Journal articles: 'FC'

1

Febriyanti, Eka. "FC." Majalah Ilmiah Pengkajian Industri 11, no. 1 (June 5, 2017): i—v. http://dx.doi.org/10.29122/mipi.v11i1.2079.

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Herberhold, Max, Berthold Distler, Heidi Maisel, Wolfgang Milius, Bernd Wrackmeyer, and Piero Zanello. "Ferrocenyl Sulfinylimide and Diferrocenyl Sulfurdiimide, Fc?NSO and Fc(NSN)Fc." Zeitschrift f�r anorganische und allgemeine Chemie 622, no. 9 (September 1996): 1515–23. http://dx.doi.org/10.1002/zaac.19966220913.

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3

Mimoto, F., H. Katada, S. Kadono, T. Igawa, T. Kuramochi, M. Muraoka, Y. Wada, K. Haraya, T. Miyazaki, and K. Hattori. "Engineered antibody Fc variant with selectively enhanced Fc RIIb binding over both Fc RIIaR131 and Fc RIIaH131." Protein Engineering Design and Selection 26, no. 10 (June 5, 2013): 589–98. http://dx.doi.org/10.1093/protein/gzt022.

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4

Yuan, Qianqian, and Hailou Yao. "FC-Projective Comodules and FC-Projective Dimensions." International Journal of Applied Physics and Mathematics 14, no. 1 (2024): 12–19. http://dx.doi.org/10.17706/ijapm.2024.14.1.12-19.

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5

&NA;. "FC Search." Dimensions of Critical Care Nursing 16, no. 5 (September 1997): 256. http://dx.doi.org/10.1097/00003465-199709000-00004.

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6

Dempsey, P. "TV FC." Engineering & Technology 6, no. 6 (July 1, 2011): 76–79. http://dx.doi.org/10.1049/et.2011.0613.

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7

Ravetch, Jeffrey V. "Fc receptors." Current Opinion in Immunology 9, no. 1 (February 1997): 121–25. http://dx.doi.org/10.1016/s0952-7915(97)80168-9.

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8

Ravetch, J. V., and J. P. Kinet. "Fc Receptors." Annual Review of Immunology 9, no. 1 (April 1991): 457–92. http://dx.doi.org/10.1146/annurev.iy.09.040191.002325.

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9

Artemovych, Orest. "$FC$-rings." Miskolc Mathematical Notes 18, no. 2 (2017): 623. http://dx.doi.org/10.18514/mmn.2017.1531.

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10

Traets, Marissa J. M., Kathelijn Fischer, Nanda Uitslager, Paul R. van der Valk, Idske C. L. Kremer Hovinga, Lize F. D. van Vulpen, and Roger E. G. Schutgens. "Real-Life Pharmacokinetics of rFVIII-Fc and rFIX-Fc." TH Open 04, no. 04 (October 2020): e362-e364. http://dx.doi.org/10.1055/s-0040-1718416.

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11

Frank, Martin, Ross C. Walker, William N. Lanzilotta, James H. Prestegard, and Adam W. Barb. "Immunoglobulin G1 Fc Domain Motions: Implications for Fc Engineering." Journal of Molecular Biology 426, no. 8 (April 2014): 1799–811. http://dx.doi.org/10.1016/j.jmb.2014.01.011.

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12

Harridon, Mohd, Mohd Zaharull Hamdan, and Muhd Siv Azhar Merican Abdullah. "Soccer Match Analysis of UniKL FC Versus UPM FC." International Journal of Scientific and Research Publications 13, no. 10 (October 24, 2023): 150–53. http://dx.doi.org/10.29322/ijsrp.13.10.2023.p14224.

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13

Wang, Binghe, and Daniel N. Sauder. "Fc Rγ Represents the Fc Receptor γ Chain Whereas FcγR Means the Fc Receptor for IgG." Journal of Investigative Dermatology 116, no. 2 (February 2001): 350. http://dx.doi.org/10.1038/sj.jid.5600989.

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14

Alber, G., U. M. Kent, and H. Metzger. "Functional comparison of Fc epsilon RI, Fc gamma RII, and Fc gamma RIII in mast cells." Journal of Immunology 149, no. 7 (October 1, 1992): 2428–36. http://dx.doi.org/10.4049/jimmunol.149.7.2428.

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Abstract The cellular responses initiated by cross-linking rodent Fc gamma RII-b1, Fc gamma RII-b2, Fc gamma RIII, and Fc epsilon RI in mast cells were compared. Individual murine Fc gamma R isoforms were transfected into rat basophilic leukemia cells and after cross-linking the FcR, changes in the phosphorylation of protein tyrosines, in the level of intracellular Ca2+, in the hydrolysis of phosphoinositides, and in the release of arachidonic acid metabolites and hexosaminidase were monitored. Cross-linking of Fc gamma RIII initiated all of these early and late biochemical functions, and although they were quantitatively somewhat smaller, the responses were qualitatively indistinguishable from those stimulated by the endogenous Fc epsilon RI. However, despite ample expression, neither Fc gamma RII-b1 nor Fc gamma RII-b2 stimulated these functions when cross-linked. The functional differences between Fc gamma RII and Fc gamma RIII were studied further by assessing the responses to cross-linking of the endogenous Fc gamma R (Fc gamma RII-b1, Fc gamma RII-b2, and Fc gamma RIII) on P815 mouse mastocytoma cells that had been transfected with normal or functionally defective Fc epsilon RI. Two types of mutant subunits had previously been observed to impair the activity of Fc epsilon RI: gamma-chains missing the cytoplasmic domain, and beta-chains missing the COOH-terminal cytoplasmic domain. In both types of transfectants the functional inhibition of the endogenous Fc gamma R paralleled that of the transfected Fc epsilon RI. These results are consistent with the gamma subunit being associated with the functions of Fc gamma RIII as well as of Fc epsilon RI. The functional results also complement the recently reported evidence that Fc gamma RIII can interact with Fc epsilon RI beta-subunits (J. Exp. Med. 175:447, 1992).

