The Language Function Analysis 2011 Corpus (LFA-11) is a German text corpus of promotional text, reviews and blog posts on music and smartphones. The texts were manually classified with respect to their topic relevance, language function, and sentiment polarity.

The purpose of the corpus is to provide textual data for the development and evaluation of approaches to language function analysis and sentiment analysis. Therefore, each text is classified by language function (personal, commercial, or informational) as well as by sentiment (positive, negative, neutral).

The corpus consists of two separated collections, which contain the texts about music and smartphones respectively. The music collection consists of 2,713 promotional texts and reviews from both users and professionals. The smartphone collection contains 2,093 blog posts on smartphones from the Spinn3r corpus.

The role of Gαi proteins coupled to chemokine receptors in directed migration of immune cells is well understood. In this study we show that the separate class of Gαq/11 proteins is required for the underlying ability of T cells to migrate both randomly and in a directed chemokine-dependent manner. Interfering with Gαq or Gα11 using dominant negative cDNA constructs or siRNA for Gαq causes accumulation of LFA-1 adhesions and stalled migration. Gαq/11 has an impact on LFA-1 expression at plasma membrane level and also on its internalization. Additionally Gαq co-localizes with LFA-1- and EEA1-expressing intracellular vesicles and partially with Rap1- but not Rab11-expressing vesicles. However the influence of Gαq is not confined to the vesicles that express it, as its reduction alters intracellular trafficking of other vesicles involved in recycling. In summary vesicle-associated Gαq/11 is required for the turnover of LFA-1 adhesion that is necessary for migration. These G proteins participate directly in the initial phase of recycling and this has an impact on later stages of the endo-exocytic pathway.

BACKGROUND: Lymphocyte function-associated antigen-1 (LFA-1, CD11a/CD18, alphaLbeta2), the most abundant and widely expressed beta2-integrin, is required for many cellular adhesive interactions during the immune response. Many studies have shown that LFA-1 is centrally involved in the pathogenesis of several diseases caused by Repeats-in-toxin (RTX)-producing bacteria. RESULTS: The porcine-LFA-1 CD11a (alpha) subunit coding sequence was cloned, sequenced and compared with the available mammalian homologues in this study. Despite some focal differences, it shares all the main characteristics of these latter. Interestingly, as in sheep and humans, an allelic variant with a triplet insertion resulting in an additional Gln-744 was consistently identified, which suggests an allelic polymorphism that might be biologically relevant. CONCLUSION: Together with the pig CD18-encoding cDNA, which has been available for a long time, the sequence data provided here will allow the successful expression of porcine CD11a, thus giving the first opportunity to express the Sus scrofa beta2-integrin LFA-1 in vitro as a tool to examine the specificities of inflammation in the porcine species.

LFA-1 (CD11a-CD18) - BioCentury Target Profiles for the biopharma industry

JAM-A plays a key role in leukocyte transmigration and inflammatory extravasation. Transmigration of human leukocytes has been shown to involve heterophilic interactions of JAM-A with its integrin receptor LFA-1.

This event has been computationally inferred from an event that has been demonstrated in another species.

The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.

More details and caveats of the event inference in Reactome. For details on PANTHER see also: http://www.pantherdb.org/about.jsp

The CD11a/CD18 (leukocyte function-associated antigen 1 or LFA-1) leukocyte integrin is expressed at high levels on the cell surface of T lymphocytes and macrophages, where it mediates homotypic and heterotypic adherence between leukocytes and other cell types by binding to intracellular adhesion molecules 1 and 2 on the conjugate cell. To initiate studies of the molecular regulation of expression of the CD11a molecule, we isolated genomic clones corresponding to the 5'-flanking region of CD11a, identified the transcriptional start sites for CD11a, and characterized the CD11a promoter sequence in transient expression assays. The CD11a promoter (1.7 kb) directed functional activity of a heterologous reporter gene in the T-lymphocyte cell line Jurkat and the myeloid cell line HL-60 but did not direct functional activity in three different nonleukocyte cell lines. Deletional analysis of the CD11a promoter sequence indicated the presence of distinct, cell-type-specific regulatory sequences with the region from -40 to -17 relative to the transcription start sites responsible for most of the in vitro activity of the CD11a promoter in the Jurkat T-cell line, and the promoter sequence located within the first 17 bp relative to the transcription start sites responsible for CD11a promoter activity in the HL-60 cell line. Identification of the CD11a promoter provides the opportunity to identify unique cis-acting elements and trans-acting factors responsible for the cell-type-specific expression of CD11a in human leukocytes. Further, the CD11a promoter may be useful in transgenic constructs and in retroviral vectors to direct expression of heterologous genes selectively in leukocytes.

