Bio


Dr. Avinash Londhe is a postdoctoral researcher in Dr. Katrin Svensson’s lab in the Department of Pathology at Stanford University, where he investigates the complex mechanisms linking cancer, metabolism, and obesity. His research focuses on understanding how orphan peptide hormones regulate metabolic pathways and identifying novel receptor-peptide interactions. Driven by a passion for translational science, Dr. Londhe is committed to translating fundamental discoveries into real-world solutions that improve patient outcomes.

During his doctoral training in Dr. Benoit Boivin’s lab at SUNY Polytechnic Institute, Dr. Londhe gained in-depth expertise in molecular mechanisms underlying metabolic disorders and cancer. His work contributed to the development of therapeutic strategies aimed at metabolic dysfunction. In addition to research, he excelled at managing laboratory operations and mentoring both graduate and undergraduate students, fostering a dynamic and collaborative research environment.

Currently, Dr. Londhe is broadening his research toolkit by integrating bioinformatics, molecular biology, and biophysical techniques into his experimental approaches. His goal is to address critical challenges in cancer metabolism and metabolic diseases through innovative research.

Dr. Londhe aspires to secure a faculty position at a leading university, where he can advance impactful research, mentor emerging scientists, and continue driving scientific innovation.

Honors & Awards


  • RNA Fellow, RNA Institute, University of Albany (2020)
  • Young Investigator Award, Society for Redox Biology and Medicine (Nov-2022)
  • John J. Sullivan Professional Development Award, State University of New York (02/2020, 11/2022)
  • Campus de Excelencia Internacional UAM+CSIC, Universidad Autonoma de Madrid (Sep-2014)
  • Eklavya Fellowship for Masters, Eklavya India Foundation (2008)

Professional Education


  • Ph.D., State Unviersity of New York, Albany NY, Nanobioscience (2024)
  • M.S., Autonomous University of Madrid, Spain, Molecular Biomedicine (2015)
  • M.Sc., National Institute of Virology, Pune, Virology (2010)
  • Bachelor of Science, University Of Pune (2008)

Stanford Advisors


All Publications


  • Measuring the Reversible Oxidation of Protein Tyrosine Phosphatases Using a Modified Cysteinyl-Labeling Assay. Methods in molecular biology (Clifton, N.J.) Londhe, A. D., Boivin, B. 2024; 2743: 223-237

    Abstract

    The modified cysteinyl-labeling assay enables the labeling, enrichment, and detection of all members of the protein tyrosine phosphatase (PTP) superfamily that become reversibly oxidized in cells to facilitate phosphorylation-dependent signaling. In this chapter, we describe the method in detail and highlight the pitfalls of avoiding post-lysis oxidation of PTPs to measure the dynamic and transient oxidation and reduction of PTPs in cell signaling.

    View details for DOI 10.1007/978-1-0716-3569-8_15

    View details for PubMedID 38147219

    View details for PubMedCentralID 2481340

  • Protein tyrosine phosphatase 1B regulates miR-208b-argonaute 2 association and thyroid hormone responsiveness in cardiac hypertrophy. Science signaling Coulis, G., Londhe, A. D., Sagabala, R. S., Shi, Y., Labbé, D. P., Bergeron, A., Sahadevan, P., Nawaito, S. A., Sahmi, F., Josse, M., Vinette, V., Guertin, M. C., Karsenty, G., Tremblay, M. L., Tardif, J. C., Allen, B. G., Boivin, B. 2022; 15 (730): eabn6875

    Abstract

    Increased production of reactive oxygen species plays an essential role in the pathogenesis of several diseases, including cardiac hypertrophy. In our search to identify redox-sensitive targets that contribute to redox signaling, we found that protein tyrosine phosphatase 1B (PTP1B) was reversibly oxidized and inactivated in hearts undergoing hypertrophy. Cardiomyocyte-specific deletion of PTP1B in mice (PTP1B cKO mice) caused a hypertrophic phenotype that was exacerbated by pressure overload. Furthermore, we showed that argonaute 2 (AGO2), a key component of the RNA-induced silencing complex, was a substrate of PTP1B in cardiomyocytes and in the heart. Our results revealed that phosphorylation at Tyr393 and inactivation of AGO2 in PTP1B cKO mice prevented miR-208b-mediated repression of thyroid hormone receptor-associated protein 1 (THRAP1; also known as MED13) and contributed to thyroid hormone-mediated cardiac hypertrophy. In support of this conclusion, inhibiting the synthesis of triiodothyronine (T3) with propylthiouracil rescued pressure overload-induced hypertrophy and improved myocardial contractility and systolic function in PTP1B cKO mice. Together, our data illustrate that PTP1B activity is cardioprotective and that redox signaling is linked to thyroid hormone responsiveness and microRNA-mediated gene silencing in pathological hypertrophy.

