About

Moshmi Bhattacharya is an Associate Professor in the Department of Medicine at Rutgers University. Her research focuses on understanding the molecular mechanisms by which G protein-coupled receptors (GPCRs) regulate metabolic disorders, including cancer (specifically breast and liver cancer) and obesity-induced fatty liver disease. Her multidisciplinary studies utilize cell and 3-D culture models, genetically engineered mouse models, clinical biopsies, and blood samples to investigate these processes. Her key research interests include cancer biology, cytoskeleton, endocrinology, metabolism/nutrition, and signaling. She employs techniques such as biochemistry, cell biology, cell culture, imaging, and metabolomics in her work. Her lab aims to identify unique metabolic adaptations in diseased cells that can serve as promising drug targets, contributing to the development of novel therapeutic strategies for metabolic disorders.

Research topics

• Biology
• Internal medicine
• Endocrinology
• Medicine

Selected publications

• β-arrestin 1 and integrin-linked kinase interact in epidermal keratinocytes and regulate cell motility

  Tissue Barriers · 2025-02-13 · 1 citations

  articleOpen access

  Arrestins and integrin-linked kinase (ILK) are important scaffold proteins that regulate myriad cell functions in metazoans. β-arrestins, first identified as critical components in G-protein-coupled receptor (GPCR) signaling pathways, participate in inflammatory, immunomodulatory and tissue repair processes in GPCR-dependent and -independent manners. ILK is a central mediator of signaling cascades elicited by activation of integrins, regulating cell motility, proliferation, and mechanotransduction. In the epidermis, ILK is essential for maintenance of barrier function, hair follicle development, melanocyte colonization and regeneration after injury. In this tissue, β-arrestin 2 mitigates inflammatory processes and development of allergic dermatitis, which also is associated with loss of epidermal barrier function. However, the functional role of β-arrestin 1 in epidermal cells is poorly understood. We now report that β-arrestin 1 directly binds ILK, forming hitherto unidentified protein complexes in epidermal keratinocytes. In the absence of exogenous GPCR ligand stimulation, β-arrestin 1 and ILK are found throughout the cytoplasm in epidermal keratinocytes, and also co-localize to plasma membrane regions associated with cell protrusions. Inactivation of the genes that encode both β-arrestin 1 and 2 attenuates forward cell migration, whereas expression of ILK together with β-arrestin 1 restores cell motility. The cooperative effect of ILK and β-arrestin 1 in promoting directional cell migration may have important implications for epidermal regeneration and reestablishment of barrier function after injury.

  PublisherOA PDFDOI

• Kisspeptin Mitigates Hepatic De Novo Lipogenesis in Metabolic Dysfunction-Associated Steatotic Liver Disease

  Cells · 2025-08-20 · 1 citations

  articleOpen accessSenior authorCorresponding

  The peptide hormone kisspeptin, signaling via its receptor, KISS1R, decreases hepatic steatosis and protects against metabolic dysfunction-associated steatotic liver disease (MASLD). Enhanced de novo lipogenesis (DNL) contributes to MASLD. Here, we investigated whether kisspeptin treatment in obese, diabetic mice directly attenuates DNL. DNL was assessed in kisspeptin-treated mouse livers, using a mouse model of MASLD, (DIAMOND mice), employing 2H2O-enriched water, mass spectrometry analysis, and transcriptomic profiling. Gene and protein expression were evaluated in primary hepatocytes and livers. Additionally, hepatic Kiss1r expression was increased in DIAMOND mice, following which various biochemical and metabolic assessments were employed. Metabolic tracing in kisspeptin-treated steatotic livers demonstrated a decrease in the DNL of free fatty acids (FFAs), known to be associated with diabetes, steatosis, and hepatocellular carcinoma. Transcriptomic profiling of kisspeptin-treated livers identified disruption of key metabolic pathways, the most prominent being a decrease in fatty acid metabolism, and downregulation of Cidea, a key regulator of lipid droplet formation. Kisspeptin treatment of FFA-loaded primary mouse hepatocytes significantly decreased Cidea expression. Mechanistically, we found that kisspeptin administration decreased levels of transcription factor SREBP-1c, a crucial regulator of DNL, and CIDEA. Thus, enhanced KISS1R signaling limits hepatic DNL, suggesting a crucial role in restricting MASLD.

