---
title: "Mass spectrometry imaging identifies lipid signatures associated with Cyp27b1 loss in MMTV‑PyMT br"
id: "biorxiv-0-mass-spectrometry-imaging-shows-specific-lipids-signals-linked-to-cyp27b1"
canonical_url: "https://medichelpline.com/clinical-feed/biorxiv-0-mass-spectrometry-imaging-shows-specific-lipids-signals-linked-to-cyp27b1"
content_type: "clinical_feed_article"
specialty: "Oncology"
source_name: "bioRxiv (Biomedical Preprints)"
source_url: "https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1?rss=1"
published_at: "2026-08-11T12:00:00.000Z"
evidence_level: "Verified Feed"
license: "CC-BY-NC-4.0 / Informational Use"
---
# Mass spectrometry imaging identifies lipid signatures associated with Cyp27b1 loss in MMTV‑PyMT br
## Provenance & Clinical Metadata
- **Canonical URL:** https://medichelpline.com/clinical-feed/biorxiv-0-mass-spectrometry-imaging-shows-specific-lipids-signals-linked-to-cyp27b1
- **Specialty:** [Oncology](https://medichelpline.com/clinical-feed/oncology.md)
- **Primary Source:** bioRxiv (Biomedical Preprints)
- **Source URL:** [Original Journal Publication](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1?rss=1)
- **Published At:** 2026-08-11T12:00:00.000Z
- **Evidence Rating:** Verified Feed
## Executive GIST (TL;DR)
- The study used **mass spectrometry imaging** to compare intratumoral lipid composition in the MMTV‑PyMT mouse model of breast cancer with and without epithelial-specific ablation of **Cyp27b1**. - Cyp27b1 encodes the enzyme 1‑α‑hydroxylase that produces bioactive **1,25(OH)2D** from circulating 25(OH)D; tumor-produced 1,25(OH)2D is implicated in mammary tumor progression. - The MMTV‑PyMT model recapitulates four stages of human breast cancer progression: hyperplasia, adenoma/mammary intraepithelial neoplasia (MIN), early carcinoma and late carcinoma; the authors compared lipid signals across these stages. - In non‑ablated (control) animals, specific lipid signals changed with tumor stage and several lipid signals were significantly upregulated across progression stages. - In mice with mammary epithelial Cyp27b1 ablation, lipid signal patterns differed: hyperplastic lesions in ablated mice showed distinct lipid signals compared with controls. - Several lipid signals detected in non‑ablated tumors were absent in hyperplasia from ablated animals, indicating loss of Cyp27b1 alters early lipid changes observed prior to hyperplasia. - The authors interpret these results to suggest that locally produced **1,25(OH)2D** in the mammary epithelium is mechanistically related to early alterations in tumor lipid composition that precede hyperplasia. - Prior work by the group showed Cyp27b1 ablation in mammary epithelium enhanced spontaneous tumor initiation and progression in this model; the current lipid imaging data add molecular context to those phenotypic findings. - This report is a preprint and has not been peer reviewed; supplementary material and full dataset are referenced in the original source for further details.
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Pryce, Ami Grunbaum, Pierre Chaurand, Richard Kremer doi: https://doi.org/10.64898/2026.08.10.743249 This article is a preprint and has not been certified by peer review [[what does this mean?](https://www.biorxiv.org/about/FAQ#unrefereed)]. Mengdi Xing 1 McGill University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Mengdi%2BXing%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Xing%20M&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AMengdi%2BXing%2B) Ethan Yang 2 University of Montreal * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Ethan%2BYang%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Yang%20E&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AEthan%2BYang%2B) Jiarong Li 1 McGill University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Jiarong%2BLi%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Li%20J&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AJiarong%2BLi%2B) Frederic Fournelle 2 University of Montreal * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Frederic%2BFournelle%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Fournelle%20F&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AFrederic%2BFournelle%2B) Rachel S. Pryce 2 University of Montreal * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Rachel%2BS.%2BPryce%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Pryce%20RS&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ARachel%2BS.