publication . Article . 2018

Cosmosiin Increases ADAM10 Expression via Mechanisms Involving 5’UTR and PI3K Signaling

Zhuo Min; Ying Tang; Xiao-Tong Hu; Bing-Lin Zhu; Yuan-Lin Ma; Jing-Si Zha; Xiao-Juan Deng; Zhen Yan; Guo-Jun Chen;
Open Access English
  • Published: 01 Jun 2018 Journal: Frontiers in Molecular Neuroscience, volume 11 (issn: 1662-5099, eissn: 1662-5099, Copyright policy)
  • Publisher: Frontiers Media S.A.
Abstract
The α-secretase “a disintegrin and metalloproteinase domain-containing protein” (ADAM10) is involved in the processing of amyloid precursor protein (APP). Upregulation of ADAM10 precludes the generation of neurotoxic β-amyloid protein (Aβ) and represents a plausible therapeutic strategy for Alzheimer’s disease (AD). In this study, we explored compounds that can potentially promote the expression of ADAM10. Therefore, we performed high-throughput small-molecule screening in SH-SY5Y (human neuroblastoma) cells that stably express a luciferase reporter gene driven by the ADAM10 promoter, including a portion of its 5’-untranslated region (5’UTR). This has led to the...
Subjects
free text keywords: Neurosciences. Biological psychiatry. Neuropsychiatry, PI3K, RC321-571, Neuroscience, translation, ADAM10, Original Research, cosmosiin, 5’UTR
53 references, page 1 of 4

Bitterman P. B.Polunovsky V. A. (2012). Attacking a nexus of the oncogenic circuitry by reversing aberrant eIF4F-mediated translation. Mol. Cancer Ther. 11, 1051–1061. 10.1158/1535-7163.MCT-11-0530 22572598 [OpenAIRE] [PubMed] [DOI]

Bjornsti M. A.Houghton P. J. (2004). Lost in translation: dysregulation of cap-dependent translation and cancer. Cancer Cell 5, 519–523. 10.1016/j.ccr.2004.05.027 15193254 [PubMed] [DOI]

Chen C. S.Ho D. R.Chen F. Y.Chen C. R.Ke Y. D.Su J. G. (2014). AKT mediates actinomycin D-induced p53 expression. Oncotarget 5, 693–703. 10.18632/oncotarget.1328 24525337 [OpenAIRE] [PubMed] [DOI]

Colciaghi F.Borroni B.Pastorino L.Marcello E.Zimmermann M.Cattabeni F.. (2002). [α]-Secretase ADAM10 as well as [α]APPs is reduced in platelets and CSF of Alzheimer disease patients. Mol. Med.8, 67–74. 12080182 [OpenAIRE] [PubMed]

Corbett G. T.Gonzalez F. J.Pahan K. (2015). Activation of peroxisome proliferator-activated receptor α stimulates ADAM10-mediated proteolysis of APP. Proc. Natl. Acad. Sci. U S A 112, 8445–8450. 10.1073/pnas.1504890112 26080426 [OpenAIRE] [PubMed] [DOI]

Costa-Mattioli M.Sossin W. S.Klann E.Sonenberg N. (2009). Translational control of long-lasting synaptic plasticity and memory. Neuron 61, 10–26. 10.1016/j.neuron.2008.10.055 19146809 [OpenAIRE] [PubMed] [DOI]

Dai J.Liu Z. Q.Wang X. Q.Lin J.Yao P. F.Huang S. L.. (2015). Discovery of small molecules for up-regulating the translation of antiamyloidogenic secretase, a disintegrin and metalloproteinase 10 (ADAM10), by binding to the G-Quadruplex-Forming Sequence in the 5′ untranslated region (UTR) of its mRNA. J. Med. Chem.58, 3875–3891. 10.1021/acs.jmedchem.5b00139 25822852 [PubMed] [DOI]

De Strooper B.Vassar R.Golde T. (2010). The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat. Rev. Neurol. 6, 99–107. 10.1038/nrneurol.2009.218 20139999 [OpenAIRE] [PubMed] [DOI]

