| 1. |
- Lau, Daniela, et al.
(författare)
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The cartilage-specific lectin C-type lectin domain family 3 member A (CLEC3A) enhances tissue plasminogen activator-mediated plasminogen activation
- 2018
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Ingår i: Journal of Biological Chemistry. - 0021-9258. ; 293:1, s. 203-214
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Tidskriftsartikel (refereegranskat)abstract
- C-type lectin domain family 3 member A (CLEC3A) is a poorly characterized protein belonging to the superfamily of C-type lectins. Its closest homologue tetranectin binds to the kringle 4 domain of plasminogen and enhances its association with tissue plasminogen activator (tPA) thereby enhancing plasmin production, but whether CLEC3A contributes to plasminogen activation is unknown. Here, we recombinantly expressed murine and human full-length CLEC3As as well as truncated forms of CLEC3A in HEK-293 Epstein-Barr nuclear antigen (EBNA) cells. We analyzed the structure of recombinant CLEC3A by SDS-PAGE and immunoblot, glycan analysis, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, size-exclusion chromatography, circular dichroism spectroscopy, and electron microscopy; compared the properties of the recombinant protein with those of CLEC3A extracted from cartilage; and investigated its tissue distribution and extracellular assembly by immunohistochemistry and immunofluorescence microscopy. We found that CLEC3A mainly occurs as a monomer, but also forms dimers and trimers, potentially via a coiled-coil α-helix. We also noted that CLEC3A can be modified with chondroitin/dermatan sulfate side chains and tends to oligomerize to form higher aggregates. We show that CLEC3A is present in resting, proliferating, and hypertrophic growth-plate cartilage and assembles into an extended extracellular network in cultures of rat chondrosarcoma cells. Further, we found that CLEC3A specifically binds to plasminogen and enhances tPA-mediated plasminogen activation. In summary, we have determined the structure, tissue distribution, and molecular function of the cartilage-specific lectin CLEC3A and show that CLEC3A binds to plasminogen and participates in tPA-mediated plasminogen activation.
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| 2. |
- Mavroidis, Iakovos, et al.
(författare)
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ECOSCALE: Reconfigurable computing and runtime system for future exascale systems
- 2016
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Ingår i: 19th Design, Automation and Test in Europe Conference and Exhibition, DATE 2016, Dresden, Germany, 14-18 March 2016. - 1530-1591. - 9783981537062 ; , s. 696-701
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Konferensbidrag (refereegranskat)abstract
- In order to reach exascale performance, current HPC systems need to be improved. Simple hardware scaling is not a feasible solution due to the increasing utility costs and power consumption limitations. Apart from improvements in implementation technology, what is needed is to refine the HPC application development flow as well as the system architecture of future HPC systems. ECOSCALE tackles these challenges by proposing a scalable programming environment and architecture, aiming to substantially reduce energy consumption as well as data traffic and latency. ECOSCALE introduces a novel heterogeneous energy-efficient hierarchical architecture, as well as a hybrid many-core+OpenCL programming environment and runtime system. The ECOSCALE approach is hierarchical and is expected to scale well by partitioning the physical system into multiple independent Workers (i.e. compute nodes). Workers are interconnected in a tree-like fashion and define a contiguous global address space that can be viewed either as a set of partitions in a Partitioned Global Address Space (PGAS), or as a set of nodes hierarchically interconnected via an MPI protocol. To further increase energy efficiency, as well as to provide resilience, the Workers employ reconfigurable accelerators mapped into the virtual address space utilizing a dual stage System Memory Management Unit with coherent memory access. The architecture supports shared partitioned reconfigurable resources accessed by any Worker in a PGAS partition, as well as automated hardware synthesis of these resources from an OpenCL-based programming model.
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| 3. |
- Mayorca-Guiliani, Alejandro E, et al.
(författare)
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Decellularization and antibody staining of mouse tissues to map native extracellular matrix structures in 3D
- 2019
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Ingår i: Nature Protocols. - : Springer Science and Business Media LLC. - 1750-2799 .- 1754-2189. ; 14, s. 3395-3425
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Tidskriftsartikel (refereegranskat)abstract
- The extracellular matrix (ECM) is a major regulator of homeostasis and disease, yet the 3D structure of the ECM remains poorly understood because of limitations in ECM visualization. We recently developed an ECM-specialized method termed in situ decellularization of tissues (ISDoT) to isolate native 3D ECM scaffolds from whole organs in which ECM structure and composition are preserved. Here, we present detailed surgical instructions to facilitate decellularization of 33 different mouse tissues and details of validated antibodies that enable the visualization of 35 mouse ECM proteins. Through mapping of these ECM proteins, the structure of the ECM can be determined and tissue structures visualized in detail. In this study, perfusion decellularization is presented for bones, skeletal muscle, tongue, salivary glands, stomach, duodenum, jejunum/ileum, large intestines, mesentery, liver, gallbladder, pancreas, trachea, bronchi, lungs, kidneys, urinary bladder, ovaries, uterine horn, cervix, adrenal gland, heart, arteries, veins, capillaries, lymph nodes, spleen, peripheral nerves, eye, outer ear, mammary glands, skin, and subcutaneous tissue. Decellularization, immunostaining, and imaging take 4-5 d.
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