ArticleProceedings of the National Academy of Sciences of the United States of America1996
BEN/SC1/DM-GRASP, a homophilic adhesion molecule, is required for in vitro myeloid colony formation by avian hemopoietic progenitors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 58 citations in OpenAlex.
- Mesenchymal stromal cell-associated migrasomes: a new source of chemoattractant for cells of hematopoietic origin.Cell communication and signaling : CCS · 2023Article
- The RNA m6A reader YTHDF2 controls NK cell antitumor and antiviral immunity.The Journal of experimental medicine · 2021Article
- Article
- SC1, an immunoglobulin-superfamily cell adhesion molecule, is involved in the brain metastatic activity of lung cancer cells.Oncology letters · 2015Article
- Alcam regulates long-term hematopoietic stem cell engraftment and self-renewal.Stem cells (Dayton, Ohio) · 2013Article
- Essential role for ALCAM gene silencing in megakaryocytic differentiation of K562 cells.BMC molecular biology · 2010Article
- Activated leukocyte cell adhesion molecule in breast cancer: prognostic indicator.Breast cancer research : BCR · 2004Article
- BEN/SC1/DM-GRASP expression during neuromuscular development: a cell adhesion molecule regulated by innervation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- MEMD, a new cell adhesion molecule in metastasizing human melanoma cell lines, is identical to ALCAM (activated leukocyte cell adhesion molecule).The American journal of pathology · 1998Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BEN/SC1/DM-GRASP is a membrane glycoprotein of the immunoglobulin superfamily isolated in the chick by several groups, including ours. Its expression is strictly developmentally regulated in several cell types of the nervous and hemopoietic systems and in certain epithelia. Each of these cell types expresses isoforms of BEN which differ by their level of N-glycosylation and by the presence or absence of the HNK-1 carbohydrate epitope. In the present work, the influence of glycosylation on BEN homophilic binding properties was investigated by two in vitro assays. First, each BEN isoform was covalently coupled to microspheres carrying different fluorescent dyes and an aggregation test was performed. We found that homophilic aggregates form indifferently between the same or different BEN isoforms, showing that glycosylation does not affect BEN homophilic binding properties. This was confirmed in the second test, where the BEN-coated microspheres bound to the neurites of BEN- expressing neurons, irrespective of the isoform considered. The transient expression of the BEN antigen on hemopoietic progenitors prompted us to see whether it might play a role in their proliferation and differentiation. When added to hemopoietic progenitor cells in an in vitro colony formation assay anti-BEN immunoglobulin strongly inhibited myeloid, but not erythroid, colony formation although both types of precursors express the molecule.
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