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15

Dumont, Jennifer A., Susan C. Low, Robert T. Peters, and Alan J. Bitonti. "Monomeric Fc Fusions." BioDrugs 20, no. 3 (2006): 151–60. http://dx.doi.org/10.2165/00063030-200620030-00002.

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16

Jazayeri, Jalal A., and Graeme J. Carroll. "Fc-Based Cytokines." BioDrugs 22, no. 1 (2008): 11–26. http://dx.doi.org/10.2165/00063030-200822010-00002.

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17

Boyle, M. D. P., and K. J. Reis. "Bacterial Fc Receptors." Nature Biotechnology 5, no. 7 (July 1987): 697–703. http://dx.doi.org/10.1038/nbt0787-697.

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18

Khalili, H., P. T. Khaw, and S. Brocchini. "Fc-fusion mimetics." Biomaterials Science 4, no. 6 (2016): 943–47. http://dx.doi.org/10.1039/c6bm00077k.

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19

Cohen-Solal, J. "Fc γ receptors." Immunology Letters 92, no. 3 (April 15, 2004): 199–205. http://dx.doi.org/10.1016/j.imlet.2004.01.012.

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20

Hogarth, P. Mark. "Fc Receptors: Introduction." Immunological Reviews 268, no. 1 (October 26, 2015): 1–5. http://dx.doi.org/10.1111/imr.12372.

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21

Vidal, Ariovaldo José. "FC no Brasil." Revista USP, no. 65 (May 1, 2005): 194. http://dx.doi.org/10.11606/issn.2316-9036.v0i65p194-201.

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22

Dago, Ana. "Foro AF-FC." Pharmaceutical Care España 24, no. 5 (October 15, 2022): 4–5. http://dx.doi.org/10.60103/phc.v24i5.789.

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Foro de Atención Farmacéutica se constituye en 2004 con el impulso del Consejo General de Colegios de Farmacéuticos. Forman parte de este grupo de trabajo representantes de las distintas instituciones de todos los ámbitos profesionales (académico, colegial, primaria, hospitalaria y comunitaria). Conscientes de las dificultades de implantación y desarrollo de la Atención Farmacéutica, inician un proyecto de trabajo para llegar a acuerdos de definición, terminología y práctica de la Atención Farmacéutica que tiene como resultado el Documento de Consenso de Foro en 2008…

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23

Smith, G. A., and E. G. Ruppel. "Registration of FC 609 and FC 609 CMS Sugarbeet Germplasm." Crop Science 28, no. 6 (November 1988): 1039. http://dx.doi.org/10.2135/cropsci1988.0011183x002800060070x.

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24

Berasategui, M., G. A. Argüello, and M. A. Burgos Paci. "Thermal decomposition of FC(O)OCH3 and FC(O)OCH2CH3." Physical Chemistry Chemical Physics 20, no. 18 (2018): 12817–26. http://dx.doi.org/10.1039/c7cp08656c.

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25

Weigle, W. O., M. V. Hobbs, and E. L. Morgan. "Fc receptors and immunoglobulin Fc region interaction as immunoregulatory events." Annales de l'Institut Pasteur / Immunologie 136, no. 3 (January 1985): 421–23. http://dx.doi.org/10.1016/s0769-2625(85)80019-2.

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26

Beaven, Michael A., and Henry Metzger. "Signal transduction by Fc receptors: the Fc&RI case." Immunology Today 14, no. 5 (May 1993): 222–26. http://dx.doi.org/10.1016/0167-5699(93)90167-j.

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27

Grevys, Algirdas, Malin Bern, Stian Foss, Diane Bryant Bratlie, Anders Moen, Kristin Støen Gunnarsen, Audun Aase, Terje Einar Michaelsen, Inger Sandlie, and Jan Terje Andersen. "Fc Engineering of Human IgG1 for Altered Binding to the Neonatal Fc Receptor Affects Fc Effector Functions." Journal of Immunology 194, no. 11 (April 22, 2015): 5497–508. http://dx.doi.org/10.4049/jimmunol.1401218.

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28

Letourneur, O., I. C. Kennedy, A. T. Brini, J. R. Ortaldo, J. J. O'Shea, and J. P. Kinet. "Characterization of the family of dimers associated with Fc receptors (Fc epsilon RI and Fc gamma RIII)." Journal of Immunology 147, no. 8 (October 15, 1991): 2652–56. http://dx.doi.org/10.4049/jimmunol.147.8.2652.

