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  1. Article ; Online: Macrocystis pyrifera ferment-containing creams for optimizing facial skin rejuvenation.

    Gold, Michael / Bae, Yoon-Soo Cindy / Goldberg, David J / Jamal, Sumayah / Lewis, Amy B / Marchbein, Shari / Ros, Adriana / Santhanam, Uma / DiNatale, Lisa / Emmetsberger, Jaime

    Journal of cosmetic dermatology

    2023  Volume 22, Issue 12, Page(s) 3313–3319

    Abstract: Background: There is an increasing demand for facial skin rejuvenation. Specialized aesthetic skincare treatments may be one of the first steps to help prevent or treat facial signs of aging. This article discusses aesthetic skin care for facial skin ... ...

    Abstract Background: There is an increasing demand for facial skin rejuvenation. Specialized aesthetic skincare treatments may be one of the first steps to help prevent or treat facial signs of aging. This article discusses aesthetic skin care for facial skin rejuvenation, particularly data on two creams containing Macrocystis pyrifera ferment.
    Methods: The authors convened a dermatology advisory board to discuss challenges and practices in using skincare for facial rejuvenation, combining their expert opinion and experience on facial rejuvenation with preclinical and clinical data on two creams containing Macrocystis pyrifera ferment and a review of the literature.
    Results: Preclinical and clinical studies on Macrocystis pyrifera ferment and two creams containing the ferment exhibit anti-inflammatory, anti-aging, and healing properties. In preclinical studies, the ferment demonstrated collagen type I enhancing properties in ex vivo skin models, and skin cells treated with the ferment migrated faster than untreated cells in the in vitro study. In clinical studies measuring visible anti-inflammatory activity, the ferment alone and the ferment-containing products significantly decreased erythema, and in anti-aging studies, they improved visible skin aging parameters. Finally, in clinical studies on the stratum corneum, the two creams increased moisture levels and decreased transepidermal water loss (TEWL), reflecting healing by enhancing barrier strength and recovery.
    Conclusions: The Macrocystis pyrifera ferment and creams containing the ferment are effective skin care treatment products to decrease the visible effects of inflammation and signs of aging while promoting healing by enhancing barrier resilience and recovery.
    MeSH term(s) Humans ; Macrocystis ; Rejuvenation ; Skin ; Epidermis ; Dermatologic Agents ; Skin Aging ; Anti-Inflammatory Agents
    Chemical Substances Dermatologic Agents ; Anti-Inflammatory Agents
    Language English
    Publishing date 2023-12-02
    Publishing country England
    Document type Review ; Journal Article
    ZDB-ID 2280551-5
    ISSN 1473-2165 ; 1473-2130
    ISSN (online) 1473-2165
    ISSN 1473-2130
    DOI 10.1111/jocd.15986
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 6539: Show issues Location:
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  2. Article ; Online: Microglial inhibitory factor (MIF/TKP) mitigates secondary damage following spinal cord injury.

    Emmetsberger, Jaime / Tsirka, Stella E

    Neurobiology of disease

    2012  Volume 47, Issue 3, Page(s) 295–309

    Abstract: Spinal cord injury (SCI) induces an immune response during which microglia, the resident immunocompetent cells of the central nervous system, become activated and migrate to the site of damage. Depending on their state of activation, microglia secrete ... ...