%2BPryce%2B) Ami Grunbaum 1 McGill University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Ami%2BGrunbaum%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Grunbaum%20A&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3AAmi%2BGrunbaum%2B) Pierre Chaurand 2 University of Montreal * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Pierre%2BChaurand%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Chaurand%20P&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3APierre%2BChaurand%2B) Richard Kremer 1 McGill University; * [Find this author on Google Scholar](https://www.biorxiv.org/lookup/google-scholar?link_type=googlescholar&gs_type=author&author%5B0%5D=Richard%2BKremer%2B "Open in new tab") * [Find this author on PubMed](https://www.biorxiv.org/lookup/external-ref?access_num=Kremer%20R&link_type=AUTHORSEARCH "Open in new tab") * [Search for this author on this site](https://www.biorxiv.org/search/author1%3ARichard%2BKremer%2B) * For correspondence: richard.kremer@mcgill.ca * [Abstract](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_art/node:5696480/1) * [Info/History](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1.article-info)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_info/node:5696480/1) * [Metrics](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1.article-metrics)[](https://www.biorxiv.org/panels_ajax_tab/article_tab_metrics/node:5696480/1) * [Supplementary material](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1.supplementary-material)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_data/node:5696480/1) * [ Preview PDF](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1.full.pdf+html)[](https://www.biorxiv.org/panels_ajax_tab/biorxiv_tab_pdf/node:5696480/1) ![Loading](https://www.biorxiv.org/sites/all/modules/contrib/panels_ajax_tab/images/loading.gif) ## Abstract Bioactive vitamin D (1,25-dihydoxyvitamin D or 1,25(OH)2D) is synthesized from its inert circulating form 25-hydroxyvitamin D (25(OH)D) by the enzyme 1-α-hydroxylase in the kidneys and in other tissues including breast. Because breast cancer is associated with changes in intra-tumoral lipid composition and vitamin D is known to affect lipid metabolism, we investigated the potential role of tumor-produced 1,25(OH)2D on lipid profile expression during breast tumor progression. For that purpose, we used the MMTV-PyMT mouse model which mimics the four phases of tumor progression seen in human breast cancer (hyperplasia, adenoma/mammary intraepithelial neoplasia (MIN), early carcinoma and late carcinoma). In previous studies we showed that conditional ablation of the gene encoding 1-α-hydroxylase (Cyp27b1), specifically in the mammary epithelium of this MMTV-PyMT mouse model, resulted in enhanced spontaneous tumor initiation and progression. In the present study, we used mass spectrometry imaging to compare lipid composition in the mammary glands of Cyp27b1 ablated and non-ablated MMTV-PyMT mice. In non-ablated control animals, we observed changes to specific lipid signals linked to stages of tumor progression. In particular, several discriminatory lipid signals were significantly up regulated throughout tumor progression. In ablated mice, absence of Cyp27b1 in the mammary epithelium was accompanied by different lipid signals in hyperplastic lesions. Several lipid signals were exclusively detected in non-ablated tumors but absent in hyperplasia. Our findings suggest that the tumor-produced 1,25(OH)2D known to play a key role in mammary tumor progression is mechanistically related to early changes in lipid composition seen prior to the development of hyperplasia. ### Competing Interest Statement The authors have declared no competing interest. ## Funder Information Declared Canadian Institutes of Health Research, MOP 10839 Natural Sciences and Engineering Research Council of Canada, RGPIN/03125-2021 Copyright The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a [CC-BY-NC-ND 4.0 International license](http://creativecommons.org/licenses/by-nc-nd/4.0/). bioRxiv and medRxiv thank the following for their generous financial support: > The Chan Zuckerberg Initiative, Cold Spring Harbor Laboratory, the Sergey Brin Family Foundation, California Institute of Technology, Centre National de la Recherche Scientifique, Fred Hutchinson Cancer Center, Imperial College London, Massachusetts Institute of Technology, Stanford University, The University of Edinburgh, University of Washington, and Vrije Universiteit Amsterdam. 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[ Download PDF](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1.full.pdf) Print/Save Options [Download PDF](https://www.biorxiv.org/content/biorxiv/early/2026/08/11/2026.08.10.743249.full.pdf)Full Text & In-line FiguresXML [More Info](https://www.biorxiv.org/about/FAQ#PrintOptions "More Information on Print/Save Options") [Supplementary Material ](https://www.biorxiv.org/content/10.64898/2026.08.10.743249v1.supplementary-material) [ Email](https://www.biorxiv.org/ "Email this Article") [ Share](https://www.biorxiv.org/) Mass spectrometry imaging shows specific lipids signals linked to Cyp27b1 ablation in the MMTV PyMT breast cancer model Mengdi Xing, Ethan Yang, Jiarong Li, Frederic Fournelle, Rachel S. Pryce, Ami Grunbaum, Pierre Chaurand, Richard Kremer bioRxiv 2026.08.10.743249; doi: https://doi.org/10.64898/2026.08.10.743249 This article is a preprint and has not been certified by peer review [[what does this mean?](https://www.biorxiv.org/about/FAQ#unrefereed)]. 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