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Abstract The receptor for IgE (Fc epsilon RI) is a multimeric complex containing one alpha chain, one beta chain with four transmembrane domains and one homodimer of disulfide-linked gamma-chains. The Fc epsilon RI gamma-chains form additional disulfide-linked dimers with the homologous zeta- and eta-chains, as part of the TCR complex. The low affinity receptor for IgG (Fc gamma RIII)2 on NK cells is also associated with zeta-chains. Here we show that the gamma-chain is expressed in NK cells both as a group of heterogenous gamma gamma homodimers and also as a heterodimer bound to zeta. Fc gamma RIIIA is associated with three types of dimers zeta zeta, gamma zeta, and notably gamma gamma as well. In fact, gamma gamma appears to be the predominant species associating with Fc gamma RIIIA. The surface expressed Fc epsilon RI also associates with the same group of heterogenous gamma gamma homodimers. We also show that there is no C-terminal posttranslational cleavage of gamma occurring before its insertion into the plasma membrane as previously suggested. Thus, like the TCR, Fc gamma RIIIA may form a variety of receptor isoforms, though at present we do not understand the functional implications of these structures.

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29

Bildstein, Benno, Wolfgang Skibar, Manuela Schweiger, Holger Kopacka, and Klaus Wurst. "In situ synthesis of the first C7 cumulene (Fc)2CCCCCCC(Fc)2 via deprotonation of its conjugate acid [(Fc)2C7H(Fc)2]+BF4− (Fc=ferrocenyl)." Journal of Organometallic Chemistry 622, no. 1-2 (March 2001): 135–42. http://dx.doi.org/10.1016/s0022-328x(00)00882-2.

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30

Hecker, R. J., and E. G. Ruppel. "Registration of Rhizoctonia Root Rot Resistant Sugarbeet Germplasms FC 701/6, FC 702/7, and FC 705/1." Crop Science 25, no. 2 (1985): 374. http://dx.doi.org/10.2135/cropsci1985.0011183x002500020063x.

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31

Canales, Silvia, Olga Crespo, Angela Fortea, M. Concepción Gimeno, Peter G. Jones, and Antonio Laguna. "Gold and silver complexes with the ligands Fc(SPh)2 and Fc(SePh)2 (Fc = (η5-C5H4)2Fe)." Journal of the Chemical Society, Dalton Transactions, no. 10 (April 16, 2002): 2250–55. http://dx.doi.org/10.1039/b111459j.

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32

Tkaczyk, Christine, Dean Metcalfe, and Alasdair Gilfillan. "Fc gamma RI and Other Fc Receptors on Human Mast Cells." Allergy & Clinical Immunology International - Journal of the World Allergy Organization 14, no. 3 (2002): 0109–16. http://dx.doi.org/10.1027/0838-1925.14.3.109.

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33

Montgomery, R. R., M. H. Nathanson, and S. E. Malawista. "Fc- And Non-Fc-Mediated Phagocytosis Of Borrelia Burgdorferi By Maerophages." Journal of Infectious Diseases 170, no. 4 (October 1, 1994): 890–93. http://dx.doi.org/10.1093/infdis/170.4.890.

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34

Boyd, Darryl A., Robert J. Crutchley, Phillip E. Fanwick, and Tong Ren. "Fc-Fc Electronic Interaction through Equatorial Pathways of a Diruthenium Core." Inorganic Chemistry 49, no. 4 (February 15, 2010): 1322–24. http://dx.doi.org/10.1021/ic902378h.

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35

Litwin, Virginia, and Charles Grose. "Herpesviral Fc receptors and their relationship to the human Fc receptors." Immunologic Research 11, no. 3-4 (December 1992): 226–38. http://dx.doi.org/10.1007/bf02919129.

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36

Wang, Yu, and Dexu Zhou. "Gorenstein FC-projective modules." Journal of Algebra and Its Applications 19, no. 04 (April 26, 2019): 2050066. http://dx.doi.org/10.1142/s0219498820500668.

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In this paper, we investigate Gorenstein FC-projective modules and Gorenstein FC-projective dimensions, and characterize rings over which every module is Gorenstein FC-projective and rings over which every submodule of a projective is Gorenstein FC-projective, respectively. Under an almost excellent extension of rings, we obtain several invariant properties of Gorenstein FC-projective modules and Gorenstein FC-projective dimensions.

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37

Schreiber, R. E., A. Buku, and J. C. Unkeless. "Expression of murine Fc receptors for IgG." Journal of Immunology 144, no. 12 (June 15, 1990): 4735–41. http://dx.doi.org/10.4049/jimmunol.144.12.4735.