    Abstract Spinal cord injury (SCI) induces an immune response during which microglia, the resident immunocompetent cells of the central nervous system, become activated and migrate to the site of damage. Depending on their state of activation, microglia secrete neurotoxic or neurotrophic factors that influence the surrounding environment and have a detrimental or restorative effect following SCI, including causing or protecting bystander damage to nearby undamaged tissue. Subsequent infiltration of macrophages contributes to the SCI outcome. We show here that suppressing microglia/macrophage activation using the tripeptide macrophage/microglia inhibitory factor (MIF/TKP) reduced secondary injury around the lesion epicenter in the murine dorsal hemisection model of SCI; it decreased the hypertrophic change of astrocytes and caused an increase in the number of axons present within the lesion epicenter. Moreover, timely inhibition of microglial/macrophage activation prevented demyelination and axonal dieback by modulating oligodendrocyte survival and oligodendrocyte precursor maturation. Microglia/macrophages located within or proximal to the lesion produced neurotoxic factors, such as tumor necrosis factor alpha (TNF-α). These results suggest that microglia/macrophages within the epicenter at early time points post injury are neurotoxic, contributing to demyelination and axonal degeneration and that MIF/TKP could be used in combination with other therapies to promote functional recovery.
    MeSH term(s) Animals ; Animals, Newborn ; Antigens/metabolism ; Autophagy-Related Proteins ; Axons/drug effects ; Axons/metabolism ; Axons/pathology ; Bromodeoxyuridine/metabolism ; Calcium-Binding Proteins/metabolism ; Cell Proliferation/drug effects ; Cells, Cultured ; Cholera Toxin ; Chondroitin Sulfate Proteoglycans/metabolism ; Coculture Techniques ; Cytokines/metabolism ; Disease Models, Animal ; Drug Administration Schedule ; Enzyme-Linked Immunosorbent Assay ; Gene Expression Regulation/drug effects ; Glial Fibrillary Acidic Protein/metabolism ; In Situ Nick-End Labeling ; Intracellular Signaling Peptides and Proteins/metabolism ; Ki-67 Antigen/metabolism ; Lipopolysaccharides/pharmacology ; Macrophage Activation/drug effects ; Mice ; Mice, Inbred C57BL ; Microfilament Proteins/metabolism ; Microglia/drug effects ; Microglia/ultrastructure ; Microscopy, Electron, Transmission ; Myelin Basic Protein/metabolism ; Neuroprotective Agents/therapeutic use ; Oligodendroglia/drug effects ; Oligodendroglia/physiology ; Oligopeptides/therapeutic use ; Peptide Fragments ; Proteoglycans/metabolism ; Spinal Cord Injuries/drug therapy ; Spinal Cord Injuries/pathology ; Time Factors
    Chemical Substances Aif1 protein, mouse ; Antigens ; Autophagy-Related Proteins ; Calcium-Binding Proteins ; Chondroitin Sulfate Proteoglycans ; Cytokines ; Glial Fibrillary Acidic Protein ; Intracellular Signaling Peptides and Proteins ; Ki-67 Antigen ; Lipopolysaccharides ; Microfilament Proteins ; Myelin Basic Protein ; Neuroprotective Agents ; Oligopeptides ; Peptide Fragments ; Proteoglycans ; Rb1cc1 protein, mouse ; cholera toxin B subunit (50-75) ; chondroitin sulfate proteoglycan 4 ; threonyl-lysyl-proline (41961-56-2) ; Cholera Toxin (9012-63-9) ; Bromodeoxyuridine (G34N38R2N1)
    Language English
    Publishing date 2012-05-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1211786-9
    ISSN 1095-953X ; 0969-9961
    ISSN (online) 1095-953X
    ISSN 0969-9961
    DOI 10.1016/j.nbd.2012.05.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 4444: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Personalized expression of bitter 'taste' receptors in human skin.

    Shaw, Lauren / Mansfield, Corrine / Colquitt, Lauren / Lin, Cailu / Ferreira, Jaime / Emmetsberger, Jaime / Reed, Danielle R

    PloS one

    2018  Volume 13, Issue 10, Page(s) e0205322

    Abstract: The integumentary (i.e., skin) and gustatory systems both function to protect the human body and are a first point of contact with poisons and pathogens. These systems may share a similar protective mechanism because, as we show here, both human taste ... ...

    Abstract The integumentary (i.e., skin) and gustatory systems both function to protect the human body and are a first point of contact with poisons and pathogens. These systems may share a similar protective mechanism because, as we show here, both human taste and skin cells express mRNA for bitter 'taste' receptors (TAS2Rs). We used gene-specific methods to measure mRNA from all known bitter receptor genes in adult human skin from freshly biopsied samples and from samples collected at autopsy from the Genotype-Tissue Expression project. Human skin expressed some but not all TAS2Rs, and for those that were expressed, the relative amounts differed markedly among individuals. For some TAS2Rs, mRNA abundance was related to presumed sun exposure based on the location from which the skin sample was collected (TAS2R14, TAS2R30, TAS2R42, and TAS2R60), sex (TAS2R3, TAS2R4, TAS2R8, TAS2R9, TAS2R14, and TAS2R60), and age (TAS2R5), although these effects were not large. These findings contribute to our understanding of extraoral expression of chemosensory receptors.
    MeSH term(s) Aged ; Aged, 80 and over ; Female ; Gene Expression Regulation/genetics ; Genotype ; HEK293 Cells ; Humans ; Integumentary System ; Male ; Middle Aged ; RNA, Messenger/genetics ; Receptors, Cell Surface/genetics ; Receptors, G-Protein-Coupled/genetics ; Skin/metabolism ; Taste/genetics ; Taste Buds/metabolism
    Chemical Substances RNA, Messenger ; Receptors, Cell Surface ; Receptors, G-Protein-Coupled ; TAS2R8 protein, human ; taste receptors, type 2
    Language English
    Publishing date 2018-10-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0205322
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Type III neuregulin 1 is required for multiple forms of excitatory synaptic plasticity of mouse cortico-amygdala circuits.

