Treatment of myositis with etanercept (Enbrel®), a recombinant human soluble fusion protein of TNF-α type II receptor and IgG1

Type II pulmonary epithelial cells respond to anthracite coal dust PSOC 867 with increased synthesis of extracellular matrix (ECM) components. Alveolar macrophages modulate this response by pathways that may involve soluble mediators, including tumor necrosis factor-α (TNF-α) or transforming growth factor-β1 (TGF-β1). The effects of TNF-α (10 ng/ml) and/or TGF-β1 (2 ng/ml) were thus investigated in dust-exposed primary type II cell cultures. In control day 1 or day 3 cultures, TNF-α and/or TGF-β1 had little or no effect on the synthesis of type II cellular proteins, independent of whether the cells were exposed to dust. With PSOC 867 exposure, where ECM protein synthesis is elevated, TNF-α and TGF-β1 further increased both the absolute and relative rates of ECM synthesis on day 3 but had little effect on day 1. Each mediator increased expression of fibronectin mRNA, as well as of ECM fibronectin content, in a manner qualitatively similar to their effects on synthesis. Thus TNF-α and TGF-β1 modulate both ECM synthesis and fibronectin content in coal dust-exposed type II cell cultures.

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Methods for Increasing the Expression Level of a Soluble Fusion Protein Encoding a 62 Amino Acid Fragment of the α-Subunit of the Nicotinic Acetylcholine Receptora

Annals of the New York Academy of Sciences ◽

10.1111/j.1749-6632.1995.tb17468.x ◽

1995 ◽

Vol 757 (1) ◽

pp. 117-119

Author(s):

LISA N. GENTILE ◽

EDWARD HAWROT

Keyword(s):

Amino Acid ◽

Fusion Protein ◽

Expression Level ◽

Nicotinic Acetylcholine ◽

Α Subunit ◽

Amino Acid Fragment ◽

Acid Fragment ◽

Protein Encoding ◽

Soluble Fusion Protein

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Efficacy of joint cavity injection with recombinant human type II tumor necrosis factor receptor antibody fusion protein for rheumatoid arthritis combined with knee arthritis

Osteoarthritis and Cartilage ◽

10.1016/j.joca.2021.02.460 ◽

2021 ◽

Vol 29 ◽

pp. S355

Author(s):

Z. Yazhou ◽

C. Liu

Keyword(s):

Rheumatoid Arthritis ◽

Tumor Necrosis Factor ◽

Fusion Protein ◽

Tumor Necrosis ◽

Tumor Necrosis Factor Receptor ◽

Type Ii ◽

Knee Arthritis ◽

Joint Cavity ◽

Antibody Fusion Protein ◽

Necrosis Factor

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Effects of bone marrow-derived mesenchymal stromal cells on gene expression in human alveolar type II cells exposed to TNF-α , IL-1β , and IFN-γ

Physiological Reports ◽

10.14814/phy2.13831 ◽

2018 ◽

Vol 6 (16) ◽

pp. e13831 ◽

Cited By ~ 2

Author(s):

Matthew Schwede ◽

Erin M. Wilfong ◽

Rachel L. Zemans ◽

Patty J. Lee ◽

Claudia dos Santos ◽

...

Keyword(s):

Gene Expression ◽

Bone Marrow ◽

Mesenchymal Stromal Cells ◽

Stromal Cells ◽

Alveolar Type ◽

Type Ii Cells ◽

Type Ii ◽

Alveolar Type Ii Cells ◽

Tnf Α ◽

Ifn Γ

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TNF-α induction of IL-6 in alveolar type II epithelial cells: Contributions of JNK/c-Jun/AP-1 element, C/EBPδ/C/EBP binding site and IKK/NF-κB p65/κB site

Molecular Immunology ◽

10.1016/j.molimm.2018.05.004 ◽

2018 ◽

Vol 101 ◽

pp. 585-596 ◽

Cited By ~ 6

Author(s):

Chunguang Yan ◽

Chunmin Deng ◽

Xiufang Liu ◽

Yutong Chen ◽

Jiawei Ye ◽

...

Keyword(s):

Epithelial Cells ◽

Binding Site ◽

Alveolar Type ◽

Type Ii ◽

Tnf Α

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Aggregation kinetics in the presence of brain lipids of Aβ(1–40) cleaved from a soluble fusion protein

Biochimica et Biophysica Acta (BBA) - Biomembranes ◽

10.1016/j.bbamem.2018.03.005 ◽

2018 ◽

Vol 1860 (9) ◽

pp. 1681-1686 ◽

Cited By ~ 6

Author(s):

Miriam A. Kael ◽

Daniel K. Weber ◽

Frances Separovic ◽

Marc-Antoine Sani

Keyword(s):