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Abstract There are two distinct genes that encode murine low affinity Fc gamma RII, murine Fc gamma RII alpha, and murine Fc gamma RII beta, which are transcribed in specific cell lineages. Fc gamma RII alpha transcripts are present in macrophages, NK cells, and mesangial cells; Fc gamma RII beta transcripts are expressed in Fc gamma R-bearing B cells, T cells, and macrophages. We have devised a sandwich ELISA to quantify the expression of Fc gamma RII alpha protein. The ELISA is specific for Fc gamma RII alpha, and does not detect the closely related Fc gamma RII beta protein. Upon stimulation with IFN-gamma the Fc gamma RII beta- macrophage cell line J774a expressed a twelvefold enhanced level of Fc gamma RII alpha protein. Peritoneal macrophages synthesized varying amounts of Fc gamma RII alpha. High levels of Fc gamma RII alpha were observed in resident and thioglycollate-elicited peritoneal macrophages, but no Fc gamma RII alpha was detected in Bacillus Calmette Guérin-elicited macrophages. J774a cells stimulated with rIL-6 bound approximately twice as much anti-Fc gamma RII mAb 2.4G2 IgG as did unstimulated controls. However, the Fc gamma RII alpha-specific ELISA showed no change in the amount of Fc gamma RII alpha expressed. A probe encompassing the extracellular coding sequence of Fc gamma RII beta hybridized to two distinct transcripts that were elevated in rIL-6-stimulated J774a cells. One of these transcripts had the same mobility in electrophoresis as Fc gamma RII alpha mRNA and hybridized to an Fc gamma RII alpha-specific probe, whereas the other transcript was larger and did not hybridize to probes specific for either Fc gamma RII alpha or Fc gamma RII beta. Moreover, we confirmed, with an Fc gamma RII beta-specific probe, that J774a cells do not make Fc gamma RII beta mRNA. Thus, the larger transcript appears to encode a novel Fc gamma RII. We suggest that the increased level of binding of the anti-Fc gamma RII mAb 2.4G2 to rIL-6-induced cells represents translation of a Fc gamma R distinct from Fc gamma RII alpha or Fc gamma RII beta.

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38

Jegaskanda, Sinthujan, Hillary A. Vanderven, Adam K. Wheatley, and Stephen J. Kent. "Fc or not Fc; that is the question: Antibody Fc-receptor interactions are key to universal influenza vaccine design." Human Vaccines & Immunotherapeutics 13, no. 6 (April 3, 2017): 1288–96. http://dx.doi.org/10.1080/21645515.2017.1290018.

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39

Jouhara, Hussam, and Anthony J. Robinson. "Experimental investigation of small diameter two-phase closed thermosyphons charged with water, FC-84, FC-77 and FC-3283." Applied Thermal Engineering 30, no. 2-3 (February 2010): 201–11. http://dx.doi.org/10.1016/j.applthermaleng.2009.08.007.

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40

Edberg, J. C., and R. P. Kimberly. "Modulation of Fc gamma and complement receptor function by the glycosyl-phosphatidylinositol-anchored form of Fc gamma RIII." Journal of Immunology 152, no. 12 (June 15, 1994): 5826–35. http://dx.doi.org/10.4049/jimmunol.152.12.5826.

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Abstract Human neutrophils express two structurally distinct receptors for IgG, the transmembrane Fc gamma RII (CD32) and the glycosyl-phosphatidylinositol-linked Fc gamma RIII (CD16). To explore the respective functional roles of Fc gamma RII and Fc gamma RIII, we have used anti-receptor mAb fragments coupled with erythrocytes to quantify both individual and cooperative receptor functions. With individual receptor engagement, Fc gamma RII (E-IV.3) was much more efficient than Fc gamma RIIIB (E-3G8) in initiating phagocytosis (p < 0.001). However, when identical total numbers of receptors were engaged, co-ligation of Fc gamma RII and Fc gamma RIIIB resulted in a phagocytic response, which was: 1) greater than that for either receptor alone (> twofold Fc gamma RII alone (p < 0.001) and > 20-fold Fc gamma RIIIB alone (p < 0.001)); 2) greater than the sum of Fc gamma RII and Fc gamma RIIIB (p < 0.001); and 3) comparable to the phagocytic potential of Fc gamma RII in FMLP pre-activated neutrophils. This synergistic capacity of Fc gamma RIIIB also enabled CR phagocytosis. Furthermore, the capacity for Fc gamma RIIIB to interact synergistically with Fc gamma RII was preserved in FMLP-preactivated neutrophils. The activation of Fc gamma RII by Fc gamma RIIIB was associated with tyrosine phosphorylation of the Fc gamma RII cytoplasmic domain, which is essential for Fc gamma RII function and which, by analogy to the Ig alpha-chain of the B cell Ag receptor complex, the zeta-chain of CD3, and the gamma-chain of some Fc epsilon Rs and Fc gamma Rs, may enhance the binding and activation of Src or Syk family tyrosine kinases. Thus, Fc gamma RIIIB can affect multiple receptor families and play a role in achieving maximal Fc gamma R capacity, even in stimulated neutrophils in inflammatory sites.

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41

Kindt, G. C., J. G. van de Winkel, S. A. Moore, and C. L. Anderson. "Identification and structural characterization of Fc gamma-receptors on pulmonary alveolar macrophages." American Journal of Physiology-Lung Cellular and Molecular Physiology 260, no. 6 (June 1, 1991): L403—L411. http://dx.doi.org/10.1152/ajplung.1991.260.6.l403.

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Little is known about the structure of the cell surface receptors for the Fc portion of immunoglobulin G (Fc gamma R) on tissue macrophages. Studies on leukocytes indicate the existence of three classes of Fc gamma R, denoted I, II, and III. The purpose of this study was to structurally characterize Fc gamma R on alveolar macrophages obtained by bronchoalveolar lavage, comparing them with Fc gamma R of monocytes, neutrophils, and U937 cells. Flow-cytometric evaluation, utilizing anti-Fc gamma R class-specific monoclonal antibodies, showed that alveolar macrophages expressed three Fc gamma R classes. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the immunopurified Fc gamma R molecules revealed the following apparent molecular mass for each Fc gamma R class: Fc gamma RI, 70 kDa; Fc gamma RII, 44 kDa; and Fc gamma RIII, 57-65 kDa. RNA blot analysis demonstrated a 1.7-kb transcript for Fc gamma RI, 2.5 and 1.6 kb transcripts for Fc gamma RII, and a 2.2 kb mRNA for Fc gamma RIII. Fc gamma RII displayed the high-responder/low-responder polymorphism. Fc gamma RIII did not express the neutrophil antigen-type specific structural polymorphism of the deglycosylated Fc gamma R molecule and appeared to be a transmembrane molecule.