Edwards D. R.Handsley M. M.Pennington C. J. (2008). The ADAM metalloproteinases. Mol. Aspects Med. 29, 258–289. 10.1016/j.mam.2008.08.001 18762209 [OpenAIRE] [PubMed] [DOI]

Endres K.Fahrenholz F. (2010). Upregulation of the α-secretase ADAM1 0–risk or reason for hope? FEBS J. 277, 1585–1596. 10.1111/j.1742-4658.2010.07566.x 20136654 [PubMed] [DOI]

Epis R.Marcello E.Gardoni F.Vastagh C.Malinverno M.Balducci C.. (2010). Blocking ADAM10 synaptic trafficking generates a model of sporadic Alzheimer’s disease. Brain 133, 3323–3335. 10.1093/brain/awq217 20805102 [OpenAIRE] [PubMed] [DOI]

Fellgiebel A.Kojro E.Müller M. J.Scheurich A.Schmidt L. G.Fahrenholz F. (2009). CSF APPs α and phosphorylated tau protein levels in mild cognitive impairment and dementia of Alzheimer’s type. J. Geriatr. Psychiatry Neurol. 22, 3–9. 10.1177/0891988708327810 19073834 [PubMed] [DOI]

Fernandez J. W.Rezai-Zadeh K.Obregon D.Tan J. (2010). EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APP. FEBS Lett. 584, 4259–4267. 10.1016/j.febslet.2010.09.022 20849853 [OpenAIRE] [PubMed] [DOI]

Fuchs J.Milbradt R. (1993). Skin anti-inflammatory activity of apigenin-7-glucoside in rats. Arzneimittelforschung 43, 370–372. 7683883 [PubMed]

Holz M. K.Ballif B. A.Gygi S. P.Blenis J. (2005). mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123, 569–580. 10.1016/j.cell.2005.10.024 16286006 [OpenAIRE] [PubMed] [DOI]

53 references, page 1 of 4
Abstract
The α-secretase “a disintegrin and metalloproteinase domain-containing protein” (ADAM10) is involved in the processing of amyloid precursor protein (APP). Upregulation of ADAM10 precludes the generation of neurotoxic β-amyloid protein (Aβ) and represents a plausible therapeutic strategy for Alzheimer’s disease (AD). In this study, we explored compounds that can potentially promote the expression of ADAM10. Therefore, we performed high-throughput small-molecule screening in SH-SY5Y (human neuroblastoma) cells that stably express a luciferase reporter gene driven by the ADAM10 promoter, including a portion of its 5’-untranslated region (5’UTR). This has led to the...
Subjects
free text keywords: Neurosciences. Biological psychiatry. Neuropsychiatry, PI3K, RC321-571, Neuroscience, translation, ADAM10, Original Research, cosmosiin, 5’UTR
53 references, page 1 of 4

Bitterman P. B.Polunovsky V. A. (2012). Attacking a nexus of the oncogenic circuitry by reversing aberrant eIF4F-mediated translation. Mol. Cancer Ther. 11, 1051–1061. 10.1158/1535-7163.MCT-11-0530 22572598 [OpenAIRE] [PubMed] [DOI]

Bjornsti M. A.Houghton P. J. (2004). Lost in translation: dysregulation of cap-dependent translation and cancer. Cancer Cell 5, 519–523. 10.1016/j.ccr.2004.05.027 15193254 [PubMed] [DOI]

Chen C. S.Ho D. R.Chen F. Y.Chen C. R.Ke Y. D.Su J. G. (2014). AKT mediates actinomycin D-induced p53 expression. Oncotarget 5, 693–703. 10.18632/oncotarget.1328 24525337 [OpenAIRE] [PubMed] [DOI]

Colciaghi F.Borroni B.Pastorino L.Marcello E.Zimmermann M.Cattabeni F.. (2002). [α]-Secretase ADAM10 as well as [α]APPs is reduced in platelets and CSF of Alzheimer disease patients. Mol. Med.8, 67–74. 12080182 [OpenAIRE] [PubMed]