    Jiang, Li / Emmetsberger, Jaime / Talmage, David A / Role, Lorna W

    The Journal of neuroscience : the official journal of the Society for Neuroscience

    2013  Volume 33, Issue 23, Page(s) 9655–9666

    Abstract: The amygdala plays an important role in the formation and storage of memories associated with emotional events. The cortical glutamatergic inputs onto pyramidal neurons in the basolateral nucleus of the amygdala (BLA) contribute to this process. As the ... ...

    Abstract The amygdala plays an important role in the formation and storage of memories associated with emotional events. The cortical glutamatergic inputs onto pyramidal neurons in the basolateral nucleus of the amygdala (BLA) contribute to this process. As the interaction between neuregulin 1 (Nrg1) and its ErbB receptors has been implicated in the pathological mechanisms of schizophrenia, loss of Nrg1 may disrupt cortical-amygdala neural circuits, resulting in altered processing of salient memories. Here we show that Nrg1 is critical in multiple forms of plasticity of cortical projections to pyramidal neurons of the BLA. The miniature EPSCs in Nrg1 heterozygous animals have a faster time constant of decay and evoked synaptic currents have a smaller NMDA/AMPA ratio than those recorded in wild-type (WT) littermates. Both high-frequency electrical stimulation of cortical inputs and θ burst stimulation combined with nicotine exposure results in long-lasting potentiation in WT animals. However, the same manipulations have little to no effect on glutamatergic synaptic plasticity in the BLA from Nrg1 heterozygous mice. Comparison of WT, Nrg1 heterozygous animals and α7 nicotinic receptor heterozygous mice reveals that the sustained phase of potentiation of glutamatergic transmission after θ burst stimulation with or without nicotine only occurs in the WT mice. Together, these findings support the idea that type III Nrg1 is essential to multiple aspects of the modulation of excitatory plasticity at cortical-BLA synapses.
    MeSH term(s) Amygdala/physiology ; Animals ; Cerebral Cortex/physiology ; Excitatory Postsynaptic Potentials/physiology ; Female ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Nerve Net/physiology ; Neuregulin-1/physiology ; Neuronal Plasticity/physiology ; Organ Culture Techniques ; Synaptic Transmission/physiology
    Chemical Substances Neuregulin-1 ; Nrg1 protein, mouse
    Language English
    Publishing date 2013-06-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 604637-x
    ISSN 1529-2401 ; 0270-6474
    ISSN (online) 1529-2401
    ISSN 0270-6474
    DOI 10.1523/JNEUROSCI.2888-12.2013
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1668: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article: tPA-mediated generation of plasmin is catalyzed by the proteoglycan NG2.

    Nolin, Westley B / Emmetsberger, Jaime / Bukhari, Noreen / Zhang, Yan / Levine, Joel M / Tsirka, Stella E

    Glia

    2007  Volume 56, Issue 2, Page(s) 177–189

    Abstract: Paralysis resulting from spinal cord injury is devastating and persistent. One major reason for the inability of the body to heal this type of injury ensues from the local increase of glial cells leading to the formation of a glial scar, and the ... ...

