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- 저자 : Marie Morgan (검색결과 4 건)
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Rao, Anuradha,Kim, Eunjoon,Sheng, Morgan,Craig, Ann Marie 부산대학교 유전공학연구소 1998 분자생물학 연구보 Vol.14 No.-
To dertermine their roles in the assemly of glutamatergic postsynaptic sites, we studied the distributions of NMDA- and AMPA-type glutamate receptors; the NMDA receptorinteracting proteins α-actinin-2, PSD-95, and chapsyn;and the PSD-95-associated protein GKAP during the development of hippocampal nerons in culture. NMDA receptors first formed nonsynaptic proximal dendrite shaft clusters within 2-5 d. AMPA receptors were diffuse at this stage anf began to cluster on spines at 9-10 d. NMDA receptor clusters remained partially nonsynaptic and mainly distinct from AMPA receptor clusters until after 3 weeks in culture, when the two began to colocalize at spiny synatic sites. thus, the localization of NMDA and AMPA receptors must be regulated by different mechanisms. α-Actinin-2 colocalize with the NMDA receptor only at spiny synaptic clusters, but not at shrft nonsynaptic or synaptic clusters, suggesting a modulatory role in the anchoring of NMDA receptor at spines. PSD-95, chapsyn, and GKAP were present at some, but not all, nonsynaptic NMDA receptor clusters during the first 2 weeks, indicating that none is essential for NMDA receptor cluster formation. When NMDA receptor clusters becames synaptic, PSD-95 and GKAP were always present, consistent with an essential function in synaptic localization of NMDA receptors. Furthermore, PSD-95 and GKAP clustered opposite presynaptic terminals serveral days before either NMDA or AMPA receptors clustered at these presumptive postsynaptic sites. These results suggest that synapse development proceeds by formation of a postsynaptic scaffold containing PSD-95 and GKAP in concert with presynaptic vesicle clustering, followed by regulated attachment of glutamate receptor subtypes to this scaffold.
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Discovery Elbow System arthroplasty polyethylene bearing exchange: outcomes and experience
Daniel L J Morris,Katherine Walstow,Lisa Pitt,Marie Morgan,Amol A Tambe,David I Clark,Timothy Cresswell,Marius P Espag 대한견주관절학회 2024 대한견주관절의학회지 Vol.27 No.1
Background: The Discovery Elbow System (DES) utilizes a polyethylene bearing within the ulnar component. An exchange bearing requires preoperative freezing and implantation within 2 minutes of freezer removal to allow insertion. We report our outcomes and experience using this technique. Methods: This was an analysis of a two-surgeon consecutive series of DES bearing exchange. Inclusion criteria included patients in which exchange was attempted with a minimum 1-year follow-up. Clinical and radiographic review was performed 1, 2, 3, 5, 8 and 10 years postoperative. Outcome measures included range of movement, Oxford Elbow Score (OES), Mayo Elbow Performance Score (MEPS), complications and requirement for revision surgery. Results: Eleven DESs in 10 patients were included. Indications were bearing wear encountered during humeral component revision (n=5); bearing failure (n=4); and infection treated with debridement, antibiotics and implant retention (DAIR; n=2). Bearing exchange was conducted on the first attempt in 10 cases. One case required a second attempt. One patient developed infection postoperatively managed with two-stage revision. Mean follow-up of the bearing exchange DES was 3 years. No further surgery was required, with no infection recurrence in DAIR cases. Mean elbow flexion-extension and pronosupination arcs were 107° (±22°) and 140° (±26°). Mean OES was 36/48 (±12) and MEPS was 83/100 (±19). Conclusions: Our results support the use of DES bearing exchange in cases of bearing wear with well-fixed stems or acute infection. This series provides surgeons managing DES arthroplasty with management principles, successful and reproducible surgical techniques and expected clinical outcomes in performing DES polyethylene bearing exchange. Level of evidence: IV.
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Naisbitt, Scott,Kim, Eunjoon,Weinberg, Richard J.,Rao, Anuradha,Yang, Fu-Chia,Craig, Ann Marie,Sheng, Morgan 부산대학교 유전공학연구소 1997 분자생물학 연구보 Vol.13 No.-
The structure of central synapses in poorly understood at the molecular level. A recent advance came with the identification of the postsynaptic density-95(PSD-95)/synapse-associated protein 90 family of proteins as important mediators of the synaptic clustering of certain classes of ion channels, By yeast two-hybrid screening, a novel oritein termed guanylate kinase-associated protein(GKAP) has been isolated that binds to the GK-like domain of PSD-95(Kim et al.,1997). Here we present a detailed characterization of GKAP expression in the rat brain and report the cloning of a novel GKAP splic variant. By Northern blot,GKAP mRNAs(4,6.5,and 8kB) are expressed predominantly in the rat brain. By in situ hydridization,GKAP is expressed widely in neurons of cortex and hippocampus and in the Purkinje and granule cells of the cerebellum. On brain immunoblots, two prominent bands of 95 and 130 kDa are detected that correspond to products of short and long N-terminal splic variants of GKAP. Two independent GKAP antibodies label somatodendritic puncta in neocortical and hippocampal neurons in a pattern consistent with synaptic elements. Immunogold electron microscopy reveals GKAP to be predominantly postsynptic and present at asymmetric synapses and in dendritic spines. The distribution of GKAP immunogold particles is uniform in the lateral plane of the PSD but peaks in the perpendicular axis∼20nm from the postsynaotic menbrane. In cultured hippocampal neurons GKAP immunoreactive puncta colocalize with the AMPA receptor subunit Glu receptor 1 but not with the GABA_A receptor subunil β2and β3. Thus GKAP is a widely expressed neuronal protein localized specifically in the PSD of glutamatergic synapses, consistent with its direct interaction with PSD-95 family proteins.
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Kim, Eunjoon,Naisbitt, Scott,Hsueh, Yi-Ping,Rao, Anuradha,Rothschild, Adam,Graig, Ann Marie,Sheng, Morgan 부산대학교 유전공학연구소 1997 분자생물학 연구보 Vol.13 No.-
The molecular mechanisms underlying the organization of ion channels and signsling molecules at the synaptic junction are largely unknown. Recently, members of the PSD-95/SAP90 family of synaptic MAGUK(menbrane-acssociated guanylate kinase) proteins have been shown to interact. via their NH_2-terminal PDZ domains, with certain ion channels(NMDA receptors and K^+channels). thereby promoting the clustering of these proteins. Although the function of the NH_2-terminal PDZ domains in relatively well characterized, the function of the Src homology 3(SH3) domain and the guanylate kinase-like(GK)domain in the COOH-terminal half of PSD-95 has remained obscure. WE now repoet the isolation of a novel synaptic protein. termed GKAP for guanylate kinase-associated protein. that binds directly to the GK domain of the known members of the mammalian PSD-95 family. GKAP shows a unique domain structure and appear to be a major constituent of the postsynaptic density. GKAP colocalizes and coimmunoprecipitates with PSD-95 in vivo,and colusters with PSD-95 and K^+ channels/parent lack of guanylate kinase enzymatic activity, the fact that the GK domain can as a site for protein-protein interaction has implications for the function of diverse GK-containing proteins(such as p55,ZO-1,and LIN-2/CASK).
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