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Purified GPI-linked molecules incorporate spontaneously in vitro into mammalian cell plasma membranes. Recent evidence suggests that the transferred molecules insert stably into the external leaflet of the acceptor cell plasma membrane through their acyl chains and behave subsequently in a way similar to endogenous GPI-linked molecules. Transfer of GPI-linked proteins between cells has also been documented in vivo and may explain the uptake by host cells o f pathogen-derived virulence factors carrying a GPI anchor. In this comment article, Subburaj Ilangumaran, Peter Robinson and Daniel Hoessli review what is known about GPI transfer and discuss the use of GPI transfer for transient cell-surface expression of foreign proteins. 相似文献
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Gagnon J Ramanathan S Leblanc C Cloutier A McDonald PP Ilangumaran S 《Journal of immunology (Baltimore, Md. : 1950)》2008,180(12):7958-7968
Recent reports have shown that IL-21, in synergy with IL-15, stimulates proliferation of CD8(+) T lymphocytes in the absence of signaling via the TCR. In this study, we show that IL-6, which induces phosphorylation of STAT3 similarly to IL-21, also can stimulate proliferation of CD8(+) T cells in synergy with IL-7 or IL-15. IL-6 displays a stronger synergy with IL-7 than with IL-15 to stimulate naive CD8(+) T cells. Concomitant stimulation by IL-6 or IL-21 augments phosphorylation and DNA-binding activity of STAT5 induced by IL-7 or IL-15. Like IL-21, IL-6 reduces the TCR signaling threshold required to stimulate CD8(+) T cells. Prior culture of P14 TCR transgenic CD8 T cells with IL-6 or IL-21 in the presence of IL-7 or IL-15 augments their proliferation and cytolytic activity upon subsequent stimulation by Ag. Furthermore, cytokine stimulation induces quantitatively and qualitatively distinct phenotypic changes on CD8(+) T cells compared with those induced by TCR signaling. We propose that the ability of IL-6 to induce TCR-independent activation of CD8(+) T cells in synergy with IL-7 or IL-15 may play an important role in the transition from innate to adaptive immunity. 相似文献
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Gregory Lacraz Volatiana Rakotoarivelo Sebastien M. Labbé Mathieu Vernier Christophe Noll Marian Mayhue Jana Stankova Adel Schwertani Guillaume Grenier André Carpentier Denis Richard Gerardo Ferbeyre Julie Fradette Marek Rola-Pleszczynski Alfredo Menendez Marie-France Langlois Subburaj Ilangumaran Sheela Ramanathan 《PloS one》2016,11(11)
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Kannan S 《Cell biology international》2003,27(2):147-151
Fatty acid translocase (FAT)/CD36-mediated long-chain fatty acid uptake in human umbilical vessel endothelial cells is associated with as yet uncharacterized translocase activity. The molecular mechanism of its function is not yet understood. Numerous attempts to purify rat cardiac sarcolemmal E-NTPase (an integral membrane protein also referred to as ecto-Ca(2+)/Mg(2+)ATPase) have revealed a complete amino acid sequence identity for FAT/CD36 protein. The most striking observation is that purified CD36 from human platelets shows significant E-NTPase activity. In view of recent progress in understanding CD36 functional properties, an attempt is made in this article to illustrate the point that association of E-NTPase (possibly extracellular Ca(2+)/Mg(2+)nucleotide triphosphate diphosphohydrolase) activity with CD36 may be of potential functional significance. 相似文献
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Signaling through sphingolipid microdomains of the plasma membrane: The concept of signaling platform 总被引:1,自引:0,他引:1
Daniel C. Hoessli Subburaj Ilangumaran Alex Soltermann Peter J. Robinson Bettina Borisch Nasir- Ud-Din 《Glycoconjugate journal》2000,17(3-4):191-197
Transmembrane signaling requires modular interactions between signaling proteins, phosphorylation or dephosphorylation of the interacting protein partners [1] and temporary elaboration of supramolecular structures [2], to convey the molecular information from the cell surface to the nucleus. Such signaling complexes at the plasma membrane are instrumental in translating the extracellular cues into intracellular signals for gene activation. In the most straightforward case, ligand binding promotes homodimerization of the transmembrane receptor which facilitates modular interactions between the receptor's cytoplasmic domains and intracellular signaling and adaptor proteins [3]. For example, most growth factor receptors contain a cytoplasmic protein tyrosine kinase (PTK) domain and ligand-mediated receptor dimerization leads to cross phosphorylation of tyrosines in the receptor's cytoplasmic domains, an event that initiates the signaling cascade [4]. In other signaling pathways where the receptors have no intrinsic kinase activity, intracellular non-receptor PTKs (i.e. Src family PTKs, JAKs) are recruited to the cytoplasmic domain of the engaged receptor. Execution of these initial phosphorylations and their translation into efficient cellular stimulation requires concomitant activation of diverse signaling pathways. Availability of stable, preassembled matrices at the plasma membrane would facilitate scaffolding of a large array of receptors, coreceptors, tyrosine kinases and other signaling and adapter proteins, as it is the case in signaling via the T cell antigen receptor [5]. The concept of the signaling platform [6] has gained usage to characterize the membrane structure where many different membrane-bound components need to be assembled in a coordinated manner to carry out signaling.The structural basis of the signaling platform lies in preferential assembly of certain classes of lipids into distinct physical and functional compartments within the plasma membrane [7,8]. These membrane microdomains or rafts (Figure 1) serve as privileged sites where receptors and proximal signaling molecules optimally interact [9]. In this review, we shall discuss first how signaling platforms are assembled and how receptors and their signaling machinery could be functionally linked in such structures. The second part of our review will deal with selected examples of raft-based signaling pathways in T lymphocytes and NK cells to illustrate the ways in which rafts may facilitate signaling. 相似文献
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Pei Ge Pengchao Hao Min Cao Guangfang Guo Dongwen Lv Saminathan Subburaj Xiaohui Li Xing Yan Jitian Xiao Wujun Ma Yueming Yan 《Proteomics》2013,13(20):3046-3058
As an abundant ROS, hydrogen peroxide (H2O2) plays pivotal roles in plant growth and development. In this work, we conducted for the first time an iTRAQ‐based quantitative proteomic analysis of wheat seedling growth under different exogenous H2O2 treatments. The growth of seedlings and roots was significantly restrained by increased H2O2 concentration stress. Malondialdehyde, soluble sugar, and proline contents as well as peroxidase activity increased with increasing H2O2 levels. A total of 3 425 proteins were identified by iTRAQ, of which 157 showed differential expression and 44 were newly identified H2O2‐responsive proteins. H2O2‐responsive proteins were mainly involved in stress/defense/detoxification, signal transduction, and carbohydrate metabolism. It is clear that up‐regulated expression of signal transduction and stress/defence/detoxification‐related proteins under H2O2 stress, such as plasma membrane intrinsic protein 1, fasciclin‐like arabinogalactan protein, and superoxide dismutase, could contribute to H2O2 tolerance of wheat seedlings. Increased gluconeogenesis (phosphoenol‐pyruvate carboxykinase) and decreased pyruvate kinase proteins are potentially related to the higher H2O2 tolerance of wheat seedlings. A metabolic pathway of wheat seedling growth under H2O2 stress is presented. 相似文献