    View details for DOI 10.1126/scisignal.abn6875

    View details for PubMedID 35439023

    View details for PubMedCentralID PMC9125740

  • In Vitro Activity Assays to Quantitatively Assess the Endogenous Reversible Oxidation State of Protein Tyrosine Phosphatases in Cells. Current protocols in chemical biology Londhe, A. D., Rizvi, S. H., Boivin, B. 2020; 12 (3): e84

    Abstract

    The reversible oxidation of protein tyrosine phosphatases (PTPs) impairs their ability to dephosphorylate substrates in vivo. This transient inactivation of PTPs occurs as their conserved catalytic cysteine residue reacts with cellular oxidants thereby abolishing the ability of this reactive cysteine to attack the phosphate of the target substrate. Hence, in vivo, the inhibition of specific PTPs in response to regulated and localized rises in cellular oxidants enables phospho-dependent signaling. We present assays that measure the endogenous activity of specific PTPs that become transiently inactivated in cells exposed to growth factors. Here, we describe the methods and highlight the pitfalls to avoid post-lysis oxidation of PTPs in order to assess the inactivation and the reactivation of PTPs targeted by cellular oxidants in signal transduction. © 2020 Wiley Periodicals LLC. Basic Protocol 1: Cell transfection (optional) Support Protocol: Preparation of degassed lysis buffers Basic Protocol 2: Cellular extraction in anaerobic conditions Basic Protocol 3: Enrichment and activity assay of specific PTPs Alternate Protocol: Measurement of active PTPs via direct cysteinyl labeling.

    View details for DOI 10.1002/cpch.84

    View details for PubMedID 32805074

    View details for PubMedCentralID PMC7493824

  • Regulation of PTP1B activation through disruption of redox-complex formation. Nature chemical biology Londhe, A. D., Bergeron, A., Curley, S. M., Zhang, F., Rivera, K. D., Kannan, A., Coulis, G., Rizvi, S. H., Kim, S. J., Pappin, D. J., Tonks, N. K., Linhardt, R. J., Boivin, B. 2020; 16 (2): 122-125

    Abstract

    We have identified a molecular interaction between the reversibly oxidized form of protein tyrosine phosphatase 1B (PTP1B) and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B prevented PTP1B inactivation by reactive oxygen species and decreased epidermal growth factor receptor phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells.

    View details for DOI 10.1038/s41589-019-0433-0

    View details for PubMedID 31873221

    View details for PubMedCentralID PMC6982540

  • Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis. Acta crystallographica. Section F, Structural biology and crystallization communications Khandokar, Y. B., Londhe, A., Patil, S., Forwood, J. K. 2013; 69 (Pt 11): 1303-6

    Abstract

    Neisseria meningitidis is the causative microorganism of many human diseases, including bacterial meningitis; together with Streptococcus pneumoniae, it accounts for approximately 80% of bacterial meningitis infections. The emergence of antibiotic-resistant strains of N. meningitidis has created a strong urgency for the development of new therapeutics, and the high-resolution structural elucidation of enzymes involved in cell metabolism represents a platform for drug development. Acetyl-CoA hydrolase is involved in multiple functions in the bacterial cell, including membrane synthesis, fatty-acid and lipid metabolism, gene regulation and signal transduction. Here, the first recombinant protein expression, purification and crystallization of a hexameric acetyl-CoA hydrolase from N. meningitidis are reported. This protein was crystallized using the hanging-drop vapour-diffusion technique at pH 8.5 and 290 K using ammonium phosphate as a precipitant. Optimized crystals diffracted to 2.0 Å resolution at the Australian Synchrotron and belonged to space group P2(1)3 (unit-cell parameters a = b = c = 152.2 Å), with four molecules in the asymmetric unit.

    View details for DOI 10.1107/S1744309113028042

    View details for PubMedID 24192375

    View details for PubMedCentralID PMC3818059