ArticleThe Journal of clinical investigation1995
Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association.
Article in The Journal of clinical investigation, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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
13 citing papers in PubMed, 71 citations in OpenAlex.
- Profiling the Genetic and Molecular Characteristics of Glanzmann Thrombasthenia: Can It Guide Current and Future Therapies?Journal of blood medicine · 2021Review
- Glanzmann thrombasthenia: state of the art and future directions.Seminars in thrombosis and hemostasis · 2013Review
- Do cell junction protein mutations cause an airway phenotype in mice or humans?American journal of respiratory cell and molecular biology · 2011Review
- Platelet gene therapy improves hemostatic function for integrin alphaIIbbeta3-deficient dogs.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Three novel beta-propeller mutations causing Glanzmann thrombasthenia result in production of normally stable pro-alphaIIb, but variably impaired progression of pro-alphaIIbbeta3 from endoplasmic reticulum to Golgi.Journal of thrombosis and haemostasis : JTH · 2005Article
- Mutations in and near the second calcium-binding domain of integrin alphaIIb affect the structure and function of integrin alphaIIbbeta3.The Biochemical journal · 2004Article
- Insights into integrin-ligand binding and activation from the first crystal structure.Arthritis research · 2002Review
- Platelet integrin alphaIIbbeta3-ligand interactions: what can we learn from the structure?International journal of hematology · 2001Review
- Demystified...adhesion molecule deficiencies.Molecular pathology : MP · 2001Review
- Defining extracellular integrin alpha-chain sites that affect cell adhesion and adhesion strengthening without altering soluble ligand binding.Molecular biology of the cell · 1997Article
- Truncation of the cytoplasmic domain of beta3 in a variant form of Glanzmann thrombasthenia abrogates signaling through the integrin alpha(IIb)beta3 complex.The Journal of clinical investigation · 1997Article
- Glanzmann thrombasthenia. Cooperation between sequence variants in cis during splice site selection.The Journal of clinical investigation · 1996Article
- The regulation of integrin function by divalent cations.Cell adhesion & migrationReview
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
To gain insight into region of the platelet GPIIb-IIIa complex involved in receptor biogenesis and function, we examined the biochemical properties of a defective GPIIb-IIIa complex from patient suffering from type II Glanzmann thrombasthenia. Flow cytometric as well as immunoblot analysis of patient platelets showed significantly reduced levels of GPIIb and GPIIIa compared with a normal control. Patient platelets, however, retained the ability to retract a fibrin clot. Sequence analysis of PCR-amplified platelet GPIIb mRNA revealed an Arg327-->His amino acid substitution between the second and third calcium-binding domains of the GPIIb heavy chain, a residue that is highly conserved among integrin alpha-subunits. The recombinant His327 form of GPIIb was found to be fully capable of associating with GPIIIa, therefore the role of the calcium-binding domains in intersubunit association was further examined by constructing amino-terminal segments of GPIIb that ended before the first, second, and third calcium-binding domains. All three fragments were found to associate with GPIIIa, demonstrating that the calcium-binding domains of GPIIb are not necessary for initial complex formation. Regions amino-terminal to the calcium-binding domains of GPIIb may play a heretofore unappreciated role in integrin subunit association.
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