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  1. Article: Highly sensitive

    Mikati, Marwa O / Erdmann-Gilmore, Petra / Connors, Rose / Conway, Sineadh M / Malone, Jim / Woods, Justin / Sprung, Robert W / Reid Townsend, R / Al-Hasani, Ream

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Enkephalins are opioid peptides that modulate analgesia, reward, and stress. ...

    Abstract Enkephalins are opioid peptides that modulate analgesia, reward, and stress.
    Language English
    Publishing date 2023-08-02
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.02.15.528745
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Requirements for the selective degradation of endoplasmic reticulum-resident major histocompatibility complex class I proteins by the viral immune evasion molecule mK3.

    Wang, Xiaoli / Connors, Rose / Harris, Michael R / Hansen, Ted H / Lybarger, Lonnie

    Journal of virology

    2005  Volume 79, Issue 7, Page(s) 4099–4108

    Abstract: Recent studies suggest that certain viral proteins co-opt endoplasmic reticulum (ER) degradation pathways to prevent the surface display of major histocompatibility complex class I molecules to the immune system. A novel example of such a molecule is the ...

    Abstract Recent studies suggest that certain viral proteins co-opt endoplasmic reticulum (ER) degradation pathways to prevent the surface display of major histocompatibility complex class I molecules to the immune system. A novel example of such a molecule is the mK3 protein of gammaherpesvirus 68. mK3 belongs to an extensive family of structurally similar viral and cellular proteins that function as ubiquitin ligases using a conserved RING-CH domain. In the specific case of mK3, it selectively targets the rapid degradation of nascent class I heavy chains in the ER while they are associated with the class I peptide-loading complex (PLC). We present here evidence that the PLC imposes a relative proximity and/or orientation on the RING-CH domain of mK3 that is required for it to specifically target class I molecules for degradation. Furthermore, we demonstrate that full assembly of class I molecules with peptide is not a prerequisite for mK3-mediated degradation. Surprisingly, although the cytosolic tail of class I is required for rapid mK3-mediated degradation, we observed that a class I mutant lacking lysine residues in its cytosolic tail was ubiquitinated and degraded in the presence of mK3 in a manner indistinguishable from wild-type class I molecules. These findings are consistent with a "partial dislocation" model for turnover of ER proteins and define some common features of ER degradation pathways initiated by structurally distinct herpesvirus proteins.
    MeSH term(s) Animals ; Antiporters/metabolism ; Cell Line ; Endoplasmic Reticulum/metabolism ; Gammaherpesvirinae/immunology ; Gammaherpesvirinae/pathogenicity ; Histocompatibility Antigens Class I/metabolism ; Immunoglobulins/metabolism ; Membrane Proteins/metabolism ; Membrane Transport Proteins ; Mice ; Protein Structure, Tertiary ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/physiology ; Viral Proteins/physiology
    Chemical Substances Antiporters ; Histocompatibility Antigens Class I ; Immunoglobulins ; Membrane Proteins ; Membrane Transport Proteins ; Ubiquitin ; Viral Proteins ; tapasin ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2005-04
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.79.7.4099-4108.2005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class I and the peptide-loading complex.

    Wang, Xiaoli / Lybarger, Lonnie / Connors, Rose / Harris, Michael R / Hansen, Ted H

    Journal of virology

    2004  Volume 78, Issue 16, Page(s) 8673–8686

    Abstract: The mK3 protein of gammaherpesvirus 68 and the kK5 protein of Kaposi's sarcoma-associated herpesvirus are members of a family of structurally related viral immune evasion molecules that all possess a RING-CH domain with ubiquitin ligase activity. These ... ...

