ArticleBlood advances2018
Glycophorin-C sialylation regulates Lu/BCAM adhesive capacity during erythrocyte aging.
Article in Blood advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 28 citations in OpenAlex.
- Protein S Enhances the Phagocytosis of Phosphatidylserine-Exposing Erythrocytes: Implications in Sickle Cell Disease.American journal of hematology · 2026Article
- Non-Integrin Laminin Receptors: Shedding New Light and Clarity on Their Involvement in Human Diseases.International journal of molecular sciences · 2025Review
- Sialic acid in the regulation of blood cell production, differentiation and turnover.Immunology · 2024Review
- The Role of Lutheran/Basal Cell Adhesion Molecule in Hematological Diseases and Tumors.International journal of molecular sciences · 2024Review
- The Double-Edged Sword of Erythrocytes in Health and Disease via Their Adhesiveness.International journal of molecular sciences · 2023Review
- Malaria-associated adhesion molecule activation facilitates the destruction of uninfected red blood cells.Blood advances · 2022Article
- Measurement of erythrocyte membrane mannoses to assess splenic function.British journal of haematology · 2022Article
- Erythrocyte flow through the interendothelial slits of the splenic venous sinus.Biomechanics and modeling in mechanobiology · 2021Article
- The RBC's road to ghost and removal: splenic clearance.Blood advances · 2021Article
- Oxidative stress activates red cell adhesion to laminin in sickle cell disease.Haematologica · 2021Article
- The Multiple Facets of Iron Recycling.Genes · 2021Review
- Article
- Red Blood Cells: Tethering, Vesiculation, and Disease in Micro-Vascular Flow.Diagnostics (Basel, Switzerland) · 2021Article
- Glycosylation and Aging.Advances in experimental medicine and biology · 2021Article
- How Do Red Blood Cells Die?Frontiers in physiology · 2021Review
- The Gardos effect drives erythrocyte senescence and leads to Lu/BCAM and CD44 adhesion molecule activation.Blood advances · 2020Article
- Red Blood Cells: Chasing Interactions.Frontiers in physiology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lutheran/basal cell adhesion molecule (Lu/BCAM) is a transmembrane adhesion molecule expressed by erythrocytes and endothelial cells that can interact with the extracellular matrix protein laminin-α5. In sickle cell disease, Lu/BCAM is thought to contribute to adhesion of sickle erythrocytes to the vascular wall, especially during vaso-occlusive crises. On healthy erythrocytes however, its function is unclear. Here we report that Lu/BCAM is activated during erythrocyte aging. We show that Lu/BCAM-mediated binding to laminin-α5 is restricted by interacting, in cis, with glycophorin-C-derived sialic acid residues. Following loss of sialic acid during erythrocyte aging, Lu/BCAM is released from glycophorin-C and allowed to interact with sialic acid residues on laminin-α5. Decreased glycophorin-C sialylation, as observed in individuals lacking exon 3 of glycophorin-C, the so-called Gerbich phenotype, was found to correlate with increased Lu/BCAM-dependent binding to laminin-α5. In addition, we identified the sialic acid-binding site within the third immunoglobulin-like domain within Lu/BCAM that accounts for the interaction with glycophorin-C and laminin-α5. Last, we present evidence that neuraminidase-expressing pathogens, such as
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.