Rarastoeti Pratiwi
Department of Tropical Biology, Faculty of Biology, Universitas Gadjah Mada, Yogyakarta, Indonesia

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Non-contact electro capacitive cancer therapy (ECCT) modulate the mRNA expression of p53, Apaf-1, survivin, NF-κB, TSP-1 and bFGF in DMBA-induced breast cancer rat Nurul Hidayah; Agung Putra; Firman Alamsyah; Rarastoeti Pratiwi
Indonesian Journal of Biomedicine and Clinical Sciences Vol 58 No 1 (2026)
Publisher : Published by Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/inajbcs.v58i1.24954

Abstract

Breast cancer is the most common cancer that causes death in women in the world. Cancer development is facilitated by the inhibition of apoptosis and induction of angiogenesis. Current cancer therapy still encounters problems in the form of recurrence, resistance, and side effects of drugs. Non-contact static electric field therapy, electro capacity cancer therapy (ECCT) with medium frequency, is a therapy developed to inhibit the proliferation of tumor cells. This study aimed to determine the mRNA expression of p53, Apaf-1, survivin related to apoptosis and NF-κB, bFGF and TSP-1 related to angiogenesis in rat breast tumor tissue after ECCT frequency of 150 kHz. Breast tissue samples and rat breast tumor nodules stored in RNA later at -20°C were used. The tissue was obtained from the non-induction non-therapy (NINT) group, induction non-therapy (INT), non-induction therapy (NIT), and induction therapy (IT). mRNA expression of p53, Apaf-1, NF-κB, bFGF and TSP-1 were analyzed using qRT-PCR and calculated with the Livak formula. Data were analyzed using one-way Anova and post-hoc LSD. The results showed that, mRNA expression of p53, Apaf-1 and TSP-1 in the IT group increased significantly, and mRNA expression of survivin and bFGF decreased significantly compared to the INT group. However, the expression of NF-κB mRNA in the IT group remained the same as in the INT group. In conclusion, ECCT with a frequency of 150 kHz upregulates p53, Apaf-1 and TSP-1 mRNA expression and downregulates survivin and bFGF mRNA expression but have no effect on NF-κB mRNA expression in rat breast tumor tissue.
Identification and structural characterization of F8 gene variants in Indonesian patients with nonsevere hemophilia A: Evidence from targeted next generation sequencing and in silico analyses Niken SN. Handayani; Suprianto Suprianto; Ni GAGC. Kirana; Indra Lesmana; Usi Sukorini; Nastiti Wijayanti; Rarastoeti Pratiwi
Narra X Vol. 4 No. 3 (2026): December 2026 (In Press)
Publisher : Narra Sains Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.52225/narrax.v4i3.297

Abstract

Hemophilia A is a rare genetic disorder caused by deficiency of coagulation factor VIII resulting from pathogenic variants in the F8 gene. The aim of this study was to identify potential pathogenic variants using targeted next generation sequencing (NGS), followed by in silico structural and pathogenicity analyses. Genomic DNA extracted from saliva samples of 11 patients with nonsevere hemophilia A was analyzed using targeted sequencing of F8 exons 23–26, while targeted NGS was performed on two selected patients for broader variant detection. Identified variants were further evaluated using computational pathogenicity prediction and three-dimensional protein structural modeling. No variants were detected within exons 23–26. Nevertheless, targeted NGS identified a missense variant, c.2095A>G (p.Met699Val), in exon 13 in patient HM1 and a splice-site variant, c.1271+1G>A, in intron 8 in patient HM7. Variant assessment predicted that the variants were classified as likely pathogenic and pathogenic, respectively. Structural comparison between wild-type and mutant factor VIII proteins showed no major differences in overall conformation, secondary structure, or ProMotif features. Nonetheless, physicochemical and atomic interaction analyses indicated local structural perturbations that may affect protein stability and function. These findings suggest that the identified F8 variants, particularly p.Met699Val, may contribute to factor VIII dysfunction despite preservation of the global protein structure. However, further validation using molecular dynamics simulations and functional experimental studies is required to clarify its structural impact and confirm pathogenicity.