1
40
3
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.18632/oncotarget.7323" target="_blank" rel="noreferrer noopener">http://doi.org/10.18632/oncotarget.7323</a>
Pages
13932–13944
Issue
12
Volume
7
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Osteoactivin (GPNMB) ectodomain protein promotes growth and invasive behavior of human lung cancer cells.
Publisher
An entity responsible for making the resource available
Oncotarget
Date
A point or period of time associated with an event in the lifecycle of the resource
2016
2016-03
Subject
The topic of the resource
Female; Humans; Animals; Mice; Apoptosis; GPNMB; *Cell Movement; Neoplasm Invasiveness; Membrane Glycoproteins/*metabolism; Biomarkers; *Cell Proliferation; cell adhesion; Cell Adhesion; integrin; lung cancer; Lung Neoplasms/metabolism/*pathology; NSCLC; Protein Domains; Xenograft Model Antitumor Assays; Carcinoma; Cultured; Tumor Cells; Nude; Non-Small-Cell Lung/metabolism/*pathology; Tumor/*metabolism
Creator
An entity primarily responsible for making the resource
Oyewumi Moses O; Manickavasagam Dharani; Novak Kimberly; Wehrung Daniel; Paulic Nikola; Moussa Fouad M; Sondag Gregory R; Safadi Fayez F
Description
An account of the resource
The potential application of GPNMB/OA as a therapeutic target for lung cancer will require a greater understanding of the impact of GPNMB/OA ectodomain (ECD) protein shedding into tumor tissues. Thus, in this work we characterized GPNMB/OA expression and extent of shedding of its ECD protein while evaluating the impact on lung cancer progression using three non-small cell lung cancer (NSCLC) cell lines: A549, SK-MES-1 and calu-6. We observed a direct correlation (R2 = 0.89) between GPNMB/OA expression on NSCLC cells and the extent of GPNMB/OA ECD protein shedding. Meanwhile, siRNA-mediated knockdown of GPNMB/OA in cancer cells significantly reduced GPNMB/OA ECD protein shedding, migration, invasion and adhesion to extracellular matrix materials. Also, exogenous treatment of cancer cells (expressing low GPNMB/OA) with recombinant GPNMB/OA protein (rOA) significantly facilitated cell invasion and migration, but the effects of rOA was negated by inclusion of a selective RGD peptide. Further studies in athymic (nu/nu) mice-bearing calu-6 showed that intratumoral supplementation with rOA effectively facilitated in vivo tumor growth as characterized by a high number of proliferating cells (Ki67 staining) coupled with a low number of apoptotic cells. Taken together, our results accentuate the relevance of GPNMB/OA ECD protein shedding to progression of lung cancer. Thus, strategies that suppress GPNMB/OA expression on lung cancer cells as well as negate shedding of GPNMB/OA ECD protein are worthy of consideration in lung cancer therapeutics.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.18632/oncotarget.7323" target="_blank" rel="noreferrer noopener">10.18632/oncotarget.7323</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Cell Movement
*Cell Proliferation
2016
Animals
Apoptosis
Biomarkers
Carcinoma
Cell Adhesion
Cultured
Department of Anatomy & Neurobiology
Department of Pharmaceutical Sciences
Female
GPNMB
Humans
integrin
Lung cancer
Lung Neoplasms/metabolism/*pathology
Manickavasagam Dharani
Membrane Glycoproteins/*metabolism
Mice
Moussa Fouad M
NEOMED College of Medicine
NEOMED College of Pharmacy
Neoplasm Invasiveness
Non-Small-Cell Lung/metabolism/*pathology
Novak Kimberly
NSCLC
Nude
Oncotarget
Oyewumi Moses O
Paulic Nikola
Protein Domains
Safadi Fayez F
Sondag Gregory R
Tumor Cells
Tumor/*metabolism
Wehrung Daniel
Xenograft Model Antitumor Assays
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1038/emm.2016.78" target="_blank" rel="noreferrer noopener">http://doi.org/10.1038/emm.2016.78</a>
Pages
e257–e257
Issue
9
Volume
48
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Osteoactivin inhibition of osteoclastogenesis is mediated through CD44-ERK signaling.