integrin subunit alpha L Enables ICAM-3 receptor activity and cell adhesion molecule binding activity. Involved in several processes, including T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; and memory T cell extravasation. Located in cell surface. Part of integrin alphaL-beta2 complex. ITGAL encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed on all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Protein-Protein, Genetic, and Chemical Interactions for Bechard D (2001):Human endothelial-cell specific molecule-1 binds directly to the integrin CD11a/CD18 (LFA-1) and blocks binding to intercellular adhesion molecule-1. curated by BioGRID (https://thebiogrid.org); ABSTRACT: ICAMs are ligands for LFA-1, a major integrin of mononuclear cells involved in the immune and inflammatory processes. We previously showed that endothelial cell specific molecule-1 (ESM-1) is a proteoglycan secreted by endothelial cells under the control of inflammatory cytokines. Here, we demonstrate that ESM-1 binds directly to LFA-1 onto the cell surface of human blood lymphocytes, monocytes, and Jurkat cells. The binding of ESM-1 was equally dependent on Ca(2+), Mg(2+), or Mn(2+) divalent ions, which are specific, saturable, and sensitive to temperature. An anti-CD11a mAb or PMA induced a transient increase in binding, peaking 5 min after activation. Direct binding of ESM-1 to LFA-1 integrin was demonstrated by specific coimmunoprecipitation by CD11a and CD18 mAbs. A cell-free system using a Biacore biosensor confirmed that ESM-1 and LFA-1 dynamically interacted in real time with high affinity (K(d) = 18.7 nM). ESM-1 consistently inhibited the specific binding of soluble ICAM-1 to Jurkat cells in a dose-dependent manner. These results suggest that ESM-1 and ICAM-1 interact with LFA-1 on binding sites very close to but distinct from the I domain of CD11a. Through this mechanism, ESM-1 could be implicated in the regulation of the LFA-1/ICAM-1 pathway and may therefore influence both the recruitment of circulating lymphocytes to inflammatory sites and LFA-1-dependent leukocyte adhesion and activation.

The Bordetella adenylate cyclase toxinhemolysin (CyaA) and the α-hemolysin (HlyA) of Escherichia coli both belong to the family of cytolytic pore-forming Repeats in ToXin (RTX) cytotoxins. HlyA preferentially binds the αLβ2 integrin LFA-1 (CD11a/CD18) of leukocytes and can promiscuously bind and permeabilize also a variety of other cells. CyaA bears an Nterminal adenylyl cyclase enzyme (AC) domain linked to a pore-forming RTX cytolysin (Hly) moiety and binds the complement receptor 3 (CR3, αMβ2, CD11b/CD18 or Mac-1) of myeloid phagocytes, penetrates their plasma membrane and delivers into cytosol the AC enzyme. We constructed a set of CyaA/HlyA chimeras and show that the CyaC-acylated segment and the CR3-binding RTX domain of CyaA can be functionally replaced by the much shorter HlyCacylated and LFA-1-binding RTX moiety of HlyA. Instead of binding CR3, a CyaA1710/HlyA411-1024 chimera bound the LFA-1 receptor and effectively delivered the AC enzyme into Jurkat lymphoblastoma T cells. At high chimera concentrations (25 nM), the interaction with LFA-1 was not required for CyaA1-710/HlyA411-1024 binding to CHO cells. However, interaction with the LFA-1 receptor strongly enhanced the specific capacity of the bound CyaA1-710/HlyA411-1024 chimera to penetrate cells and deliver the AC enzyme into their cytosol. Hence, interaction of the acylated RTX moiety of HlyA with LFA-1 promoted a productive membrane interaction of the chimera. These results allow to delimit the residues 400 to 710 of CyaA as the 'AC translocon' sufficient for translocation of the AC enzyme polypeptide across the plasma membrane of target cells

