthetic labeling and immunoprecipitation revealed an apparently cross-reactive protein(s) of approximately 250 to 300 kd in AML cells. No T-ALL cell lines examined expressed either cytoplasmic or surface CD22. Thus, cytoplasmic and surface expression of bona fide CD22 appears restricted to B cells, which suggests that this molecule subserves a function unique to B cells.

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Jegalian, Armin G., Alan S. Wayne, Robert J. Kreitman, Francis J. Mussai, Ira Pastan, Constance M. Yuan, and Maryalice Stetler-Stevenson. "CD22 Expression in Pediatric B-Lineage Acute Lymphoblastic Leukemia." Blood 114, no. 22 (November 20, 2009): 4119. http://dx.doi.org/10.1182/blood.v114.22.4119.4119.

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Abstract Abstract 4119 While the majority of pediatric patients with newly diagnosed B-lineage acute lymphoblastic leukemia (ALL) are cured with standard chemotherapy regimens, treatment is associated with multiple toxicities, and ALL remains the most frequent cause of cancer mortality in childhood. CD22, a B-lineage surface glycoprotein involved in B cell signaling and adhesion, is expressed in most cases of B-lineage ALL. We are conducting clinical trials of anti-CD22 immunotoxins [RFB4(dsFv)-PE38] for pediatric ALL. To assess eligibility for such targeted therapy, CD22 expression by ALL cells was studied in peripheral blood and/or bone marrow aspirate samples from 50 patients with relapsed ALL. The level of CD22 expression by ALL cells was quantitated by measuring mean anti-CD22 antibody binding per ALL cell (ABC) under saturating conditions using flow cytometry and the BD Biosciences QuantiBRITE system for fluorescence quantitation. Patients ranged in age from 3 to 22 years (median 10 years) and included 27 males and 23 females. CD22 expression was detected in all samples, and the vast majority of cases demonstrated expression of CD22 in 100% of leukemic blasts. CD22 antigen density in ALL cells varied widely among patients at baseline (range 451 - 14,519; mean 4276; median 3824; standard deviation 2976; see graph). CD22-directed immunotoxin therapy was initiated in 29 of the 50 patients, 19 of whom had samples quantitated for CD22 expression levels both before and after immunotoxin therapy. Most patients exhibited limited variation in the mean number of anti-CD22 molecules bound per ALL cell when comparing multiple specimens. In conclusion, CD22 expression varies widely in pediatric B-lineage ALL and persists despite repeated exposure to CD22-directed therapy. (MedImmune, LLC, sponsored the clinical studies of anti-CD22 immunotoxin CAT-8015.) Disclosures: No relevant conflicts of interest to declare.

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