    Abstract The mK3 protein of gammaherpesvirus 68 and the kK5 protein of Kaposi's sarcoma-associated herpesvirus are members of a family of structurally related viral immune evasion molecules that all possess a RING-CH domain with ubiquitin ligase activity. These proteins modulate the expression of major histocompatibility complex class I molecules (mK3 and kK5) as well as other molecules like ICAM-1 and B7.2 (kK5). Previously, mK3 was shown to ubiquitinate nascent class I molecules, resulting in their rapid degradation, and this process was found to be dependent on TAP and tapasin, endoplasmic reticulum molecules involved in class I assembly. Here, we demonstrate that in murine cells, kK5 does not affect class I expression but does downregulate human B7.2 molecules in a TAP/tapasin-independent manner. These differences in substrate specificity and TAP/tapasin dependence between mK3 and kK5 permitted us, using chimeric molecules, to map the sites of mK3 interaction with TAP/tapasin and to determine the requirements for substrate recognition by mK3. Our findings indicate that mK3 interacts with TAP1 and -2 via their C-terminal domains and with class I molecules via their N-terminal domains. Furthermore, by orienting the RING-CH domain of mK3 appropriately with respect to class I, mK3 binding to TAP/tapasin, rather than the presence of unique sequences in class I, appears to be the primary determinant of substrate specificity.
    MeSH term(s) ATP-Binding Cassette Sub-Family B Member 2 ; ATP-Binding Cassette Transporters/metabolism ; Amino Acid Sequence ; Animals ; Antigens, CD/metabolism ; Antiporters/metabolism ; B7-2 Antigen ; Down-Regulation ; Gammaherpesvirinae/metabolism ; Gammaherpesvirinae/pathogenicity ; Herpesvirus 8, Human/metabolism ; Herpesvirus 8, Human/pathogenicity ; Histocompatibility Antigens Class I/metabolism ; Humans ; Immunoglobulins/metabolism ; Membrane Glycoproteins/metabolism ; Membrane Transport Proteins ; Mice ; Models, Molecular ; Molecular Sequence Data ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Ubiquitin-Protein Ligases/chemistry ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances ATP-Binding Cassette Sub-Family B Member 2 ; Antigens, CD ; Antiporters ; B7-2 Antigen ; CD86 protein, human ; Cd86 protein, mouse ; Histocompatibility Antigens Class I ; Immunoglobulins ; Membrane Glycoproteins ; Membrane Transport Proteins ; Recombinant Fusion Proteins ; TAP1 protein, human ; Tap1 protein, mouse ; Viral Proteins ; tapasin ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2004-08
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/JVI.78.16.8673-8686.2004
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  4. Article ; Online: β-amyloid dynamics in human plasma.

    Huang, Yafei / Potter, Rachel / Sigurdson, Wendy / Kasten, Tom / Connors, Rose / Morris, John C / Benzinger, Tammie / Mintun, Mark / Ashwood, Tim / Ferm, Mats / Budd, Samantha L / Bateman, Randall J

    Archives of neurology

    2012  Volume 69, Issue 12, Page(s) 1591–1597

    Abstract: Objectives: To investigate dynamic changes in human plasma β-amyloid (Aβ) concentrations, evaluate the effects of aging and amyloidosis on these dynamics, and determine their correlation with cerebrospinal fluid (CSF) Aβ concentrations.: Design: A ... ...

