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  • Life and Medical Sciences  (2)
  • Shallow convection  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 32 (1986), S. 281-291 
    ISSN: 0730-2312
    Keywords: protease nexin ; cellular binding sites ; extracellular matrix ; elastase ; thrombin ; urokinase ; fibroblasts ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: This review summarizes the mechanisms by which several serine proteases, particularly urokinase, thrombin, and elastase, interact with cultured fibroblasts. Many of these studies were prompted by findings that interactions of these proteases with cells and the extracellular matrix are important in a number of physiologic and pathologic processes. Two main pathways have been identified for specific interactions of these proteases with fibroblasts. One involves surface binding sites for the free protease that appear to bind only one particular protease. An unusual feature collectively shared by the binding sites for urokinase, thrombin, and elastase is that the bound protease is not detectably internalized by the fibroblasts. The other pathway by which serine proteases interact with fibroblasts involves proteins named protease nexins (PNs). Three PNs have been identified. They are secreted by fibroblasts and inhibit certain serine proteases by forming a covalent complex with the protease catalytic site serine. The complexes then bind back to the fibroblasts via the PN portion of the complex and are internalized and degraded. Recent studies showing that the fibroblast surface and extracellular matrix accelerate the inactivation of thrombin by PN-1 support the hypothesis that the PNs control protease activity at and near the cell surface. The PNs differ from plasma protease inhibitors in their molecular properties, absence in plasma, site of synthesis, and site of clearance of the inhibitor:protease complexes.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 134 (1988), S. 179-188 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Protease nexin-1 (PN-1) is a protease inhibitor that is secreted by fibroblasts and several other cultured cells. PN-1 forms complexes with certain serine proteases in the extracellular environment including thrombin, urokinase, and plasmin. The complexes then bind to the cells and are rapidly internalized and degraded. This report demonstrates that PN-1 is present on the surface of fibroblasts, bound to the extracellular matrix. Immunofluorescent studies showed that PN-1 colocalized with fibronectin on both intact cells and in preparations of extracellular matrix made from these cells. In contrast, PN-1 did not colocalize with the epidermal growth factor receptor, a plasma membrane marker. An enzyme-lined immunosorbent assay was developed which showed that the extracellular matrix contained at least 60-80% of the cellular immunoreactive PN-1. Extraction of the matrix with 2 M NaCl removed PN-1 in a form which reacted with 125l-thrombin to form complexes which were immunoprecipitated by anti-PN-1 lgG and were of identical size as complexes made from soluble PN-1 and 125l-thrombin. These data indicate that in addition to its role as a soluble protease inhibitor, PN-1 is also a component of the extracellular matrix and might control its proteolysis.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Publication Date: 2022-05-26
    Description: © The Author(s), 2017. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Surveys in Geophysics 38 (2017): 1529–1568, doi:10.1007/s10712-017-9428-0.
    Description: Trade-wind cumuli constitute the cloud type with the highest frequency of occurrence on Earth, and it has been shown that their sensitivity to changing environmental conditions will critically influence the magnitude and pace of future global warming. Research over the last decade has pointed out the importance of the interplay between clouds, convection and circulation in controling this sensitivity. Numerical models represent this interplay in diverse ways, which translates into different responses of trade-cumuli to climate perturbations. Climate models predict that the area covered by shallow cumuli at cloud base is very sensitive to changes in environmental conditions, while process models suggest the opposite. To understand and resolve this contradiction, we propose to organize a field campaign aimed at quantifying the physical properties of trade-cumuli (e.g., cloud fraction and water content) as a function of the large-scale environment. Beyond a better understanding of clouds-circulation coupling processes, the campaign will provide a reference data set that may be used as a benchmark for advancing the modelling and the satellite remote sensing of clouds and circulation. It will also be an opportunity for complementary investigations such as evaluating model convective parameterizations or studying the role of ocean mesoscale eddies in air–sea interactions and convective organization.
    Description: The EUREC4A project is supported by the European Research Council (ERC), under the European Union’s Horizon 2020 research and innovation programme (Grant Agreement No. 694768), by the Max Planck Society and by DFG (Deutsche Forschungsgemeinschaft, German Research Foundation) Priority Program SPP 1294.
    Keywords: Trade-wind cumulus ; Shallow convection ; Cloud feedback ; Atmospheric circulation ; Field campaign
    Repository Name: Woods Hole Open Access Server
    Type: Article
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