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42

Daëron, M., C. Bonnerot, S. Latour, and W. H. Fridman. "Murine recombinant Fc gamma RIII, but not Fc gamma RII, trigger serotonin release in rat basophilic leukemia cells." Journal of Immunology 149, no. 4 (August 15, 1992): 1365–73. http://dx.doi.org/10.4049/jimmunol.149.4.1365.

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Abstract Murine Fc gamma RII and Fc gamma RIII have highly homologous extracellular domains, but unrelated transmembrane and intracytoplasmic (IC) domains. Murine Fc gamma RIIb1 and b2 are two isoforms of single-chain receptors which differ only by 47 aa in their IC domain. Murine Fc gamma RIII are composed of an IgG-binding alpha-chain, the intracellular portion of which is unrelated to that of Fc gamma RII, and of a homodimeric gamma-chain which also associates with Fc epsilon RI. Murine mast cells express Fc gamma RII, Fc gamma RIII, and Fc epsilon RI. They can be induced to degranulate by murine IgG immune complexes or by F(ab')2 fragments of the rat anti-murine Fc gamma RII/III mAb 2.4G2, complexed to mouse anti-rat (MAR) F(ab')2. In order to determine which murine Fc gamma R can activate mast cells, cDNA encoding murine Fc gamma RIIb1, Fc gamma RIIb2 or Fc gamma RIII alpha were stably transfected into RBL-2H3 cells. Murine Fc gamma RIII but not Fc gamma RIIb1 or Fc gamma RIIb2 induced serotonin release when aggregated by (2.4G2-MAR) F(ab')2 complexes. The respective roles of the IC domains of murine Fc gamma RIII subunits in signal transduction were investigated by stably transfecting cDNA encoding IC-deleted or chimeric murine Fc gamma R into RBL-2H3 cells. The substitution of the IC domain of murine Fc gamma RII for that of murine Fc gamma RIII gamma, but not that of murine Fc gamma RIII alpha, conferred the ability to trigger serotonin release. The deletion of IC sequences of the alpha subunit did not alter the ability of murine Fc gamma RIII to trigger serotonin release. It follows that 1) murine Fc gamma RIII, but not Fc gamma RII, can induce RBL cells to release serotonin, 2) the aggregation of the IC domain of the murine Fc gamma RIII gamma subunit is sufficient, but 3) the IC domain of the murine Fc gamma RIII alpha subunit is neither sufficient nor necessary for triggering serotonin release.

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43

Daeron, M., and K. Ishizaka. "Induction of Fc epsilon receptors on mouse macrophages and lymphocytes by homologous IgE." Journal of Immunology 136, no. 5 (March 1, 1986): 1612–19. http://dx.doi.org/10.4049/jimmunol.136.5.1612.

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Abstract Normal mouse peritoneal macrophages express Fc gamma 2aR, Fc gamma 1/2bR, and Fc epsilon R, whereas B lymphocytes in mesenteric lymph nodes (MLN) bear Fc gamma 2bR, Fc gamma 1R, and Fc epsilon R. Rosette formation of Fc epsilon R+ macrophages and lymphocytes with IgE-coated ox erythrocytes was inhibited by rodent IgE but not by any other isotype of mouse immunoglobulins. In contrast, IgG1 rosettes and IgG2b rosettes of both macrophages and lymphocytes were inhibited not only by homologous isotype but also by IgE, suggesting that IgE has some affinity for Fc gamma 1/2bR on macrophages and for both Fc gamma 1R and Fc gamma 2bR on lymphocytes. Incubation of normal mouse macrophages with mouse IgE for 24 hr resulted in a twofold increase in the proportion of Fc epsilon R+ cells. Mouse IgE can induce Fc epsilon R on B cells as well. Incubation of MLN cells with mouse IgE for 2 to 4 hr, followed by culture of the cells in the absence of IgE, resulted in a 1.8- to 2.9-fold increase in Fc epsilon R+ cells. Determination of Fc gamma R+ cells in the same MLN cells revealed that induction of Fc epsilon R by IgE was accompanied by a substantial decrease in the expression of Fc gamma 1R and Fc gamma 2bR. Induction of Fc epsilon R by IgE on macrophages and lymphocytes requires protein synthesis. In MLN cells, cycloheximide inhibited not only the IgE-induced increase in Fc epsilon R+ cells but also the decrease in Fc gamma 1R+ cells and Fc gamma 2bR+ cells. It was also found that induction of Fc epsilon R by IgE on macrophages was completely inhibited if IgG1 or IgG2b was added to the cells together with IgE. In contrast, IgG2a did not affect the IgE-induced expression of Fc epsilon R on macrophages. In MLN cells, IgG2b but not IgG1 inhibited both IgE-induced increase in Fc epsilon R and decrease in Fc gamma 1R and Fc gamma 2bR. The results indicate that expression of various Fc receptors on lymphocytes is mutually regulated.

