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  1. Article ; Online: Binary effects of intravascular laser irradiation of blood on motor recovery and homocysteine reduction in a case with ischemic hemiparesis: portrayed with brain perfusion images.

    Li, Sheng-Wen A / Lin, Yen-Po / Hsieh, Shih-Po / Chang, Shin-Tsu

    BMC neurology

    2022  Volume 22, Issue 1, Page(s) 370

    Abstract: Background: Stroke is a burdensome cerebral eventthat affects many aspects of daily activities such as motion, speech, memory, vision, and cognition. Intravascular laser irradiation of blood (ILIB) is a novel therapy, going beyond conventional ... ...

    Abstract Background: Stroke is a burdensome cerebral eventthat affects many aspects of daily activities such as motion, speech, memory, vision, and cognition. Intravascular laser irradiation of blood (ILIB) is a novel therapy, going beyond conventional rehabilitation modalities, that is effective in stroke recovery. Homocysteine ​​is an important risk factor associated with stroke. However, there are few studies that examine the relationship between ILIB treatment and the level of homocysteine. In recent years, researchers use the single-photon emission computed tomography (SPECT) scan of the brain to evaluate stroke patients and patients with a neurologicdeficit. The present report investigates the clinical effect of ILIB treatment on the level of serum homocysteine, the perfusion change of impaired brain region via SPECT, and the patient's neurologic appearance.
    Casepresentation: We focus on a case of a 62-year-old man with subacute stroke accompanied with left hemiparesis and hyperhomocysteinemia, who showed dramatic improvement in muscle power, a decreasing level of homocysteine, and increased blood flow of the right cerebral after three-courseILIB treatment.
    Conclusion: We found that ILIB is effective in lowering serum levels of homocysteine and facilitating cerebral circulation for the patient with subacute stroke.
    MeSH term(s) Brain/blood supply ; Cerebrovascular Circulation ; Homocysteine ; Humans ; Ischemia ; Lasers ; Male ; Middle Aged ; Paresis/complications ; Perfusion/adverse effects ; Stroke/complications ; Stroke/diagnostic imaging ; Tomography, Emission-Computed, Single-Photon/methods
    Chemical Substances Homocysteine (0LVT1QZ0BA)
    Language English
    Publishing date 2022-09-27
    Publishing country England
    Document type Case Reports ; Journal Article
    ZDB-ID 2041347-6
    ISSN 1471-2377 ; 1471-2377
    ISSN (online) 1471-2377
    ISSN 1471-2377
    DOI 10.1186/s12883-022-02896-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: HAI-1 is required for the novel role of FGFBP1 in maintenance of cell morphology and F-actin rearrangement in human keratinocytes.

    Lu, Dajun D / Huang, Nanxi / Li, Sheng-Wen A / Fang, Jessica R / Lai, Chih-Hsin / Wang, Jehng-Kang / Chan, Khee-Siang / Johnson, Michael D / Lin, Chen-Yong

    Human cell

    2023  Volume 36, Issue 4, Page(s) 1403–1415

    Abstract: Formation and maintenance of skin barrier function require tightly controlled membrane-associated proteolysis, in which the integral membrane Kunitz-type serine protease inhibitor, HAI-1, functions as the primary inhibitor of the membrane-associated ... ...

    Abstract Formation and maintenance of skin barrier function require tightly controlled membrane-associated proteolysis, in which the integral membrane Kunitz-type serine protease inhibitor, HAI-1, functions as the primary inhibitor of the membrane-associated serine proteases, matriptase and prostasin. Previously, HAI-1 loss in HaCaT human keratinocytes resulted in an expected increase in prostasin proteolysis but a paradoxical decrease in matriptase proteolysis. The paradoxical decrease in shed active matriptase is further investigated in this study with an unexpected discovery of novel functions of fibroblast growth factor-binding protein 1 (FGFBP1), which acts as an extracellular ligand that can rapidly elicit F-actin rearrangement and subsequently affect the morphology of human keratinocytes. This novel growth factor-like function is in stark contrast to the canonical activity of this protein through interactions with FGFs for its pathophysiological functions. This discovery began with the observation that HAI-1 KO HaCaT cells lose the characteristic cobblestone morphology of the parental cells and exhibit aberrant F-actin formation along with altered subcellular targeting of matriptase and HAI-2. The alterations in cell morphology and F-actin status caused by targeted HAI-1 deletion can be restored by treatment with conditioned medium from parental HaCaT cells, in which FGFBP1 was identified by tandem mass spectrometry. Recombinant FGFBP1 down to 1 ng/ml was able to revert the changes caused by HAI-1 loss. Our study reveals a novel function of FGFBP1 in the maintenance of keratinocyte morphology, which depends on HAI-1.
    MeSH term(s) Humans ; Actins/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Keratinocytes/metabolism ; Proteolysis ; Proteinase Inhibitory Proteins, Secretory/metabolism ; Intercellular Signaling Peptides and Proteins/metabolism
    Chemical Substances Actins ; Membrane Glycoproteins ; Proteinase Inhibitory Proteins, Secretory ; FGFBP1 protein, human (139946-12-6) ; Intercellular Signaling Peptides and Proteins
    Language English
    Publishing date 2023-04-19
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 1149134-6
    ISSN 1749-0774 ; 0914-7470
    ISSN (online) 1749-0774
    ISSN 0914-7470
    DOI 10.1007/s13577-023-00906-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3676: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Targeted deletion of HAI-1 increases prostasin proteolysis but decreases matriptase proteolysis in human keratinocytes.

