Who We Are

The Yash Gandhi Foundation is a registered 501(c)(3) not for profit organization. There are no over-head costs or salaries paid out by this foundation. All contributions are 100% directed to fund for research in I-cell.

Support the Yash Gandhi Foundation

The Yash Gandhi Foundation is the only organization worldwide that directly and solely contributed money to I-Cell research. Any contribution of any amount is incredibly valuable and will provide hope to countless families who are affected by this horrible disease. 

Contact Us

Email: ygf4icell@gmail.com

Phone: 484.802.2317

Address: 105 Spur Lane, West Chester, PA 19382

  • Facebook - Grey Circle
  • Instagram - Grey Circle
  • Twitter - Grey Circle
  • YouTube - Grey Circle

© 2018 The Yash Gandhi Foundation 

Research Publications

The Yash Gandhi Foundation has awarded a total of $364,000 in research grants to multiple academic institutions. With the funding of research from the Yash Gandhi Foundation, these institutions have been working in collaboration and conducting research to unravel the molecular basis of I-cell disease and develop new model systems (particularly in zebrafish) to identify how loss of mannose 6-phosphate lysosomal targeting contributes to the development of disease symptoms. This information may lead to new therapies to treat ML disease.  The YGF-funded researchers are interested in establishing partnerships with pharmaceutical companies to accelerate therapy.

The Yash Gandhi Foundation has been acknowleged in 8 different research publications. The published manuscripts are outlined below;

  *Hover over box for further information

1. Qian, Y., Van Meel, E., Flanagan-Steet, H., Yox, A., Steet, R., and Kornfeld, S. Analysis of Mucolipidosis II/III GNPTAB Missense Mutations Identifies Domains of UDP-GlcNAc:Lysosomal Enzyme GlcNAc-1-Phosphotransferase Involved in Catalytic Function and Lysosomal Enzyme Recognition. J. Biol. Chem., 290:3045-3056, 2015.

2. Van Meel, E., Lee, W.S., Liu, L., Qian, Y., Doray, B., and Kornfeld, S. Multiple domains of GlcNAc-1-phosphotransferase mediate recognition of lysosomal enzymes. J. Biol. Chem., 291:8295-8304, 2016.

3. Van Meel, E., and Kornfeld, S. Mucolipidosis III GNPTG Missense Mutations Cause Misfolding of the gamma Subunit of GlcNAc-1-Phosphotransferase. Human Mutation, 37:623-626, 2016.

4. Liu, L., Lee, W.S., Doray, B., and Kornfeld, S. Role of spacer-1 in the maturation and function of GlcNAc-1-phosphotransferase. FEBS Letters, 591:47-55, 2016.

5. Liu, L., Lee, W.S., Doray, B., and Kornfeld, S. Engineering of GlcNAc-1-PHosphotransferase for Production of Highly Phosphorylated Lysosomal Enzymes for Enzyme Replacement Therapy. Molecular Therapy: Methods & Clinical Development, 5:59-65, 2017.

6.  Aarnio-Peterson M, Zhao P, Yu SH, Christian C, Flanagan-Steet H, Wells L, Steet R. Altered Met receptor phosphorylation and LRP1-mediated uptake in cells lacking carbohydrate-dependent lysosomal targeting.  J Biol Chem 292:15094-15104, 2017. 

7.  Flanagan-Steet H, Christian C, Lu PN, Aarnio-Peterson M, Sanman L, Archer-Hartmann S, Azadi P, Bogyo M, Steet RA. TGF-ß Regulates Cathepsin Activation during Normal and Pathogenic Development. Cell Reports 22:2964-2977, 2018.

8. Liu, L., Doray, B., and Kornfeld, S. Recycling of Golgi glycosyltransferases requires direct binding to coatomer. PNAS 2018;115 (36):8984-8989