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44

Bisello, Annalisa, Barbara Biondi, Roberta Cardena, Renato Schiesari, Marco Crisma, Fernando Formaggio, and Saverio Santi. "Modulation of Ferrocene–Ferrocene Interactions by Varying Their Reciprocal Positions in L-Dap/Aib Helical Peptides." Inorganics 11, no. 12 (December 16, 2023): 482. http://dx.doi.org/10.3390/inorganics11120482.

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In this work, we developed two new polyfunctional hybrid systems in which the presence of Fc redox “antennas” on peptide scaffolds allows for a modulation of their electronic properties. Specifically, we synthesized two helical hexapeptides containing four Aib (α-amionoisobutyric acid) and two L-Dap (2,3-diamino propionic acid) residues. L-Dap side chains were then functionalized with Fc moieties. The structures of the two 310 helical peptides, namely Z-Aib-L-Dap(Fc)-Aib-Aib-L-Dap(Fc)-Aib-NH-iPr and Z-Aib-L-Dap(Fc)-Aib-L-Dap(Fc)-Aib-Aib-NH-iPr, were investigated by X-ray diffraction, 2D-NMR, CD and IR spectroscopies. Due to the helical conformation, in Z-Aib-L-Dap(Fc)-Aib-Aib-L-Dap(Fc)-Aib-NH-iPr, the Fc groups are located on the same face of the helix, but in Z-Aib-L-Dap(Fc)-Aib-L-Dap(Fc)-Aib-Aib-NH-iPr, they are located on opposite faces. Surprisingly, two bands were found through DPV for Z-Aib-L-Dap(Fc)-Aib-L-Dap(Fc)-Aib-Aib-NH-iPr, indicating an electrostatic interaction between the Fc groups despite their longer reciprocal distance with respect to that in Z-Aib-L-Dap(Fc)-Aib-Aib-L-Dap(Fc)-Aib-NH-iPr. CD experiments at different concentrations evidenced aggregation for Z-Aib-L-Dap(Fc)-Aib-L-Dap(Fc)-Aib-Aib-NH-iPr, even at high dilutions, thus suggesting that the Fc-Fc electrostatic interaction could be of an intermolecular nature.

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Ghazizadeh, S., and H. B. Fleit. "Tyrosine phosphorylation provides an obligatory early signal for Fc gamma RII-mediated endocytosis in the monocytic cell line THP-1." Journal of Immunology 152, no. 1 (January 1, 1994): 30–41. http://dx.doi.org/10.4049/jimmunol.152.1.30.

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Abstract The human monocytic cell line THP-1 expresses two classes of IgG Fc receptor (Fc gamma R), Fc gamma RI, a high affinity 72-kDa Fc gamma R, and Fc gamma RII, a low affinity 40-kDa Fc gamma R. Biochemical as well as indirect immunofluorescence studies demonstrated that the selective cross-linking of Fc gamma RII with either anti-Fc gamma RII mAb Fab followed by F(ab)2 fragments of goat anti-mouse IgG, or aggregated hIgG1, which represents a physiologic ligand for this receptor, resulted in the activation of a protein tyrosine kinase (PTK). Several distinct cellular proteins including the Fc gamma RII itself were specifically phosphorylated on tyrosine upon ligand binding. Cross-linking of Fc gamma RII also triggered a rapid internalization of Fc gamma RII that was dependent upon tyrosine kinase activity. The internalization of the receptor in endocytic vesicles was established by confocal microscopy. The time course of Fc gamma RII-initiated tyrosine phosphorylation paralleled endocytic events and reached a maximum between 5 and 10 min after ligand binding and declined toward basal levels as endocytosis was completed. Identical concentrations of genistein, an inhibitor of PTK, blocked Fc gamma RII-mediated endocytosis as well as the induction of tyrosine phosphorylation of Fc gamma RII and other cellular proteins. Cross-linking of Fc gamma RI also induced a rapid tyrosine phosphorylation of cellular proteins similar to the Fc gamma RII-mediated events. However, Fc gamma RII was not tyrosyl phosphorylated upon Fc gamma RI activation. Thus Fc gamma RII is a unique substrate for the PTK activity associated with Fc gamma RII upon cross-linking of this receptor. These results support the conclusion that Fc gamma RII is capable of independent signaling on monocytic cells and that protein tyrosine phosphorylation is an obligatory proximal signal for Fc gamma RII-mediated endocytosis. Furthermore, the signaling pathways employed by Fc gamma RI and Fc gamma RII are likely to be distinct.

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Graziano, R. F., R. J. Looney, L. Shen, and M. W. Fanger. "Fc gamma R-mediated killing by eosinophils." Journal of Immunology 142, no. 1 (January 1, 1989): 230–35. http://dx.doi.org/10.4049/jimmunol.142.1.230.