    Lu, Dajun D / Gu, Yayun / Li, Sheng-Wen A / Barndt, Robert J / Huang, Shih-Ming / Wang, Jehng-Kang / Su, Hui Chen / Johnson, Michael D / Lin, Chen-Yong

    Human cell

    2021  Volume 34, Issue 3, Page(s) 771–784

    Abstract: Epidermal differentiation and barrier function require well-controlled matriptase and prostasin proteolysis, in which the Kunitz-type serine protease inhibitor HAI-1 represents the primary enzymatic inhibitor for both proteases. HAI-1, however, also ... ...

    Abstract Epidermal differentiation and barrier function require well-controlled matriptase and prostasin proteolysis, in which the Kunitz-type serine protease inhibitor HAI-1 represents the primary enzymatic inhibitor for both proteases. HAI-1, however, also functions as a chaperone-like protein necessary for normal matriptase synthesis and intracellular trafficking. Furthermore, other protease inhibitors, such as antithrombin and HAI-2, can also inhibit matriptase and prostasin in solution or in keratinocytes. It remains unclear, therefore, whether aberrant increases in matriptase and prostasin enzymatic activity would be the consequence of targeted deletion of HAI-1 and so subsequently contribute to the epidermal defects observed in HAI-1 knockout mice. The impact of HAI-1 deficiency on matriptase and prostasin proteolysis was, here, investigated in HaCaT human keratinocytes. Our results show that HAI-1 deficiency causes an increase in prostasin proteolysis via increased protein expression and zymogen activation. It remains unclear, however, whether HAI-1 deficiency increases "net" prostasin enzymatic activity because all of the activated prostasin was detected in complexes with HAI-2, suggesting that prostasin enzymatic activity is still under tight control in HAI-1-deficient keratinocytes. Matriptase proteolysis is, however, unexpectedly suppressed by HAI-1 deficiency, as manifested by decreases in zymogen activation, shedding of active matriptase, and matriptase-dependent prostasin zymogen activation. This suppressed proteolysis results mainly from the reduced ability of HAI-1-deficient HaCaT cells to activate matriptase and the rapid inhibition of nascent active matriptase by HAI-2 and other yet-to-be-identified protease inhibitors. Our study provides novel insights with opposite impacts by HAI-1 deficiency on matriptase versus prostasin proteolysis in keratinocytes.
    MeSH term(s) Gene Deletion ; HaCaT Cells ; Humans ; Keratinocytes/metabolism ; Proteinase Inhibitory Proteins, Secretory/deficiency ; Proteinase Inhibitory Proteins, Secretory/genetics ; Proteinase Inhibitory Proteins, Secretory/physiology ; Proteolysis ; Serine Endopeptidases/metabolism ; Skin/cytology ; Skin/metabolism
    Chemical Substances Proteinase Inhibitory Proteins, Secretory ; SPINT1 protein, human ; Serine Endopeptidases (EC 3.4.21.-) ; matriptase (EC 3.4.21.-) ; prostasin (EC 3.4.21.-)
    Language English
    Publishing date 2021-01-24
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 1149134-6
    ISSN 1749-0774 ; 0914-7470
    ISSN (online) 1749-0774
    ISSN 0914-7470
    DOI 10.1007/s13577-021-00488-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3676: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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