Journal: International Journal of Clinical and Experimental Pathology

Article Title: Rapid diagnosis of cisplatin-sensitive and resistant cervical squamous cell carcinomas by reverse transcription loop-mediated isothermal amplification

doi:

Figure Lengend Snippet: Primer design for the detection of hCTR1 mRNA by RT-LAMP

Article Snippet: RT- LAMP primers targeting hCTR1 mRNA were designed by Primer ExplorerV4 (Eiken Chemical Co, Tokyo, Japan) as indicated in .

Techniques: Sequencing

Journal: International Journal of Clinical and Experimental Pathology

Article Title: Rapid diagnosis of cisplatin-sensitive and resistant cervical squamous cell carcinomas by reverse transcription loop-mediated isothermal amplification

doi:

Figure Lengend Snippet: Sensitivity of LAMP reaction to detect hCTR1. A. The turbidity curve of LAMP technique using a known number of hCTR1 cell copies after 60 min amplification. B. The result of LAMP reaction after 45 min amplification measured by turbidimeter. Lane 1 to 7 was loaded with serially diluted hCTR1 cell copies from one million to one. Lane 8 was loaded as ddH2O as blank control.

Article Snippet: RT- LAMP primers targeting hCTR1 mRNA were designed by Primer ExplorerV4 (Eiken Chemical Co, Tokyo, Japan) as indicated in .

Techniques: Amplification, Control

Journal: International Journal of Clinical and Experimental Pathology

Article Title: Rapid diagnosis of cisplatin-sensitive and resistant cervical squamous cell carcinomas by reverse transcription loop-mediated isothermal amplification

doi:

Figure Lengend Snippet: Representative hCTR1 over-expressed (A) cervical squamous cell carcinoma and low-expressed carcinoma (B) cases analyzed by immunohistochemical staining and RT-LAMP. In RT-LAMP reaction, carcinoma RNA was loaded into lane 1 to 4 as duplicates, while adjacent normal tissue RNA was loaded into lane 5 to 8 as duplicates. *, P<0.05; **, P>0.05.

Article Snippet: RT- LAMP primers targeting hCTR1 mRNA were designed by Primer ExplorerV4 (Eiken Chemical Co, Tokyo, Japan) as indicated in .

Techniques: Immunohistochemical staining, Staining

Journal: Journal of Clinical Medicine

Article Title: Targeting Copper in Cancer Imaging and Therapy: A New Theragnostic Agent

doi: 10.3390/jcm12010223

Figure Lengend Snippet: Schematic representation of copper metabolism at the cellular and molecular level ( 64 Cu as copper ions). 64 Cu 2+ ions are bound to plasma proteins which carry them to the external membrane, where they are reduced to Cu 2+ by reductases before their uptake into cells. Reduced copper ions are then transported across the cell membrane by the human copper transporter 1 (hCTR1). In the cell, Cu 2+ ions are closely bound by copper chaperones (cytochrome c oxidase copper chaperone (COX17), copper chaperone for SOD1 (CCS), and antioxidant protein (ATOX1)), which deliver copper ions to the cytosol (via SOD1), mitochondria (via COX) and trans-Golgi network (via copper transporting ATPase A/B). Interestingly, glutathione (GSH) binds excess Cu 2+ to prevent oxidative damage, thus protecting the cell from copper toxicity. Analogous mechanisms are carried out by metallothionein (MT). When intracellular copper is too high, hCTR1 is internalized and destroyed and copper transporting ATPase A/B (ATP7A and ATP7B) transfer from the TGN to the plasma membrane to help in the excretion of copper from the cell (adapted and modified from Michniewicz F. et al.: Copper: An Intracellular Achilles’ Heel Allowing the Targeting of Epigenetics, Kinase Pathways, and Cell Metabolism in Cancer Therapeutics. Chem Med Chem 2021 , 16 , 2315–2329. Copyright Wiley-VCH GmbH. Reproduced with permission).

Article Snippet: A high intracellular concentration of copper is allowed by an elevated expression of hCTR1, and reduced tumor 64 Cu uptake and tumor growth inhibition caused by RNA-mediated hCTR1 knockdown have been shown, suggesting that hCTR1 is a promising novel theragnostic target.

Techniques: Clinical Proteomics, Membrane, Modification