The integrin LFA-1 (CD11a/CD18) plays a critical role in the interaction of T cells with antigen presenting cells (APCs) to promote lymphocyte differentiation and proliferation. This integrin can be present either in a closed or in an open active conformation and its activation upon T-cell receptor (TCR) stimulation is a critical step to allow interaction with APCs. In this study we demonstrate that the serine/threonine kinase Ndr2 is critically involved in the initiation of TCR-mediated LFA-1 activation (open conformation) in T cells. Ndr2 itself becomes activated upon TCR stimulation and phosphorylates the intracellular integrin binding partner Filamin A (FLNa) at serine 2152. This phosphorylation promotes the dissociation of FLNa from LFA-1, allowing for a subsequent association of Talin and Kindlin-3 which both stabilize the open conformation of LFA-1. Our data suggest that Ndr2 activation is a crucial step to initiate TCR-mediated LFA-1 activation in T cells.

Sample ID: LFA_Rd6t08_A11

X-ray tomography (CT) image data of a Ti6Al4V disc. The 3D image was generated with an X-ray tomography scan performed by Dr Llion Evans with Swansea University, Advanced Imaging of Materials (AIM) equipment.

The dataset includes: raw radiographs; scan & reconstruction parameter settings file; reconstructed 3D volume. To visualise the 3D volume use software such as ImageJ (https://imagej.net/Fiji/Downloads). The volume image data (.raw file) is in binary format and has the following characteristics: 1920 x 1920 x 1536; 16-bit; little-endian byte order.

This data is part of a 'virtual testing' benchmark study, where samples are tested physically in the lab and their microscale accurate digital equivalent are tested virtually through simulation. The technique of converting 3D volumetric images directly into finite element method (FEM) meshes is part of the Image-Based Simulation (IBSim) approach.

This data is part of a batch of samples for thermal testing via laser flash analysis (LFA), following the standards ASTM E1461 / ASTM E2585. As part of the study, controlled defects were introduced into the samples. This was achieved by machining a disc shaped recess (of defined diameter and depth) into one disc which is bonded onto another disc, so that the defect is located internally within the final sample.

The samples in the batch are named as follows.

Sample ID Diameter Thickness Recess d Recess t
LFA_RNA_### 12.6 2.5 N/A N/A
LFA_Rd0t00_### 12.6 1.25 x 2 N/A N/A
LFA_Rd8t02_### 12.6 1.25 x 2 8.0 0.2
LFA_Rd8t08_### 12.6 1.25 x 2 8.0 0.8
LFA_Rd6t02_### 12.6 1.25 x 2 6.0 0.2
LFA_Rd6t08_### 12.6 1.25 x 2 6.0 0.8
LFA_Rd4t02_### 12.6 1.25 x 2 4.0 0.2
LFA_Rd4t08_### 12.6 1.25 x 2 4.0 0.8

Where ### denotes the furnace bonding batch (A-C and N for no bonding cycle) and sample number (01-30). Values in mm.

integrin subunit alpha L Predicted to enable metal ion binding activity. Predicted to act upstream of or within cell adhesion and integrin-mediated signaling pathway. Predicted to be located in membrane. Predicted to be part of integrin complex. https://www.xenbase.org/gene/showgene.do?method=display&geneId=6469565

Polymorphonuclear leukocyte (PMN) recruitment to vascular endothelium during acute inflammation involves cooperation between selectins, G-proteins, and beta2-integrins. LFA-1 (CD11a/CD18) affinity correlates with specific adhesion functions because a shift from low to intermediate affinity supports rolling on ICAM-1, whereas high affinity is associated with shear-resistant leukocyte arrest. We imaged PMN adhesion on cytokine-inflamed endothelium in a parallel-plate flow chamber to define the dynamics of beta2-integrin function during recruitment and transmigration. After arrest on inflamed endothelium, high-affinity LFA-1 aligned along the uropod-pseudopod major axis, which was essential for efficient neutrophil polarization and subsequent transmigration. An allosteric small molecule inhibitor targeted to the I-domain stabilized LFA-1 in an intermediate-affinity conformation, which supported neutrophil rolling but inhibited cell polarization and abrogated transmigration. We conclude that a shift in LFA-1 from intermediate to high affinity during the transition from rolling to arrest provides the contact-mediated signaling and guidance necessary for PMN transmigration on inflamed endothelium.