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Abstract In this report we present data on the ability of the different Fc gamma R present on eosinophils to mediate killing of erythroid and tumor targets, and on a comparison of eosinophil and neutrophil Fc gamma R-mediated killing. Erythroid target killing was assessed using chicken erythrocytes (CE) and heteroantibodies composed of Fab fragments of anti-CE antibodies covalently coupled to Fab fragments of anti-Fc gamma R antibodies. Such anti-CE x anti-Fc gamma R reagents permit linkage of CE target cells with the FcR molecules on the eosinophil or neutrophil effector cells. Tumor target killing was assessed using hybridoma cell lines (HC) bearing anti-Fc gamma R antibodies on their cell surface. Freshly isolated eosinophils and neutrophils constitutively express similar amounts of the low affinity Fc gamma R, Fc gamma RII on their cell surface, but neither cell type expresses the high affinity Fc gamma R, Fc gamma RI. In contrast, eosinophils have only about 5% as much of the low affinity Fc gamma R found on human granulocytes and large granular lymphocytes (Fc gamma RIII) as neutrophils. Untreated, freshly prepared eosinophils or neutrophils did not lyse any of the anti-Fc gamma R bearing HC nor did they lyse CE in the presence of anti-Fc gamma R containing heteroantibodies. Upon treatment with granulocyte monocyte-CSF (GM-CSF), both cell types lysed HC-bearing antibody to Fc gamma RII (HC IV.3A) and CE in the presence of anti-CE x anti-Fc gamma RII heteroantibodies. However, neither cell type lysed HC-bearing antibody to Fc gamma RI or Fc gamma RIII, or CE in the presence of anti-CE x anti-Fc gamma RI HA. Treatment with GM-CSF did not significantly alter the number of Fc gamma R on either cell type. Treatment of neutrophils with IFN-gamma for 18 h induced the expression of Fc gamma RI on these cells and their ability to lyse anti-Fc gamma RI- or Fc gamma RII-bearing HC and CE through Fc gamma RI, Fc gamma RII, and Fc gamma RIII. In contrast, 6-h treatment of eosinophils or neutrophils with IFN-gamma induced neither Fc gamma RI expression on either cell type nor killing of HC or CE through Fc gamma R. In summary, incubation with GM-CSF, induced eosinophils and neutrophils to kill anti-Fc gamma RII-bearing HC and to lyse CE through Fc gamma RII. This augmented killing was not associated with enhanced expression of Fc gamma RII.(ABSTRACT TRUNCATED AT 400 WORDS)

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Indik, ZK, JG Park, S. Hunter, and AD Schreiber. "The molecular dissection of Fc gamma receptor mediated phagocytosis." Blood 86, no. 12 (December 15, 1995): 4389–99. http://dx.doi.org/10.1182/blood.v86.12.4389.bloodjournal86124389.

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Because hematopoietic cells express multiple Fc gamma receptor isoforms, the role of the individual Fc gamma receptors in phagocytosis has been difficult to define. Transfection of Fc gamma receptors into COS-1 cells, which lack endogeneous Fc gamma receptors but have phagocytic potential, has proved valuable for the study of individual Fc gamma receptor function. Using this model system, we have established that a single class of human Fc gamma receptor mediates phagocytosis in the absence of other Fc receptors and that isoforms from each Fc gamma receptor class mediate phagocytosis, although the requirements for phagocytosis differ. In investigating the relationship between structure and function for Fc gamma receptor mediated phagocytosis, the importance of the cytoplasmic tyrosines of the receptor or its associated gamma chain has been established. For example, two cytoplasmic YXXL sequences, in a configuration similar to the conserved tyrosine-containing motif found in Ig gene family receptors, are important for phagocytosis by the human Fc gamma receptor, Fc gamma RIIA. Fc gamma RI and Fc gamma RIIIA do not possess cytoplasmic tyrosines but transmit a phagocytic signal through interaction with an associated gamma subunit that contains two YXXL sequences in a conserved motif required for phagocytosis. The human Fc gamma RII isoforms Fc gamma RIIB1 and Fc gamma RIIB2 do not induce phagocytosis and have only a single YXXL sequence. Cross-linking the phagocytic Fc gamma receptors induces tyrosine phosphorylation of either Fc gamma RIIA or the gamma chain, and treatment with tyrosine kinase inhibitors reduces both phagocytosis and phosphorylation of the receptor tyrosine residues. Activation of protein tyrosine kinases follows Fc gamma receptor engagement of IgG-coated cells. The data indicate that coexpression of the protein tyrosine kinase Syk, which is associated with the gamma chain in monocytes/macrophages, is important for phagocytosis mediated by Fc gamma RI and Fc gamma RIIIA. Furthermore, phosphatidylinositol-3 kinase is required for phagocytosis mediated by Fc gamma RIIA as well as for phagocytosis mediated by Fc gamma RI/gamma and Rc gamma RIIIA/gamma.

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Koduru, Srinivas V. "Abstract 2291: microRNA/mRNA integrated analysis of multiple myeloma transcriptomics." Cancer Research 82, no. 12_Supplement (June 15, 2022): 2291. http://dx.doi.org/10.1158/1538-7445.am2022-2291.

