ArticleThe Journal of experimental medicine1996
A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid.
Article in The Journal of experimental medicine, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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.
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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
16 citing papers in PubMed, 69 citations in OpenAlex.
- Molecular mechanism of CD44 homodimerization modulated by palmitoylation and membrane environments.Biophysical journal · 2022Article
- Chemotherapy induces feedback up-regulation of CD44v6 in colorectal cancer initiating cells throughFrontiers in oncology · 2022Article
- Proteolytic Processing of CD44 and Its Implications in Cancer.Stem cells international · 2021Review
- CNTs mediated CD44 targeting; a paradigm shift in drug delivery for breast cancer.Genes & diseases · 2020Review
- Pursuing Intracellular Pathogens with Hyaluronan. From a 'Pro-Infection' Polymer to a Biomaterial for 'Trojan Horse' Systems.Molecules (Basel, Switzerland) · 2018Review
- Coming of Age: CD96 Emerges as Modulator of Immune Responses.Frontiers in immunology · 2018Review
- Homodimerization of the Lymph Vessel Endothelial Receptor LYVE-1 through a Redox-labile Disulfide Is Critical for Hyaluronan Binding in Lymphatic Endothelium.The Journal of biological chemistry · 2016Article
- Article
- CD44 engagement promotes matrix-derived survival through the CD44-SRC-integrin axis in lipid rafts.Molecular and cellular biology · 2008Article
- Acylation of CD44 and its association with lipid rafts are required for receptor and hyaluronan endocytosis.The Journal of biological chemistry · 2006Article
- Article
- Cell-surface prion protein interacts with glycosaminoglycans.The Biochemical journal · 2002Article
- CD44-mediated oncogenic signaling and cytoskeleton activation during mammary tumor progression.Journal of mammary gland biology and neoplasia · 2001Review
- CD44 cell adhesion molecules.Molecular pathology : MP · 1999Review
- LYVE-1, a new homologue of the CD44 glycoprotein, is a lymph-specific receptor for hyaluronan.The Journal of cell biology · 1999Article
- Identification of a costimulatory molecule rapidly induced by CD40L as CD44H.The Journal of experimental medicine · 1996Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In the transmembrane domain and cytoplasmic domain of human CD44 protein there are two cysteine residues. These two cysteines are conserved in all known mammalian CD44 proteins. The functions of these cysteine residues are not known. Site-specific mutagenesis was used to create CD44 mutant proteins lacking either one or both of these cysteine residues. Wild-type CD44 and mutant CD44 genes were transfected into CD44- Jurkat cells to establish stable transfectants. These transfectants were used to study whether these two cysteine residues are important in the binding of CD44(H) to fluorescein-conjugated hyaluronic acid (F-HA). Jurkat transfectant bearing wild-type CD44 did not bind F-HA, unless they were stimulated in vitro with immobilized anti-CD3 monoclonal antibody. Anti-CD3 antibody also stimulated the binding of F-HA in Jurkat CD44.C295A transfectant in which the cytoplasmic cysteine residue has been replaced with alanine. In contrast, anti-CD3 antibody failed to stimulate the binding of F-HA in Jurkat transfectant (CD44.C286A), in which the transmembrane domain cysteine 286 has been replaced with an alanine, and in Jurkat transfectant CD44.2C2A, in which both of the cysteine residues have been altered. Binding can also be induced with a monoclonal anti-CD44 antibody (F-44-10-2) in Jurkat wild-type CD44 and Jurkat CD44.C295A transfectants but not in CD44. C286A transfectant. These results provide evidence that the transmembrane domain of CD44, more specifically the cysteine residue in the transmembrane domain, is important for both activation-induced and anti-CD44 antibody-induced binding of soluble HA.
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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.