Fusion Protein ◽

Aggregation Kinetics ◽

Brain Lipids ◽

Soluble Fusion Protein

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Cloning and analysis of a recombinant antigen containing an epitope specific for human T-cell lymphotropic virus type II

Blood ◽

10.1182/blood.v79.10.2789.2789 ◽

1992 ◽

Vol 79 (10) ◽

pp. 2789-2796 ◽

Cited By ~ 11

Author(s):

KG Hadlock ◽

JJ Lipka ◽

TP Chow ◽

SK Foung ◽

GR Reyes

Keyword(s):

Fusion Protein ◽

Western Blot ◽

Recombinant Proteins ◽

Recombinant Antigen ◽

Type Ii ◽

Lambda Phage ◽

Chain Reaction ◽

Specific Epitope ◽

Human T Cell ◽

Polymerase Chain

Abstract An immunodominant HTLV-I-specific epitope in the HTLV-I envelope glycoprotein (GP) 46 has been described. To determine if the analogous region of HTLV-II contains a similarly immunogenic and specific epitope, the polymerase chain reaction (PCR) was used to amplify HTLV- II DNA fragments encoding various portions of the putative epitope. The synthesized DNAs were cloned into lambda-phage gt11 and screened for production of immunoreactive fusion protein using sera from HTLV-II- or HTLV-I-infected individuals. Antisera from HTLV-II-infected individuals identified three of four recombinant clones when tested in a plaque immunoassay. Fusion protein from one of the clones, GH2-K15, was purified and analyzed by Western blot against a panel of HTLV-I and HTLV-II antisera. Twenty-one of 22 HTLV-II-infected sera were reactive with the GH2-K15 epitope. Sera from HTLV-I-infected and HTLV-I- uninfected individuals did not cross-react with GH2-K15. Western blot analysis of recombinant proteins encoding portions of the HTLV-II sequences in the Gh2-K15 antigen localized the HTLV-II-specific epitope to a 17-amino acid sequence. Recombinant antigens containing this epitope should be useful for type-specific serologic diagnosis of HTLV- II infection.

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Effect of Marine Phytoplankton (Oceanix) and Undenatured Type II Collagen in Combination with Exercise on Endurance Capacity and Oxidative Stress in Rats

Current Developments in Nutrition ◽

10.1093/cdn/nzaa066_019 ◽

2020 ◽

Vol 4 (Supplement_2) ◽

pp. 1764-1764

Author(s):

Kazim Sahin ◽

Cemal Orhan ◽

Mehmet Tuzcu ◽

Nurhan Sahin ◽

Vijaya Juturu

Keyword(s):

Antioxidant Enzymes ◽

Proinflammatory Cytokines ◽

Type Ii Collagen ◽

Marine Phytoplankton ◽

Albino Rats ◽

High Dose ◽

Endurance Capacity ◽

Type Ii ◽

Tnf Α ◽

Undenatured Type Ii Collagen

Abstract Objectives To study the effect of exercise training alone and or in combination with marine phytoplankton (Oceanix, OCX) and undenatured type II collagen (UCII) supplementation on the endurance capacity, pro-inflammatory markers, and antioxidant defense markers in rats. Methods A total of 28 male Wistar albino rats were randomly divided into four groups (n  =  7) (i) No exercise and no OCX (Control), (ii) Exercise, (iii) Exercise +OCX-I (2.55 mg d/rat) + UC-II (4 mg), iv) Exercise + OCX-2 (5.1 mg d/rat)+UC-II (4 mg). Levels of cholesterol, triglyceride, proinflammatory cytokines (IL-1β, IL-6, TNF-α, COMP, CRP), lactate and malondialdehyde (MDA) levels activities of antioxidant enzymes were determined in all the groups. Results Run to exhaustion (minutes) improved in the OCX + UC-II treated groups. Levels of cholesterol, triglyceride, proinflammatory cytokines (IL-1β, IL-6, TNF-α, COMP, CRP) decreased by OCX + UC-II supplementation. A significant decrease in lactate and malondialdehyde (MDA) levels and an increase in activities of antioxidant enzymes were observed in the combination of exercise and OCX + UC-II groups. Exercise + OCX + UC-II treated had lower TNF-α and IL-1β levels in muscle than exercise and control rats (P < 0.001). Muscle sterol regulatory element-binding protein 1c (SREBP-1c), liver X receptors (LXR), ATP citrate lyase (ACLY) and fatty acid synthase (FAS) levels in the exercise + OCX + UC-II group were lower than all groups (P < 0.05). The effectiveness of the high dose of OCX was more pronounced than the low dose of OCX. Conclusions These results suggest OCX and UC-II with exercise may enhance lipid metabolism by regulation of gene products involved in lipid and antioxidant metabolism including SREBP-1c, -γ, LXR, ACLY and FAS in rats. Funding Sources Lonza.

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