    Abstract Paralysis resulting from spinal cord injury is devastating and persistent. One major reason for the inability of the body to heal this type of injury ensues from the local increase of glial cells leading to the formation of a glial scar, and the upregulation of chondroitin sulfate proteoglycans (CSPGs) at the site of injury through which axons are unable to regenerate. Experimental approaches to overcome this problem have accordingly focused on reducing the inhibitory properties of CSPGs, for example by using chondroitinase to remove the sugar chains and reduce the CSPGs to their core protein constituents, although this step alone does not provide dramatic benefits as a monotherapy. Using in vitro and in vivo approaches, we describe here a potentially synergistic therapeutic opportunity based on tissue plasminogen activator (tPA), an extracellular protease that converts plasminogen (plg) into the active protease plasmin. We show that tPA and plg both bind to the CSPG protein NG2, which functions as a scaffold to accelerate the tPA-driven conversion of plg to plasmin. The binding occurs via the tPA and plg kringle domains to domain 2 of the NG2 CSPG core protein, and is enhanced in some settings after chondroitinase-mediated removal of the NG2 proteoglycan side chains. Once generated, plasmin then degrades NG2, both in an in vitro setting using recombinant protein, and in vivo models of spinal cord injury. Our finding that the tPA and plg binding is in some instances more efficient after exposure of the NG2 proteoglycan to chondroitinase treatment suggests that a combined therapeutic approach employing both chondroitinase and the tPA/plasmin proteolytic system could be of significant benefit in promoting axonal regeneration through glial scars after spinal cord injury.
    MeSH term(s) Animals ; Antigens/drug effects ; Antigens/metabolism ; Antigens/pharmacology ; CHO Cells ; Chondroitinases and Chondroitin Lyases/pharmacology ; Cricetinae ; Cricetulus ; Disease Models, Animal ; Dose-Response Relationship, Drug ; Drug Interactions ; Female ; Fibrinolysin/metabolism ; Immunoprecipitation/methods ; Mice ; Mice, Inbred C57BL ; Pentosyltransferases/deficiency ; Protein Binding/drug effects ; Protein Structure, Tertiary/physiology ; Proteoglycans/drug effects ; Proteoglycans/metabolism ; Proteoglycans/pharmacology ; Recombinant Fusion Proteins ; Silver Staining/methods ; Spinal Cord Injuries/drug therapy ; Spinal Cord Injuries/metabolism ; Time Factors ; Tissue Plasminogen Activator/therapeutic use ; UDP Xylose-Protein Xylosyltransferase
    Chemical Substances Antigens ; Proteoglycans ; Recombinant Fusion Proteins ; chondroitin sulfate proteoglycan 4 ; Pentosyltransferases (EC 2.4.2.-) ; Tissue Plasminogen Activator (EC 3.4.21.68) ; Fibrinolysin (EC 3.4.21.7) ; Chondroitinases and Chondroitin Lyases (EC 4.2.2.-)
    Language English
    Publishing date 2007-11-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 639414-0
    ISSN 1098-1136 ; 0894-1491
    ISSN (online) 1098-1136
    ISSN 0894-1491
    DOI 10.1002/glia.20603
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2345: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  6. Article ; Online: Tissue plasminogen activator alters intracellular sequestration of zinc through interaction with the transporter ZIP4.

    Emmetsberger, Jaime / Mirrione, Martine M / Zhou, Chun / Fernandez-Monreal, Monica / Siddiq, Mustafa M / Ji, Kyungmin / Tsirka, Stella E

    The Journal of neuroscience : the official journal of the Society for Neuroscience

    2010  Volume 30, Issue 19, Page(s) 6538–6547

    Abstract: Glutamatergic neurons contain free zinc packaged into neurotransmitter-loaded synaptic vesicles. Upon neuronal activation, the vesicular contents are released into the synaptic space, whereby the zinc modulates activity of postsynaptic neurons though ... ...

    Abstract Glutamatergic neurons contain free zinc packaged into neurotransmitter-loaded synaptic vesicles. Upon neuronal activation, the vesicular contents are released into the synaptic space, whereby the zinc modulates activity of postsynaptic neurons though interactions with receptors, transporters and exchangers. However, high extracellular concentrations of zinc trigger seizures and are neurotoxic if substantial amounts of zinc reenter the cells via ion channels and accumulate in the cytoplasm. Tissue plasminogen activator (tPA), a secreted serine protease, is also proepileptic and excitotoxic. However, tPA counters zinc toxicity by promoting zinc import back into the neurons in a sequestered form that is nontoxic. Here, we identify the zinc influx transporter, ZIP4, as the pathway through which tPA mediates the zinc uptake. We show that ZIP4 is upregulated after excitotoxin stimulation of the mouse, male and female, hippocampus. ZIP4 physically interacts with tPA, correlating with an increased intracellular zinc influx and lysosomal sequestration. Changes in prosurvival signals support the idea that this sequestration results in neuroprotection. These experiments identify a mechanism via which neurons use tPA to efficiently neutralize the toxic effects of excessive concentrations of free zinc.
    MeSH term(s) Animals ; Cation Transport Proteins/metabolism ; Cell Line ; Cells, Cultured ; Female ; Hippocampus/drug effects ; Hippocampus/metabolism ; Humans ; In Vitro Techniques ; Intracellular Space/drug effects ; Intracellular Space/metabolism ; Lysosomes/drug effects ; Lysosomes/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Neurons/drug effects ; Neurons/metabolism ; Neurotoxins/toxicity ; Tissue Plasminogen Activator/deficiency ; Tissue Plasminogen Activator/genetics ; Tissue Plasminogen Activator/metabolism ; Zinc/metabolism
    Chemical Substances Cation Transport Proteins ; Neurotoxins ; Slc39a4 protein, mouse ; Tissue Plasminogen Activator (EC 3.4.21.68) ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2010-05-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 604637-x
    ISSN 1529-2401 ; 0270-6474
    ISSN (online) 1529-2401
    ISSN 0270-6474
    DOI 10.1523/JNEUROSCI.6250-09.2010
    Database MEDical Literature Analysis and Retrieval System OnLINE

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