Rudiger Weseloh
Max Planck Society
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Featured researches published by Rudiger Weseloh.
Molecular Cancer | 2006
Bernhard Hemmerlein; Rudiger Weseloh; Fernanda Mello de Queiroz; Hendrik Knötgen; Araceli Sánchez; María E. Rubio; Sabine Martin; Tessa Schliephacke; Marc Jenke; Heinz-Joachim-Radzun; Walter Stühmer; Luis A. Pardo
BackgroundCertain types of potassium channels (known as Eag1, KCNH1, Kv10.1) are associated with the production of tumours in patients and in animals. We have now studied the expression pattern of the Eag1 channel in a large range of normal and tumour tissues from different collections utilising molecular biological and immunohistochemical techniques.ResultsThe use of reverse transcription real-time PCR and specifically generated monoclonal anti-Eag1 antibodies showed that expression of the channel is normally limited to specific areas of the brain and to restricted cell populations throughout the body. Tumour samples, however, showed a significant overexpression of the channel with high frequency (up to 80% depending on the tissue source) regardless of the detection method (staining with either one of the antibodies, or detection of Eag1 RNA).ConclusionInhibition of Eag1 expression in tumour cell lines reduced cell proliferation. Eag1 may therefore represent a promising target for the tailored treatment of human tumours. Furthermore, as normal cells expressing Eag1 are either protected by the blood-brain barrier or represent the terminal stage of normal differentiation, Eag1 based therapies could produce only minor side effects.
Cancer Research | 2007
David Gomez-Varela; Esther Zwick-Wallasch; Hendrik Knötgen; Araceli Sánchez; Thore Hettmann; Dmitri Ossipov; Rudiger Weseloh; Constanza Contreras-Jurado; Mike Rothe; Walter Stühmer; Luis A. Pardo
The potassium channel ether à go-go has been directly linked to cellular proliferation and transformation, although its physiologic role(s) are as of yet unknown. The specific blockade of human Eag1 (hEag1) may not only allow the dissection of the role of the channel in distinct physiologic processes, but because of the implication of hEag1 in tumor biology, it may also offer an opportunity for the treatment of cancer. However, members of the potassium channel superfamily are structurally very similar to one another, and it has been notoriously difficult to obtain specific blockers for any given channel. Here, we describe and validate the first rational design of a monoclonal antibody that selectively inhibits a potassium current in intact cells. Specifically blocking hEag1 function using this antibody inhibits tumor cell growth both in vitro and in vivo. Our data provide a proof of concept that enables the generation of functional antagonistic monoclonal antibodies against ion channels with therapeutic potential. The particular antibody described here, as well as the technique developed to make additional functional antibodies to Eag1, makes it possible to evaluate the potential of the channel as a target for cancer therapy.
The EMBO Journal | 2003
Marc Jenke; Araceli Sánchez; Francisco Monje; Walter Stühmer; Rudiger Weseloh; Luis A. Pardo
A short C‐terminal domain is required for correct tetrameric assembly in some potassium channels. Here, we show that this domain forms a coiled coil that determines not only the stability but also the selectivity of the multimerization. Synthetic peptides comprising the sequence of this domain in Eag1 and other channels are able to form highly stable tetrameric coiled coils and display selective heteromultimeric interactions. We show that loss of function caused by disruption of this domain in Herg1 can be rescued by introducing the equivalent domain from Eag1, and that this chimeric protein can form heteromultimers with Eag1 while wild‐type Erg1 cannot. Additionally, a short endoplasmic reticulum retention sequence closely preceding the coiled coil plays a crucial role for surface expression. Both domains appear to co‐operate to form fully functional channels on the cell surface and are a frequent finding in ion channels. Many pathological phenotypes may be attributed to mutations affecting one or both domains.
Archive | 1999
Synnöve Beckh; Andrea Brüggemann; Camino Fernandez-Miranda Donato Del; Luis Angel Pardo-Fernandez; Perez Araceli Sanchez; Walter Stühmer; Rudiger Weseloh
Archive | 2001
Walter Stühmer; Luis A. Pardo; Rudiger Weseloh
Archive | 2002
Luis Angel Pardo-Fernandez; Walter Stühmer; Synnöve Beckh; Andrea Brüggemann; Donato Del Camino Fernandez-Miranda; Araceli Sanchez Perez; Rudiger Weseloh
Archive | 2000
Luis Angel Pardo-Fernandez; Walter Stühmer; Synnöve Beckh; Andrea Brüggemann; Donato Del Camino Fernandez-Miranda; Araceli Sanchez Perez; Rudiger Weseloh
Archive | 2009
Luis Angel Pardo-Fernandez; Walter Stühmer; Synnöve Beckh; Andrea Brüggemann; Donato Del Camino Fernandez-Miranda; Araceli Sanchez Perez; Rudiger Weseloh
Archive | 2006
Luis Angel Pardo-Fernandez; Walter Stühmer; Synnöve Beckh; Andrea Brüggemann; Donato Del Camino Fernandez-Miranda; Araceli Sanchez Perez; Rudiger Weseloh
Archive | 2003
Luis Angel Pardo-Fernandez; Walter Stühmer; Synnöve Beckh; Andrea Brüggemann; Donato Del Camino Fernandez-Miranda; Araceli Sanchez Perez; Rudiger Weseloh