Publications by authors named "C Ampe"

Article Synopsis
  • The kisspeptin receptor (GPR54 or KISS1R) plays a crucial role in reproduction, metabolism, and cancer, but there are few tools available to visualize it directly in cells and tissues.
  • Researchers have developed a new acid-resistant fluorescent probe called Trp-BODIPY PLUS, which allows for the synthesis of fluorescent bioactive peptides that can easily bind to target receptors.
  • Using Trp-BODIPY PLUS, scientists created innovative kisspeptin-based probes that enabled them to successfully image and track GPR54 receptor activity in human cells and mouse pancreatic islets.
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High-content image-based cell phenotyping provides fundamental insights into a broad variety of life science disciplines. Striving for accurate conclusions and meaningful impact demands high reproducibility standards, with particular relevance for high-quality open-access data sharing and meta-analysis. However, the sources and degree of biological and technical variability, and thus the reproducibility and usefulness of meta-analysis of results from live-cell microscopy, have not been systematically investigated.

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The G protein-coupled kisspeptin receptor (GPR54 or KISS1R) is an important mediator in reproduction, metabolism and cancer biology; however, there are limited fluorescent probes or antibodies for direct imaging of these receptors in cells and intact tissues, which can help to interrogate their multiple biological roles. Herein, we describe the rational design and characterization of a new acid-resistant BODIPY-based amino acid (Trp-BODIPY PLUS), and its implementation for solid-phase synthesis of fluorescent bioactive peptides. Trp-BODIPY PLUS retains the binding capabilities of both short linear and cyclic peptides and displays notable turn-on fluorescence emission upon target binding for wash-free imaging.

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Background: Nonclustered mouse protocadherin genes (Pcdh) encode proteins with a typical single ectodomain and a cytoplasmic domain with conserved motifs completely different from those of classic cadherins. Alternative splice isoforms differ in the size of these cytoplasmic domains. In view of the compelling evidence for gene silencing of protocadherins in human tumors, we started investigations on Pcdh functions in mouse cancer models.

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