Publisher
An entity responsible for making the resource available
Experimental & molecular medicine
Date
A point or period of time associated with an event in the lifecycle of the resource
2016
2016-09
Subject
The topic of the resource
*MAP Kinase Signaling System; *Signal Transduction; Animals; Cell Differentiation; Cells; Cultured; Eye Proteins/*metabolism; Hyaluronan Receptors/*metabolism; Inbred C57BL; Male; Membrane Glycoproteins/*metabolism; Mice; Osteoclasts/*cytology/metabolism; RANK Ligand/metabolism; Recombinant Proteins/metabolism
Creator
An entity primarily responsible for making the resource
Sondag Gregory R; Mbimba Thomas S; Moussa Fouad M; Novak Kimberly; Yu Bing; Jaber Fatima A; Abdelmagid Samir M; Geldenhuys Werner J; Safadi Fayez F
Description
An account of the resource
Osteoactivin is a heavily glycosylated protein shown to have a role in bone remodeling. Previous studies from our lab have shown that mutation in Osteoactivin enhances osteoclast differentiation but inhibits their function. To date, a classical receptor and a signaling pathway for Osteoactivin-mediated osteoclast inhibition has not yet been characterized. In this study, we examined the role of Osteoactivin treatment on osteoclastogenesis using bone marrow-derived osteoclast progenitor cells and identify a signaling pathway relating to Osteoactivin function. We reveal that recombinant Osteoactivin treatment inhibited osteoclast differentiation in a dose-dependent manner shown by qPCR, TRAP staining, activity and count. Using several approaches, we show that Osteoactivin binds CD44 in osteoclasts. Furthermore, recombinant Osteoactivin treatment inhibited ERK phosphorylation in a CD44-dependent manner. Finally, we examined the role of Osteoactivin on receptor activator of nuclear factor-kappa B ligand (RANKL)-induced osteolysis in vivo. Our data indicate that recombinant Osteoactivin inhibits RANKL-induced osteolysis in vivo and this effect is CD44-dependent. Overall, our data indicate that Osteoactivin is a negative regulator of osteoclastogenesis in vitro and in vivo and that this process is regulated through CD44 and ERK activation.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1038/emm.2016.78" target="_blank" rel="noreferrer noopener">10.1038/emm.2016.78</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*MAP Kinase Signaling System
*Signal Transduction
2016
Abdelmagid Samir M
Animals
Cell Differentiation
Cells
Cultured
Department of Anatomy & Neurobiology
Experimental & molecular medicine
Eye Proteins/*metabolism
Geldenhuys Werner J
Hyaluronan Receptors/*metabolism
Inbred C57BL
Jaber Fatima A
Male
Mbimba Thomas S
Membrane Glycoproteins/*metabolism
Mice
Moussa Fouad M
NEOMED College of Medicine
Novak Kimberly
Osteoclasts/*cytology/metabolism
RANK Ligand/metabolism
Recombinant Proteins/metabolism
Safadi Fayez F
Sondag Gregory R
Yu Bing
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1002/(SICI)1098-2396(199809)30:1%3C9::AID-SYN2%3E3.0.CO;2-7" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/(SICI)1098-2396(199809)30:1%3C9::AID-SYN2%3E3.0.CO;2-7</a>
Pages
9–17
Issue
1
Volume
30
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Multiple binding sites for [125I]RTI-121 and other cocaine analogs in rat frontal cerebral cortex.
Publisher
An entity responsible for making the resource available
Synapse (New York, N.Y.)
Date
A point or period of time associated with an event in the lifecycle of the resource
1998
1998-09
Subject
The topic of the resource
*Membrane Transport Proteins; *Nerve Tissue Proteins; *Symporters; Animals; Binding; Binding Sites; Carrier Proteins/*metabolism; Cocaine/*analogs & derivatives/pharmacokinetics; Competitive; Corpus Striatum/*metabolism; Dopamine Plasma Membrane Transport Proteins; Dopamine/metabolism; Frontal Lobe/*metabolism; Iodine Radioisotopes/*pharmacokinetics; Kinetics; Male; Membrane Glycoproteins/*metabolism; Norepinephrine Plasma Membrane Transport Proteins; Norepinephrine/metabolism; Rats; Regression Analysis; Serotonin Plasma Membrane Transport Proteins; Serotonin/metabolism; Sprague-Dawley
Creator
An entity primarily responsible for making the resource
Boja J W; Carroll F I; Vaughan R A; Kopajtic T; Kuhar M J
Description
An account of the resource
In an effort to identify novel binding sites for cocaine and its analogs, we carried out binding studies with the high-affinity and selective ligand [125I]RTI-121 in rat frontal cortical tissue. Very low densities of binding sites were found. Saturation analysis revealed that the binding was to both high- and low-affinity sites. Pharmacological competition studies were carried out with inhibitors of the dopamine, norepinephrine, and serotonin transporters. The various transporter inhibitors inhibited the binding of 15 pM [125I]RTI-121 in a biphasic fashion following a two-site binding model. The resultant data were complex and did not suggest a simple association with any single transporter. Correlational analysis supported the following hypothesis: [125I] RTI-121 binds to known transporters and not to novel sites; these include dopamine, norepinephrine, and serotonin transporters. Immunoprecipitation of transporters photoaffinity labeled with [125]RTI-82 and subsequent analysis of SDS-page gels revealed the presence of authentic dopamine transporters in these samples; displacement of the photoaffinity label occurred with a typical dopamine transporter pharmacology. These data are compatible with the binding properties of RTI-121 and the presence of several known transporters in the tissue studied.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1002/(SICI)1098-2396(199809)30:1%3C9::AID-SYN2%3E3.0.CO;2-7" target="_blank" rel="noreferrer noopener">10.1002/(SICI)1098-2396(199809)30:1%3C9::AID-SYN2%3E3.0.CO;2-7</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Membrane Transport Proteins
*Nerve Tissue Proteins
*Symporters
1998
Animals
Binding
Binding Sites
Boja J W
Carrier Proteins/*metabolism
Carroll F I
Cocaine/*analogs & derivatives/pharmacokinetics
Competitive
Corpus Striatum/*metabolism
Dopamine Plasma Membrane Transport Proteins
Dopamine/metabolism
Frontal Lobe/*metabolism
Iodine Radioisotopes/*pharmacokinetics
Kinetics
Kopajtic T
Kuhar M J
Male
Membrane Glycoproteins/*metabolism
Norepinephrine Plasma Membrane Transport Proteins
Norepinephrine/metabolism
Rats
Regression Analysis
Serotonin Plasma Membrane Transport Proteins
Serotonin/metabolism
Sprague-Dawley
Synapse (New York, N.Y.)
Vaughan R A