  PublisherOA PDFDOI

• Kisspeptin Alleviates Human Hepatic Fibrogenesis by Inhibiting TGFβ Signaling in Hepatic Stellate Cells

  Cells · 2024-10-04 · 4 citations

  articleOpen accessSenior authorCorresponding

  The peptide hormone kisspeptin attenuates liver steatosis, metabolic dysfunction-associated steatohepatitis (MASH), and fibrosis in mouse models by signaling via the kisspeptin 1 receptor (KISS1R). However, whether kisspeptin impacts fibrogenesis in the human liver is not known. We investigated the impact of a potent kisspeptin analog (KPA) on fibrogenesis using human precision-cut liver slices (hPCLS) from fibrotic livers from male patients, in human hepatic stellate cells (HSCs), LX-2, and in primary mouse HSCs. In hPCLS, 48 h and 72 h of KPA (3 nM, 100 nM) treatment decreased collagen secretion and lowered the expression of fibrogenic and inflammatory markers. Immunohistochemical studies revealed that KISS1R is expressed and localized to HSCs in MASH/fibrotic livers. In HSCs, KPA treatment reduced transforming growth factor b (TGFβ)-the induced expression of fibrogenic and inflammatory markers, in addition to decreasing TGFβ-induced collagen secretion, cell migration, proliferation, and colony formation. Mechanistically, KISS1R signaling downregulated TGFβ signaling by decreasing SMAD2/3 phosphorylation via the activation of protein phosphatases, PP2A, which dephosphorylates SMAD 2/3. This study revealed for the first time that kisspeptin reverses human hepatic fibrogenesis, thus identifying it as a new therapeutic target to treat hepatic fibrosis.

  PublisherOA PDFDOI

• Kisspeptin Alleviates Human Hepatic Fibrogenesis by Inhibiting TGFb Signaling in Hepatic Stellate Cells

  Preprints.org · 2024-09-14 · 1 citations

  preprintOpen accessSenior author

  The peptide hormone kisspeptin attenuates liver steatosis, metabolic dysfunction-associated stea-tohepatitis (MASH) and fibrosis in mouse models, by signaling via the kisspeptin 1 receptor (KISS1R). However, whether kisspeptin impacts fibrogenesis in the human liver is not known. We investigated the impact of a potent kisspeptin analog (KPA) on fibrogenesis using human precision cut liver slices (hPCLS) from fibrotic livers from male patients, in human hepatic stellate cells (HSCs), LX-2 and in primary mouse HSCs. In hPCLS, 48 h and 72 h of KPA (3 nM, 100 nM) treatment decreased collagen secretion, and lowered expression of fibrogenic and inflammatory markers. Immunohistochemical studies revealed that KISS1R is expressed and localized to HSCs in MASH/fibrotic livers. In HSCs, KPA treatment reduced transforming growth factor beta (TGFb)-induced expression of fibrogenic and inflammatory markers, in addition to decreasing TGFb induced collagen secretion, cell migration, proliferation and colony formation. Mechanistically, KISS1R signaling downregulated TGFb signaling by decreasing SMAD2/3 phosphorylation, via activation of protein-phosphatases PP2A, that dehosphorylates SMAD 2/3. This study revealed for the first time that kisspeptin reverses human hepatic fibrogenesis thus identifying it as a new therapeutic target to treat hepatic fibrosis.

  PublisherOA PDFDOI

• Supplementary Data from β-Arrestin/Ral Signaling Regulates Lysophosphatidic Acid–Mediated Migration and Invasion of Human Breast Tumor Cells

  2023-04-03

  preprintOpen accessSenior author

  Supplementary Data from β-Arrestin/Ral Signaling Regulates Lysophosphatidic Acid–Mediated Migration and Invasion of Human Breast Tumor Cells

  PublisherOA PDFDOI

• Data from β-Arrestin/Ral Signaling Regulates Lysophosphatidic Acid–Mediated Migration and Invasion of Human Breast Tumor Cells

  2023-04-03

  preprintOpen accessSenior author

  <div>Abstract<p>The lipid mediator lysophosphatidic acid (LPA) plays a role in cancer progression and signals via specific G protein–coupled receptors, LPA<sub>1-3</sub>. LPA has been shown to enhance the metastasis of breast carcinoma cells to bone. However, the mechanisms by which LPA receptors regulate breast cancer cell migration and invasion remain unclear. Breast cancer cell proliferation has been shown to be stimulated by Ral GTPases, a member of the Ras superfamily. Ral activity can be regulated by the multifunctional protein β-arrestin. We now show that HS578T and MDA-MB-231 breast cancer cells and MDA-MB-435 melanoma cells have higher expression of β-arrestin 1 mRNA compared with the nontumorigenic mammary MCF-10A cells. Moreover, we found that the mRNA levels of LPA<sub>1</sub>, LPA<sub>2</sub>, β-arrestin 2, and Ral GTPases are elevated in the advanced stages of breast cancer. LPA stimulates the migration and invasion of MDA-MB-231 cells, but not of MCF-10A cells, and this is mediated by pertussis toxin–sensitive G proteins and LPA<sub>1</sub>. However, ectopic expression of LPA<sub>1</sub> in MCF-10A cells caused these cells to acquire an invasive phenotype. Gene knockdown of either β-arrestin or Ral proteins significantly impaired LPA-stimulated migration and invasion. Thus, our data show a novel role for β-arrestin/Ral signaling in mediating LPA-induced breast cancer cell migration and invasion, two important processes in metastasis. (Mol Cancer Res 2009;7(7):1064–77)</p></div>

