{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T21:15:57Z","timestamp":1790716557432,"version":"4.1.0"},"reference-count":114,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2022,11,18]],"date-time":"2022-11-18T00:00:00Z","timestamp":1668729600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"PHS NIH RO1","award":["CA172040"],"award-info":[{"award-number":["CA172040"]}]},{"name":"PHS NIH RO1","award":["CA090321"],"award-info":[{"award-number":["CA090321"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.3390\/ijms232214359","type":"journal-article","created":{"date-parts":[[2022,11,21]],"date-time":"2022-11-21T02:52:21Z","timestamp":1668999141000},"page":"14359","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Galectin-1 and Galectin-3 in B-Cell Precursor Acute Lymphoblastic Leukemia"],"prefix":"10.3390","volume":"23","author":[{"given":"Fei","family":"Fei","sequence":"first","affiliation":[{"name":"Section of Molecular Carcinogenesis, Department of Pediatrics, Division of Hematology\/Oncology and Bone Marrow Transplantation, The Saban Research Institute of Children\u2019s Hospital, Los Angeles, CA 90027, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mingfeng","family":"Zhang","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Somayeh S.","family":"Tarighat","sequence":"additional","affiliation":[{"name":"Section of Molecular Carcinogenesis, Department of Pediatrics, Division of Hematology\/Oncology and Bone Marrow Transplantation, The Saban Research Institute of Children\u2019s Hospital, Los Angeles, CA 90027, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eun Ji","family":"Joo","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lu","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2769-2273","authenticated-orcid":false,"given":"Nora","family":"Heisterkamp","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Beckman Research Institute City of Hope, Monrovia, CA 91016, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,11,18]]},"reference":[{"key":"ref_1","unstructured":"Varki, A., Cummings, R.D., Esko, J.D., Stanley, P., Hart, G.W., Aebi, M., Mohnen, D., Kinoshita, T., Packer, N.H., and Prestegard, J.H. 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