Corbett G. T.Gonzalez F. J.Pahan K. (2015). Activation of peroxisome proliferator-activated receptor α stimulates ADAM10-mediated proteolysis of APP. Proc. Natl. Acad. Sci. U S A 112, 8445–8450. 10.1073/pnas.1504890112 26080426 [OpenAIRE] [PubMed] [DOI]

Costa-Mattioli M.Sossin W. S.Klann E.Sonenberg N. (2009). Translational control of long-lasting synaptic plasticity and memory. Neuron 61, 10–26. 10.1016/j.neuron.2008.10.055 19146809 [OpenAIRE] [PubMed] [DOI]

Dai J.Liu Z. Q.Wang X. Q.Lin J.Yao P. F.Huang S. L.. (2015). Discovery of small molecules for up-regulating the translation of antiamyloidogenic secretase, a disintegrin and metalloproteinase 10 (ADAM10), by binding to the G-Quadruplex-Forming Sequence in the 5′ untranslated region (UTR) of its mRNA. J. Med. Chem.58, 3875–3891. 10.1021/acs.jmedchem.5b00139 25822852 [PubMed] [DOI]

De Strooper B.Vassar R.Golde T. (2010). The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat. Rev. Neurol. 6, 99–107. 10.1038/nrneurol.2009.218 20139999 [OpenAIRE] [PubMed] [DOI]

Edwards D. R.Handsley M. M.Pennington C. J. (2008). The ADAM metalloproteinases. Mol. Aspects Med. 29, 258–289. 10.1016/j.mam.2008.08.001 18762209 [OpenAIRE] [PubMed] [DOI]

Endres K.Fahrenholz F. (2010). Upregulation of the α-secretase ADAM1 0–risk or reason for hope? FEBS J. 277, 1585–1596. 10.1111/j.1742-4658.2010.07566.x 20136654 [PubMed] [DOI]

Epis R.Marcello E.Gardoni F.Vastagh C.Malinverno M.Balducci C.. (2010). Blocking ADAM10 synaptic trafficking generates a model of sporadic Alzheimer’s disease. Brain 133, 3323–3335. 10.1093/brain/awq217 20805102 [OpenAIRE] [PubMed] [DOI]

Fellgiebel A.Kojro E.Müller M. J.Scheurich A.Schmidt L. G.Fahrenholz F. (2009). CSF APPs α and phosphorylated tau protein levels in mild cognitive impairment and dementia of Alzheimer’s type. J. Geriatr. Psychiatry Neurol. 22, 3–9. 10.1177/0891988708327810 19073834 [PubMed] [DOI]

Fernandez J. W.Rezai-Zadeh K.Obregon D.Tan J. (2010). EGCG functions through estrogen receptor-mediated activation of ADAM10 in the promotion of non-amyloidogenic processing of APP. FEBS Lett. 584, 4259–4267. 10.1016/j.febslet.2010.09.022 20849853 [OpenAIRE] [PubMed] [DOI]

Fuchs J.Milbradt R. (1993). Skin anti-inflammatory activity of apigenin-7-glucoside in rats. Arzneimittelforschung 43, 370–372. 7683883 [PubMed]

Holz M. K.Ballif B. A.Gygi S. P.Blenis J. (2005). mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events. Cell 123, 569–580. 10.1016/j.cell.2005.10.024 16286006 [OpenAIRE] [PubMed] [DOI]

53 references, page 1 of 4
Powered by OpenAIRE Open Research Graph
Any information missing or wrong?Report an Issue
publication . Article . 2018

Cosmosiin Increases ADAM10 Expression via Mechanisms Involving 5’UTR and PI3K Signaling

Zhuo Min; Ying Tang; Xiao-Tong Hu; Bing-Lin Zhu; Yuan-Lin Ma; Jing-Si Zha; Xiao-Juan Deng; Zhen Yan; Guo-Jun Chen;