Ralf Ketter
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Ralf Ketter has a total of 177 co-authors. Here are the top co-authors by number of shared publications:
- Steffi Urbschat
Department of Neurosurgery, Saarland University Medical Center, Building 90.5, Kirrbergerstraße 100, 66421, Homburg, Germany.
67 shared publications - Hermann Eichler
Institute of Clinical Haemostaseology and Transfusion Medicine Saarland University and Saarland University Hospital Homburg Germany
62 shared publications - Stefan Linsler
Department of Neurosurgery, Saarland University, D‑66421 Homburg, Germany
62 shared publications - Andreas Müller
Universität des Saarlandes
61 shared publications - Bin Qu
Biophysics, Center for Integrative Physiology and Molecular Medicine (CIPMM), School of Medicine, Saarland University, Homburg, Germany
61 shared publications - Carolin Wolter
Institute of Clinical Hemostaseology and Transfusion Medicine, Saarland University and University Medical Center, Homburg, Germany
61 shared publications
Latest Publications
- Open Access
Chromosome 1p and 6q Loss of Heterozygosity in Meningioma: A Comprehensive Analysis of the Two Chromatin Remodeling Complex Subunits ARID1A and ARID1B
Background/Objectives: Loss of heterozygosity (LOH) in meningioma has been known for more than two decades. It has been shown that LOH on chromosome 1p36 is an independent marker of meningioma recurrence and progression. ARID1A, a tumor suppressor gene located on chromosome 1p36.11, is part of the chromatin-regulating SWI/SNF complex whose subunits are altered in 20% of cases across all tumor entities. Methods: Using our newly developed indirect enzyme-linked immunosorbent assay (ELISA), we investigated whether tumors with or without LOH 1p differ in ARID1A expression in 61 meningiomas. To study possible links between ARID1A and ARID1B, we tested for LOH 6q in association with LOH 1p using a PCR-based microsatellite approach. ARID1B, another member of the SWI/SNF complex, is located on 6q25.3. Additionally, we compared our ELISA results with immunohistochemistry data staining of ARID1A in tissue sections known to harbor LOH 1p. Results: Our results indicate that meningiomas harboring LOH 1p have significantly lower ARID1A levels compared to tumors without LOH 1p. In free nuclear protein fractions, reductions were up to 32% (CI: 6–58.7%). Interestingly, we found that ARID1A levels were significantly lower in tumors with recurrence and/or multiple localizations. In addition, our analysis of chromosome 6q uncovered a significantly strong correlation between LOH 1p and LOH 6q (p < 0.0001). Conclusions: These results highlight the importance of ARID1A in meningioma malignization and indicate for the first time functional evidence for LOH 1p.
Open AccessChromosome 1p and 6q Loss of Heterozygosity in Meningioma: A Comprehensive Analysis of the Two Chromatin Remodeling Complex Subunits ARID1A and ARID1B
Background/Objectives: Loss of heterozygosity (LOH) in meningioma has been known for more than two decades. It has been shown that LOH on chromosome 1p36 is an independent marker of meningioma recurrence and progression. ARID1A, a tumor suppressor gene located on chromosome 1p36.11, is part of the chromatin-regulating SWI/SNF complex whose subunits are altered in 20% of cases across all tumor entities. Methods: Using our newly developed indirect enzyme-linked immunosorbent assay (ELISA), we investigated whether tumors with or without LOH 1p differ in ARID1A expression in 61 meningiomas. To study possible links between ARID1A and ARID1B, we tested for LOH 6q in association with LOH 1p using a PCR-based microsatellite approach. ARID1B, another member of the SWI/SNF complex, is located on 6q25.3. Additionally, we compared our ELISA results with immunohistochemistry data staining of ARID1A in tissue sections known to harbor LOH 1p. Results: Our results indicate that meningiomas harboring LOH 1p have significantly lower ARID1A levels compared to tumors without LOH 1p. In free nuclear protein fractions, reductions were up to 32% (CI: 6–58.7%). Interestingly, we found that ARID1A levels were significantly lower in tumors with recurrence and/or multiple localizations. In addition, our analysis of chromosome 6q uncovered a significantly strong correlation between LOH 1p and LOH 6q (p < 0.0001). Conclusions: These results highlight the importance of ARID1A in meningioma malignization and indicate for the first time functional evidence for LOH 1p.
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Movie_3 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
U87MG cells on day 3 after embedding in fibrin
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Movie_3 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
U87MG cells on day 3 after embedding in fibrin
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 4 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
U87MG, U373MG and U343MG cells were embedded in a 3-dimensional matrix of fibrin and monitored over 3 days using real-time video microscopy
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 4 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
U87MG, U373MG and U343MG cells were embedded in a 3-dimensional matrix of fibrin and monitored over 3 days using real-time video microscopy
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 2 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Effect of thrombin and CaCl2 on glioblastoma growth in suspension or embedded in 3D matrigel.
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 2 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Effect of thrombin and CaCl2 on glioblastoma growth in suspension or embedded in 3D matrigel.
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Movie_1 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
U87MG cells on day 1 after embedding in fibrin
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Movie_1 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
U87MG cells on day 1 after embedding in fibrin
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 5 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Expression of integrin β1 and integrin β3 affects invadopodia formation and growth of primary glioblastoma cells in fibrin clot and plasma clot
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 5 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Expression of integrin β1 and integrin β3 affects invadopodia formation and growth of primary glioblastoma cells in fibrin clot and plasma clot
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 6 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
FAK activation in glioblastoma cells embedded in fibrin clot
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 6 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
FAK activation in glioblastoma cells embedded in fibrin clot
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 3 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Representative MR images after 2 weeks of glioma grown in mice
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 3 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Representative MR images after 2 weeks of glioma grown in mice
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Video Legend from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Legend for supplementary videos 1-6
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Video Legend from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Legend for supplementary videos 1-6
- Open Access
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Supplementary Fig. 1 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Expression of fibrin(ogen) and its clotting product fibrin in glioma tumor tissues
- 13 May 2025
- Published by American Association for Cancer Research (AACR)
Open AccessSupplementary Fig. 1 from Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Expression of fibrin(ogen) and its clotting product fibrin in glioma tumor tissues