ArticleBlood2008
Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin.
Article in Blood, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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Who cites it
13 citing papers in PubMed, 0 citations in OpenAlex.
- The Role of Lutheran/Basal Cell Adhesion Molecule in Hematological Diseases and Tumors.International journal of molecular sciences · 2024Review
- Malaria-associated adhesion molecule activation facilitates the destruction of uninfected red blood cells.Blood advances · 2022Article
- Laminin α5_CD239_Spectrin is a candidate association that compensates the linkage between the basement membrane and cytoskeleton in skeletal muscle fibers.Matrix biology plus · 2022Article
- Oxidative stress activates red cell adhesion to laminin in sickle cell disease.Haematologica · 2021Article
- The role of spectrin in cell adhesion and cell-cell contact.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Mercury leads to abnormal red blood cell adhesion to laminin mediated by membrane sulfatides.Biochimica et biophysica acta. Biomembranes · 2019Article
- Red Blood Cells: Chasing Interactions.Frontiers in physiology · 2019Review
- Glycophorin-C sialylation regulates Lu/BCAM adhesive capacity during erythrocyte aging.Blood advances · 2018Article
- Article
- The lutheran/basal cell adhesion molecule promotes tumor cell migration by modulating integrin-mediated cell attachment to laminin-511 protein.The Journal of biological chemistry · 2013Article
- Epinephrine modulates BCAM/Lu and ICAM-4 expression on the sickle cell trait red blood cell membrane.Biophysical journal · 2012Article
- An antibody to the lutheran glycoprotein (Lu) recognizing the LU4 blood type variant inhibits cell adhesion to laminin α5.PloS one · 2011Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The Lutheran (Lu) and Lu(v13) blood group glycoproteins function as receptors for extracellular matrix laminins. Lu and Lu(v13) are linked to the erythrocyte cytoskeleton through a direct interaction with spectrin. However, neither the molecular basis of the interaction nor its functional consequences have previously been delineated. In the present study, we defined the binding motifs of Lu and Lu(v13) on spectrin and identified a functional role for this interaction. We found that the cytoplasmic domains of both Lu and Lu(v13) bound to repeat 4 of the alpha spectrin chain. The interaction of full-length spectrin dimer to Lu and Lu(v13) was inhibited by repeat 4 of alpha-spectrin. Further, resealing of this repeat peptide into erythrocytes led to weakened Lu-cytoskeleton interaction as demonstrated by increased detergent extractability of Lu. Importantly, disruption of the Lu-spectrin linkage was accompanied by enhanced cell adhesion to laminin. We conclude that the interaction of the Lu cytoplasmic tail with the cytoskeleton regulates its adhesive receptor function.
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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.