Molecular and Functional Glycomics

Glycosylation is one of the most common post-translational modifications: in eukaryotes: more than 50% of the proteins are glycosylated, and it’s estimated that around 0, 5% and the 1% of the human genome is dedicated to enzymes involved in the biosynthesis or degradation of glycoconjugates. The detailed structural analysis of these glycoconjugates in a certain organism (also called Glycomics), complements the information obtained through Proteomics or Genomics and provides a more realistic and integrated vision of the complex cellular system. In our laboratory, through the establishment of a glycoanalytic platform, we will study (using molecular, cellular and physiological approaches) the influence of diverse factors in the structural alteration of N- and O- glycans in serum and tissue glycoproteins, with a special focus into inflammatory chronic diseases and cancer.Understanding the relevance of glycosylation changes in health and disease, and in particular in the the transition from normal to inflamed tissue will potentially reveal novel opportunities for translational medicine.

Molecular and Functional Glycomics

  • Head

    Karina Mariño Currículum Vitae

    PhD in Chemistry

    Researcher at CONICET

  • Postdoctoral Researcher

    Dr Alejandro Cagnoni Currículum Vitae
  • Master in Biological Sciences

    Msc Luciano Morosi
  • MsC in Biological Sciences

    Msc Anabela Cutine


Our aim as a lab is to understand the glycobiology of the intestinal system, and through this to elucidate the role of glycans in inflammatory bowel diseases. We are also interested in studying the conection between the process of intestinal inflammation and the development of colon cancer. 

Schematic representation of the intestinal system in health (A) and disease (B)

Collaborations with Industry

Most relevant publications

- Driving CARs into Sweet Roads: Targeting Glycosylated Antigens in Cancer. A.G. Blidner, K.V. Mariño and G.A. Rabinovich. Immunity 2016, 44: 1248-1250. (Articulo Preview para Posey, A.D., Schwab, R.D., Boesteanu, A.C., Steentoft, C., Mandel, U., Engels, B., Stone, J.D., Madsen, T.D., Schreiber, K., Haines, K.M., et al. (2016). Immunity 44, 1444–1454.)

- Glycosylation-dependent binding of galectin-8 to activated leukocyte cell adhesion molecule (ALCAM/CD166) promotes its surface segregation on breast cancer cells. Fernández MM, Ferragut F, Cárdenas Delgado VM, Bracalente C, Bravo AI, Cagnoni AJ, Nuñez M, Morosi LG, Quinta HR, Espelt MV, Troncoso MF, Wolfenstein-Todel C, Mariño KV, Malchiodi EL, Rabinovich GA, Elola MT. Biochim Biophys Acta2016, Apr 26. pii: S0304-4165(16)30124-6. doi: 10.1016/j.bbagen.2016.04.019. [Epub ahead of print]

- Turning-off  signaling by Siglecs, Selectins and Galectins: chemical inhibition of glycan-dependent interactions in cancer.  A.J. Cagnoni, J.M. Pérez Sáez, G.A. Rabinovich*, K.V. Mariño* Frontiers in Oncology, 2016, in press. *Corresponding authors doi: 10.3389/fonc.2016.00109 

- A systematic approach to protein glycosylation analysis: a path through the maze. K. Mariño, J Bones,JJ Kattla & PM Rudd