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Abstract Myeloma is plasma cell disorder, mostly effects adults over 60 years. Non-coding RNAs are emerging field and play vital role in development of disease. Major non-coding RNAs are miRNAs, lncRNAs, circRNAs and sn/snoRNAs. We analyzed restricted and publically available RNA-seq and small RNA-seq data sets for biomarkers identification and their involvement in myeloma. We obtained restricted data from “BluePrint”, which contains 11 myeloma plasma cells and 4 normal tonsil plasma cells (EGAS00001001110). We identified 1534 genes are differentially regulated (2-fold cut-off, >10-FC 218 genes). Top 10 upregulated genes were: EDNRB (1246-FC), SCUBE1 (737-FC), MC4R (691-FC), NDNF (601-FC), PTGS2 (567-FC), GPRC5D (531-FC), MFAP3L (467-FC), CCND1 (381-FC), CXCL12 (344-FC) and BTBD3 (326-FC) ; top 10 downregulated were: EBF1 (-111-FC), HLA-DRB1(-133-FC), CPXM1 (-171-FC), LOC642131 (-171-FC), IGHV1OR15-3 (-171-FC), HLA-DRB5 (-204-FC), PRAMENP (-210-FC), DTX1 (-220-FC), CD22 (-337-FC) and RFTN1 (-356-FC). Publically available small RNA-seq data downloaded and analyzed for miRNAs, lncRNAs, circRNAs and sn/snoRNAs which contains 3 healthy donor’s plasma cells and 3 newly diagnosed myeloma patient plasma cells (PRJNA377345). We used mirDIP portal to analyze miRNA and mRNA differentially expressed data, predicated from more than 13 databases showed major role of miR-152-3p (targets 28 mRNAs), miR-93-5p (targets 19 mRNAs), miR-301a-3p (targets 13 mRNAs), miR-29c-3p (targets 12 mRNAs), and miR-144-3p (targets 9 mRNAs). Integrated analysis can provide valuable information from the transcriptomics data and effect of miRNAs on mRNAs. Citation Format: Srinivas V. Koduru. microRNA/mRNA integrated analysis of multiple myeloma transcriptomics [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 2291.

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Migdał, Anna, Małgorzata Żuk, Dorota Jagiełłowicz-Kowalska, Zuzanna Powichrowska, and Grażyna Brzezińska-Rajszys. "Which Functional Classification Scale is Optimal for Children with Pulmonary Hypertension (PAH)?" Pediatric Cardiology 41, no. 8 (August 9, 2020): 1725–29. http://dx.doi.org/10.1007/s00246-020-02434-8.

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AbstractFunctional status assessed by the WHO-FC scale derived from adults is a known prognostic factor for pulmonary hypertension. Data on the usefulness of the Panama-FC scale in assessing children with pulmonary hypertension are limited. The study was performed to compare functional status results (WHO-FC and Panama-FC) and to assess the usefulness of these scales in various clinical situations. The reliability of the Panama-FC questionnaire method for facilitating patient evaluation was also examined. 26 functional status assessments (7 in disease progression/after treatment intensification) in both scales were analyzed in 19 patients with PAH confirmed in RHC. WHO-FC, Panama-FC scales, and questionnaire-based on Panama-FC were conducted independently by three different physicians. Results of assessments were compared with each other and with 6MWD, NTproBNP level, and echo parameters (TAPSE, RV/LV ratio). The Panama-FC scale results obtained using the medical interview method and questionnaire did not differ. Both WHO-FC and Panama-FC classes well-reflected disease advancement confirmed by non-invasive parameters (NTproBNP, 6MWD, TAPSE, RV/LV ratio). Differences between grading the class in both scales were observed: 5pts were classified to II (Panama-FC) vs I (WHO-FC), 2pts were in lower risk group in WHO-FC (II) vs Panama (IIIa). Worsening or improvement after treatment intensification in functional status in both scales was connected with the significant change of NTproBNP level. The 6-min walking distance did not change. TAPSE, RV/LV ratio changed significantly in 3pts with IPAH, accordingly to change in WHO-FC and Panama-FC. WHO-FC and Panama-FC well reflect the disease advancement. The questionnaire method simplified the use of the Panama-FC scale. The Panama-FC scale appears to be better for assessing functional status during long-term follow-up, while the WHO-FC scale was more useful in short-term treatment monitoring.

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Toscano, Stefania, and Daniela Romano. "Morphological, Physiological, and Biochemical Responses of Zinnia to Drought Stress." Horticulturae 7, no. 10 (October 4, 2021): 362. http://dx.doi.org/10.3390/horticulturae7100362.

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Bedding plants in the nursery phase are often subject to drought stress because of the small volume of the containers and the hydraulic conductivity of organic substrates used. To analyse the morphological, physiological, and enzymatic responses of zinnia (Zinnia elegans L.) plants at different irrigation levels, four treatments were performed: irrigated at 100% (100% field capacity, FC); light deficit irrigation (75% FC), medium deficit irrigation (50% FC), and severe deficit irrigation (25% FC). The growth of zinnia was significantly influenced by drought stress treatments. Different morphological parameters (dry biomass, leaf number, root to shoot ratio (R/S)) were modified only in the more severe drought stress treatment (25% FC). The stomata density increased in 50% FC and 25% FC, while the stomata size was reduced in 25% FC. The net photosynthesis, stomatal conductance, and transpiration were reduced in 50% FC and 25% FC. The relative water content (RWC) was reduced in 25% FC. Severe drought stress (25% FC) increased proline content up to seven-fold. Catalase (CAT), peroxidase (GPX), and superoxide dismutase (SOD) activity significantly increased in 50% FC and 25% FC. Principal component analysis (PCA) showed that the morphological and physiological parameters were mostly associated with the 100% FC and 75% FC treatments of the biplot, whereas the stomata density, R/S ratio, and antioxidant enzymes (GPX, CAT) were associated with 50% FC, and proline and DPPH were associated with 25% FC, respectively.

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Journal articles on the topic 'FC'

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