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Galectin-1 and Galectin-3 in B-Cell Precursor Acute Lymphoblastic Leukemia.
Fei, Fei; Zhang, Mingfeng; Tarighat, Somayeh S; Joo, Eun Ji; Yang, Lu; Heisterkamp, Nora.
Afiliação
  • Fei F; Section of Molecular Carcinogenesis, Department of Pediatrics, Division of Hematology/Oncology and Bone Marrow Transplantation, The Saban Research Institute of Children's Hospital, Los Angeles, CA 90027, USA.
  • Zhang M; Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA.
  • Tarighat SS; Section of Molecular Carcinogenesis, Department of Pediatrics, Division of Hematology/Oncology and Bone Marrow Transplantation, The Saban Research Institute of Children's Hospital, Los Angeles, CA 90027, USA.
  • Joo EJ; Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA.
  • Yang L; Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA.
  • Heisterkamp N; Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA.
Int J Mol Sci ; 23(22)2022 Nov 18.
Article em En | MEDLINE | ID: mdl-36430839
Acute lymphoblastic leukemias arising from the malignant transformation of B-cell precursors (BCP-ALLs) are protected against chemotherapy by both intrinsic factors as well as by interactions with bone marrow stromal cells. Galectin-1 and Galectin-3 are lectins with overlapping specificity for binding polyLacNAc glycans. Both are expressed by bone marrow stromal cells and by hematopoietic cells but show different patterns of expression, with Galectin-3 dynamically regulated by extrinsic factors such as chemotherapy. In a comparison of Galectin-1 x Galectin-3 double null mutant to wild-type murine BCP-ALL cells, we found reduced migration, inhibition of proliferation, and increased sensitivity to drug treatment in the double knockout cells. Plant-derived carbohydrates GM-CT-01 and GR-MD-02 were used to inhibit extracellular Galectin-1/-3 binding to BCP-ALL cells in co-culture with stromal cells. Treatment with these compounds attenuated migration of the BCP-ALL cells to stromal cells and sensitized human BCP-ALL cells to vincristine and the targeted tyrosine kinase inhibitor nilotinib. Because N-glycan sialylation catalyzed by the enzyme ST6Gal1 can regulate Galectin cell-surface binding, we also compared the ability of BCP-ALL wild-type and ST6Gal1 knockdown cells to resist vincristine treatment when they were co-cultured with Galectin-1 or Galectin-3 knockout stromal cells. Consistent with previous results, stromal Galectin-3 was important for maintaining BCP-ALL fitness during chemotherapy exposure. In contrast, stromal Galectin-1 did not significantly contribute to drug resistance, and there was no clear effect of ST6Gal1-catalysed N-glycan sialylation. Taken together, our results indicate a complicated joint contribution of Galectin-1 and Galectin-3 to BCP-ALL survival, with different roles for endogenous and stromal produced Galectins. These data indicate it will be important to efficiently block both extracellular and intracellular Galectin-1 and Galectin-3 with the goal of reducing BCP-ALL persistence in the protective bone marrow niche during chemotherapy.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Linfoma de Burkitt / Leucemia-Linfoma Linfoblástico de Células Precursoras Limite: Animals / Humans Idioma: En Revista: Int J Mol Sci Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Linfoma de Burkitt / Leucemia-Linfoma Linfoblástico de Células Precursoras Limite: Animals / Humans Idioma: En Revista: Int J Mol Sci Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos