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PandeyLab @Unibern, SWITZERLAND

@pandeylab.bsky.social

Laboratory of Pediatric Endocrinology at University of Bern, Bern, Switzerland. PI: Amit V Pandey. Posts are his own. Steroid metabolism, Cancer & pharmacology.

51 Posts36 Follower28 Folgt
PandeyLab @Unibern, SWITZERLAND@pandeylab.bsky.social · last mo.

🔬 How do human cells adapt when their microsomal electron transport is wiped out? In our new preprint we used CRISPR/Cas9 & prime editing to create the first complete POR-null human adrenal cell models. @snsf.ch @dbmr-unibe.bsky.social We found 👇 🔗 www.researchsquare.com/article/rs-1...

Complete POR ablation in human adrenal cells reveals steroidogenic rerouting and variant-dependent loss of cytochrome P450 support

Cytochrome P450 oxidoreductase (POR) is the obligate electron donor for microsomal cytochrome P450 enzymes. Recessive mutations in the POR gene cause POR deficiency (PORD), a severe metabolic disorder...

researchsquare.com

PandeyLab @Unibern, SWITZERLAND@pandeylab.bsky.social · last yr.

Latest paper in @springernature.com by Jibira Yakubu @pandeylab.bsky.social shows curcumin + piperine nanoparticles (CPN) inhibit steroid production in prostate cancer cells! #ProstateCancer #Nanomedicine #Curcumin Read: doi.org/10.1038/s415... @unibe.ch Funded by Cancer Research Switzerland

Nanoparticles with curcumin and piperine modulate steroid biosynthesis in prostate cancer - Scientific Reports

Scientific Reports - Nanoparticles with curcumin and piperine modulate steroid biosynthesis in prostate cancer

doi.org

PandeyLab @Unibern, SWITZERLAND@pandeylab.bsky.social · last yr.

New preprintalert! 🚨 We analyzed human growth hormone variants & found key residues for receptor binding & how mutations can cause growth disorders. 🧬🔬 #GrowthHormone #Research [https://doi.org/10.1101/2025.03.19.644177](doi.org/10.1101/2025...) #Science #MedTwitter #Endocrinology

Structural and Evolutionary Analysis of Human Growth Hormone Variants

Human growth hormone (GH) exerts its pleiotropic effects by binding to its receptor (GHR), leading to receptor dimerization and activation. We combined structural, evolutionary, and genetic analyses to elucidate the critical determinants of GH-GHR interaction and the impact of disease-causing mutations. Protein contact analysis revealed the specific amino acid residues involved in two distinct binding interfaces between GH and two chains of GHR. ConSurf analysis demonstrated significant sequence conservation in the receptor-binding regions of GH across species, highlighting their functional importance. A comprehensive list of known disease-causing mutations in GH was compiled and mapped to these binding interfaces and conserved regions. Computational site-directed mutagenesis (SDM) analysis predicted the impact of several mutations on protein stability, revealing both stabilizing and destabilizing effects. Sequence comparisons with orthologs from various species further supported the evolutionary conservation of key functional residues. Integrated analysis of contact residues between GH and GHR showed a strong correlation between receptor-binding residues, evolutionary conservation, and the occurrence of disease-associated mutations. These findings underscore the critical role of specific GH residues in mediating high-affinity interaction with its receptor, and how mutations in these conserved contact points can disrupt binding affinity and/or protein stability, ultimately leading to growth disorders. This multi-faceted approach provides valuable insights into the molecular mechanisms underlying growth hormone deficiency and related syndromes. ### Competing Interest Statement The authors have declared no competing interest.

doi.org

bioRxiv Pharmacology and Toxicology@biorxiv-pharma.bsky.social · last yr.

Structural and Evolutionary Analysis of Human Growth Hormone Variants https://www.biorxiv.org/content/10.1101/2025.03.19.644177v1

PandeyLab @Unibern, SWITZERLAND@pandeylab.bsky.social · last yr.

New preprint alert! 🚨 @pandeylab.bsky.social analyzed human growth hormone variants & found how mutations can cause growth disorders. @unibe.ch #ESKAS 🧬🔬 #GrowthHormone #Research [https://doi.org/10.1101/2025.03.19.644177](doi.org/10.1101/2025...) #Science #MedTwitter #Endocrinology

Structural and Evolutionary Analysis of Human Growth Hormone Variants

Human growth hormone (GH) exerts its pleiotropic effects by binding to its receptor (GHR), leading to receptor dimerization and activation. We combined structural, evolutionary, and genetic analyses t...

doi.org

bioRxivpreprint@biorxivpreprint.bsky.social · last yr.

Structural and Evolutionary Analysis of Human Growth Hormone Variants https://www.biorxiv.org/content/10.1101/2025.03.19.644177v1