    Abstract Objectives: To investigate dynamic changes in human plasma β-amyloid (Aβ) concentrations, evaluate the effects of aging and amyloidosis on these dynamics, and determine their correlation with cerebrospinal fluid (CSF) Aβ concentrations.
    Design: A repeated plasma and CSF sampling study.
    Setting: The Washington University School of Medicine in St Louis, Missouri.
    Participants: Older adults with amyloid deposition (Amyloid+), age-matched controls without amyloid deposition (Amyloid-), and younger normal controls (YNCs) were enrolled for the study.
    Main outcome measures: Hourly measurements of plasma Aβ were compared between groups by age and amyloidosis. Plasma Aβ and CSF Aβ concentrations were compared for correlation, linear increase, and circadian patterns.
    Results: Circadian patterns were observed in plasma Aβ, with diminished amplitudes with aging. Linear increase of Aβ was only observed for CSF Aβ in the YNC and Amyloid- groups, but not in the Amyloid+ group. No linear increase was observed for plasma Aβ. No significant correlations were found between plasma and CSF Aβ concentrations.
    Conclusions: Plasma Aβ, like CSF, demonstrates a circadian pattern that is reduced in amplitude with increasing age but is unaffected by amyloid deposition. However, we found no evidence that plasma and CSF Aβ concentrations were related on an hourly or individual basis.
    MeSH term(s) Adult ; Aged ; Aged, 80 and over ; Aging/blood ; Aging/cerebrospinal fluid ; Amyloid beta-Peptides/blood ; Amyloid beta-Peptides/cerebrospinal fluid ; Case-Control Studies ; Female ; Humans ; Male ; Middle Aged ; Nonlinear Dynamics ; Peptide Fragments/blood ; Peptide Fragments/cerebrospinal fluid ; Statistics as Topic ; Young Adult
    Chemical Substances Amyloid beta-Peptides ; Peptide Fragments ; amyloid beta-protein (1-40) ; amyloid beta-protein (1-42)
    Language English
    Publishing date 2012-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80049-1
    ISSN 1538-3687 ; 0003-9942
    ISSN (online) 1538-3687
    ISSN 0003-9942
    DOI 10.1001/archneurol.2012.18107
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  5. Article ; Online: Amyloid-β efflux from the central nervous system into the plasma.

    Roberts, Kaleigh Filisa / Elbert, Donald L / Kasten, Tom P / Patterson, Bruce W / Sigurdson, Wendy C / Connors, Rose E / Ovod, Vitaliy / Munsell, Ling Y / Mawuenyega, Kwasi G / Miller-Thomas, Michelle M / Moran, Christopher J / Cross, Dewitte T / Derdeyn, Colin P / Bateman, Randall J

    Annals of neurology

    2014  Volume 76, Issue 6, Page(s) 837–844

    Abstract: Objective: The aim of this study was to measure the flux of amyloid-β (Aβ) across the human cerebral capillary bed to determine whether transport into the blood is a significant mechanism of clearance for Aβ produced in the central nervous system (CNS).! ...

    Abstract Objective: The aim of this study was to measure the flux of amyloid-β (Aβ) across the human cerebral capillary bed to determine whether transport into the blood is a significant mechanism of clearance for Aβ produced in the central nervous system (CNS).
    Methods: Time-matched blood samples were simultaneously collected from a cerebral vein (including the sigmoid sinus, inferior petrosal sinus, and the internal jugular vein), femoral vein, and radial artery of patients undergoing inferior petrosal sinus sampling. For each plasma sample, Aβ concentration was assessed by 3 assays, and the venous to arterial Aβ concentration ratios were determined.
    Results: Aβ concentration was increased by ∼7.5% in venous blood leaving the CNS capillary bed compared to arterial blood, indicating efflux from the CNS into the peripheral blood (p < 0.0001). There was no difference in peripheral venous Aβ concentration compared to arterial blood concentration.
    Interpretation: Our results are consistent with clearance of CNS-derived Aβ into the venous blood supply with no increase from a peripheral capillary bed. Modeling these results suggests that direct transport of Aβ across the blood-brain barrier accounts for ∼25% of Aβ clearance, and reabsorption of cerebrospinal fluid Aβ accounts for ∼25% of the total CNS Aβ clearance in humans. Ann Neurol 2014;76:837-844.
    MeSH term(s) Adult ; Amyloid beta-Peptides/blood ; Biomarkers/blood ; Biomarkers/metabolism ; Blood-Brain Barrier/metabolism ; Brain/metabolism ; Central Nervous System/metabolism ; Female ; Humans ; Male ; Middle Aged ; Protein Transport/physiology
    Chemical Substances Amyloid beta-Peptides ; Biomarkers
    Language English
    Publishing date 2014-10-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80362-5
    ISSN 1531-8249 ; 0364-5134
    ISSN (online) 1531-8249
    ISSN 0364-5134
    DOI 10.1002/ana.24270
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    Zs.MO 478: Show issues

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