scholarly journals The Novel Membrane Protein TMEM59 Modulates Complex Glycosylation, Cell Surface Expression, and Secretion of the Amyloid Precursor Protein

2010 ◽  
Vol 285 (27) ◽  
pp. 20664-20674 ◽  
Author(s):  
Sylvia Ullrich ◽  
Anna Münch ◽  
Stephanie Neumann ◽  
Elisabeth Kremmer ◽  
Jörg Tatzelt ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Amyloid Precursor Protein ◽  
Surface Expression ◽  
Precursor Protein ◽  
Cell Surface Expression ◽  
The Novel

scholarly journals Amyloid Precursor Protein Enhances Nav1.6 Sodium Channel Cell Surface Expression

2015 ◽  
Vol 290 (19) ◽  
pp. 12048-12057 ◽  
Author(s):  
Chao Liu ◽  
Francis Chee Kuan Tan ◽  
Zhi-Cheng Xiao ◽  
Gavin S. Dawe
Keyword(s):  
Cell Surface ◽  
Amyloid Precursor Protein ◽  
Sodium Channel ◽  
Surface Expression ◽  
Precursor Protein ◽  
Cell Surface Expression

scholarly journals Secreted Amyloid Precursor Protein-Alpha Enhances LTP Through the Synthesis and Trafficking of Ca2+-Permeable AMPA Receptors

2021 ◽  
Vol 14 ◽  
Author(s):  
Rhys W. Livingstone ◽  
Megan K. Elder ◽  
Anurag Singh ◽  
Courteney M. Westlake ◽  
Warren P. Tate ◽  
...  
Keyword(s):  
Cell Surface ◽  
Amyloid Precursor Protein ◽  
De Novo ◽  
Hippocampal Slices ◽  
Long Term Potentiation ◽  
Surface Expression ◽  
Receptor Expression ◽  
Precursor Protein ◽  
Cell Surface Expression ◽  
Proximity Ligation Assay

Regulation of AMPA receptor expression by neuronal activity and neuromodulators is critical to the expression of both long-term potentiation (LTP) and memory. In particular, Ca2+-permeable AMPARs (CP-AMPAR) play a unique role in these processes due to their transient, activity-regulated expression at synapses. Secreted amyloid precursor protein-alpha (sAPPα), a metabolite of the parent amyloid precursor protein (APP) has been previously shown to enhance hippocampal LTP as well as memory formation in both normal animals and in Alzheimer’s disease models. In earlier work we showed that sAPPα promotes trafficking of GluA1-containing AMPARs to the cell surface and specifically enhances synthesis of GluA1. To date it is not known whether de novo synthesized GluA1 form CP-AMPARs or how they contribute to sAPPα-mediated plasticity. Here, using fluorescent non-canonical amino acid tagging–proximity ligation assay (FUNCAT-PLA), we show that brief treatment of primary rat hippocampal neurons with sAPPα (1 nM, 30 min) rapidly enhanced the cell-surface expression of de novo GluA1 homomers and reduced levels of de novo GluA2, as well as extant GluA2/3-AMPARs. The de novo GluA1-containing AMPARs were localized to extrasynaptic sites and later internalized by sAPPα-driven expression of the activity-regulated cytoskeletal-associated protein, Arc. Interestingly, longer exposure to sAPPα increased synaptic levels of GluA1/2 AMPARs. Moreover, the sAPPα-mediated enhancement of LTP in area CA1 of acute hippocampal slices was dependent on CP-AMPARs. Together, these findings show that sAPPα engages mechanisms which specifically enhance the synthesis and cell-surface expression of GluA1 homomers, underpinning the sAPPα-driven enhancement of synaptic plasticity in the hippocampus.

scholarly journals Neuregulin 1 regulates amyloid precursor protein cell surface expression and non-amyloidogenic processing

2018 ◽  
Vol 137 (2) ◽  
pp. 146-153 ◽  
Author(s):  
Young-Jung Kim ◽  
Ji-Young Yoo ◽  
Ok-Soon Kim ◽  
Han-byeol Kim ◽  
Junghwa Ryu ◽  
...  
Keyword(s):  
Cell Surface ◽  
Amyloid Precursor Protein ◽  
Surface Expression ◽  
Precursor Protein ◽  
Cell Surface Expression ◽  
Neuregulin 1 ◽  
Amyloidogenic Processing ◽  
Protein Cell

scholarly journals Five tumor necrosis factor-inducible cell adhesion mechanisms on the surface of mouse endothelioma cells mediate the binding of leukocytes.