  PublisherDOI

• Data from β-Arrestin/Ral Signaling Regulates Lysophosphatidic Acid–Mediated Migration and Invasion of Human Breast Tumor Cells

  2023-04-03

  preprintOpen accessSenior author

  <div>Abstract<p>The lipid mediator lysophosphatidic acid (LPA) plays a role in cancer progression and signals via specific G protein–coupled receptors, LPA<sub>1-3</sub>. LPA has been shown to enhance the metastasis of breast carcinoma cells to bone. However, the mechanisms by which LPA receptors regulate breast cancer cell migration and invasion remain unclear. Breast cancer cell proliferation has been shown to be stimulated by Ral GTPases, a member of the Ras superfamily. Ral activity can be regulated by the multifunctional protein β-arrestin. We now show that HS578T and MDA-MB-231 breast cancer cells and MDA-MB-435 melanoma cells have higher expression of β-arrestin 1 mRNA compared with the nontumorigenic mammary MCF-10A cells. Moreover, we found that the mRNA levels of LPA<sub>1</sub>, LPA<sub>2</sub>, β-arrestin 2, and Ral GTPases are elevated in the advanced stages of breast cancer. LPA stimulates the migration and invasion of MDA-MB-231 cells, but not of MCF-10A cells, and this is mediated by pertussis toxin–sensitive G proteins and LPA<sub>1</sub>. However, ectopic expression of LPA<sub>1</sub> in MCF-10A cells caused these cells to acquire an invasive phenotype. Gene knockdown of either β-arrestin or Ral proteins significantly impaired LPA-stimulated migration and invasion. Thus, our data show a novel role for β-arrestin/Ral signaling in mediating LPA-induced breast cancer cell migration and invasion, two important processes in metastasis. (Mol Cancer Res 2009;7(7):1064–77)</p></div>

  PublisherDOI

• Editorial: The versatile kisspeptin: advances in cancer, metabolism, and reproduction

  Frontiers in Endocrinology · 2023-07-13 · 1 citations

  editorialOpen accessSenior authorCorresponding

  EDITORIAL article Front. Endocrinol., 13 July 2023Sec. Experimental Endocrinology Volume 14 - 2023 | https://doi.org/10.3389/fendo.2023.1239694

  PublisherOA PDFDOI

• Supplementary Data from β-Arrestin/Ral Signaling Regulates Lysophosphatidic Acid–Mediated Migration and Invasion of Human Breast Tumor Cells

  2023-04-03

  preprintOpen accessSenior author

  Supplementary Data from β-Arrestin/Ral Signaling Regulates Lysophosphatidic Acid–Mediated Migration and Invasion of Human Breast Tumor Cells

  PublisherDOI

• Human endometrial KISS1R inhibits stromal cell decidualization in a manner associated with a reduction in ESR1 levels

  bioRxiv (Cold Spring Harbor Laboratory) · 2022-11-20 · 1 citations

  preprintOpen access

  ABSTRACT Defective endometrial stromal cell decidualization is a major cause of recurrent implantation failure (RIF), a condition with a prevalence of ∼15%. To treat RIF, a stronger understanding of the endometrial factors that regulate decidualization is required. Here we studied the role of the kisspeptin receptor (KISS1R) in regulating human endometrial stromal cell (HESC) decidualization. Our data revealed KISS1R inhibits HESC decidualization in vitro in a manner associated with a striking reduction in ESR1 protein levels. To determine whether KISSR inhibition of decidualization results from reduced ESR1 levels we expressed the dominant negative ESR1-46 isoform in decidualizing HESCs. We found that expression of ESR1-46 in decidualizing HESCs ablated the expression of ESR1-66 and ESR1-54 isomers, and blocked decidualization. Interestingly, when ESR1-64 was co-expressed with ESR1-46, ESR1-66 and ESR1-54 expression was restored and decidualization was rescued. Taken together, these results suggest that KISS1R inhibits HESC decidualization by downregulating ESR1 levels. Based on our findings, we suggest that by inhibiting HESC decidualization, KISS1R regulates the depth of embryo invasion of the stroma, a requirement for a successful pregnancy.

  PublisherOA PDFDOI

Frequent coauthors

• Andy V. Babwah

  Johnson University

  90 shared

• Macarena Pampillo

  42 shared

• Magdalena Dragan

  15 shared

• Stephania Guzman

  Don Mariano Marcos Memorial State University

  15 shared

• Cynthia Pape

  Western University

  13 shared

• Muriel Brackstone

  13 shared

• Sally Radovick

  University of Arizona

  12 shared

• Maryse R. Ahow

  Children’s Health Research Institute

  11 shared