1993 ◽  
Vol 121 (3) ◽  
pp. 655-664 ◽  
Author(s):  
M Hahne ◽  
U Jäger ◽  
S Isenmann ◽  
R Hallmann ◽  
D Vestweber
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Line ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Tnf Alpha ◽  
The Novel ◽  
Adhesion Mechanism ◽  
Tnf Induction ◽  
Necrosis Factor

We have distinguished five TNF-alpha-inducible cell adhesion mechanisms on microvasculature-derived endothelioma cells of the mouse which mediate the binding of different types of leukocytes. Three of these mechanisms could be identified as the mouse homologs of ICAM-1, VCAM-1, and E-selectin, of which the latter was defined by the novel mAb 21KC10. The fourth TNF-alpha-inducible cell adhesion mechanism was blocked by antibodies specific for mouse P-selectin. We have recently shown that TNF-alpha stimulates the synthesis of P-selectin in mouse endothelioma cells (A. Weller, S. Isenmann, D. Vestweber. 1992. J. Biol. Chem. 267:15176-15183). Here we show that this stimulation leads to maximal cell surface expression levels within 4 h after stimulation while the same endothelioma cells are also able to upregulate P-selectin at the cell surface within minutes after stimulation with PMA. Both effects are additive. The fifth TNF-induced cell adhesion mechanism is defined by mediating the binding to the mouse monocyte/macrophage cell line J774. This adhesion mechanism is not inhibited by antibodies against any of the other four CAMs; it functions well at 7 degrees C (in contrast to ICAM-1 and VCAM-1) and it is as active after 16 h of TNF induction as after 4 h (in contrast to E- and P-selectin). Furthermore, this new adhesion mechanism only functions on two of three endothelioma cell lines and is undetectable on the third, although ICAM-1, VCAM-1, E-selectin, and P-selectin could be demonstrated to function well on this cell line. Thus, in addition to the three known TNF-inducible CAMs, ICAM-1, VCAM-1, and E-selectin, also P-selectin and a fifth, as yet molecularly undefined cell adhesion mechanism, are TNF inducible at the cell surface of mouse endothelioma cells.

scholarly journals Evidence for a role of the amyloid precursor protein in thyroid carcinogenesis

2008 ◽  
Vol 198 (2) ◽  
pp. 291-299 ◽  
Author(s):  
Kerstin Krause ◽  
Stefan Karger ◽  
Sien-Yi Sheu ◽  
Thomas Aigner ◽  
Romy Kursawe ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Surface Expression ◽  
Precursor Protein ◽  
Cell Surface Expression ◽  
Prolonged Release ◽  
Mrna Levels ◽  
Thyroid Cells ◽  
And Function

We have recently found an increased expression of amyloid precursor protein (APP) in cold thyroid nodules that are difficult to classify as a truly benign thyroid neoplasm or a lesion with the potential for further dedifferentiation. Since differences in APP activity have been found in other human cancers, we asked whether thyroid carcinogenesis might be associated with an altered APP expression and function. APP regulation was studied in vitro in differentiated (FRTL-5) and dedifferentiated follicular thyroid carcinomas (FTC-133) thyroid cells after specific inhibition or activation of the cAMP-PKA, the PI3K/AKT or the protein kinase c (PKC) cascades. In vivo analysis of APP expression and downstream signalling was performed in benign and malignant thyroid tissues. We found that upregulation of APP expression and sAPP secretion is induced by TSH in differentiated thyroid cells and by insulin in thyroid cancer cells. PKC is a strong activator of APP cleavage and in FTC-133 confers prolonged release of the APP ectodomain. FTC-133 but not FRTL-5 cells show a prominent cell surface expression of the APP ectodomain, which has been suggested to function as an autocrine growth factor. Thyroid cancers are characterized by APP upregulation, increased membrane targeting of the APP ectodomain and significantly increased mRNA levels of the APP scaffold proteins JIP1, ShcA and Fe65.

scholarly journals Cell Surface Expression of the Vaccinia Virus Complement Control Protein Is Mediated by Interaction with the Viral A56 Protein and Protects Infected Cells from Complement Attack

2008 ◽  
Vol 82 (9) ◽  
pp. 4205-4214 ◽  
Author(s):  
Natasha M. Girgis ◽  
Brian C. DeHaven ◽  
Xin Fan ◽  
Kendra M. Viner ◽  
Mohammad Shamim ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Vaccinia Virus ◽  
Transmembrane Domain ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Major Protein ◽  
Complement Control Protein ◽  
Infected Cells ◽  
Control Protein

ABSTRACT The vaccinia virus (VACV) complement control protein (VCP) is the major protein secreted from VACV-infected cells. It has been reported that VCP binds to the surfaces of uninfected cells by interacting with heparan sulfate proteoglycans (HSPGs). In this study, we show that VCP is also expressed on the surfaces of infected cells and demonstrate that surface localization occurs independently of HSPGs. Since VCP does not contain a transmembrane domain, we hypothesized that VCP interacts with a membrane protein that localizes to the infected-cell surface. We show that the VACV A56 membrane protein is necessary for the cell surface expression of VCP and demonstrate that VCP and A56 interact in VACV-infected cells. Since the surface expression of VCP was abrogated by reducing agents, we examined the contribution of an unpaired cysteine residue on VCP to VCP surface expression and VCP's interaction with A56. To do this, we mutated the unpaired cysteine in VCP and generated a recombinant virus expressing the altered form of VCP. Following the infection of cells with the mutant virus, VCP was neither expressed on the cell surface nor able to interact with A56. Importantly, the cell surface expression of VCP was found to protect infected cells from complement-mediated lysis. Our findings suggest a new function for VCP that may be important for poxvirus pathogenesis and impact immune responses to VACV-based vaccines.

Sign in / Sign up

Export Citation Format

Share Document