Platelet receptors
Abstract
This article highlights the increasing knowledge of the biochemistry, pathology, and cell and molecular biology of platelet receptors. A receptor for ADP has been identified using the affinity label FSBA as aggregin, a 100-kd membrane protein, responsible for shape change, aggregation, and exposure of fibrinogen binding sites. A variety of putative receptors for collagen have been described with GP Ia and GP IV receiving the most attention recently. A thromboxane A2 receptor has been identified using receptor antagonists and photoaffinity labels. The alpha 2-adrenergic receptor has been cloned and expressed. The platelet thrombin receptor has been identified as GP Ib. Following binding of thrombin to this receptor, activation of calpain occurs with cleavage of aggregin leading to exposure of GP IIb/IIIa and platelet aggregation. Isolation, expression, or both of the ADP, collagen, and thrombin receptors as single gene products of the human platelet responsible for activation, and more complete understanding of stimulus-response coupling should allow for greater specificity of drugs with selective therapeutic actions.
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Human platelets express α2A, α2B, and β2 ADRs.
“focusing on family members present on human platelets (α2A, α2B and β2 ADRs) (Anfossi and Trovati, 1996; Barnett et al., 1985; Colman, 1990).”
From A Cardiovascular Disease-Linked Gut Microbial Metabolite Acts via Adrenergic Receptors (2020) · cites this paper as Colman, 1990
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A Cardiovascular Disease-Linked Gut Microbial Metabolite Acts via Adrenergic Receptors
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- Authors
- Colman, R. W.
- Affiliations
- Temple University (US)
- Corresponding author
- Colman, Robert W.
- Venue
- Hematology/Oncology Clinics of North America
- Publisher
- Elsevier BV
- Published
- 1990-02
- Volume
- 4
- Issue
- 1
- Pages
- 27-42
- ISSN
- 0889-8588 (ISSN-L)
- OpenAlex
- W4245028793
- Cited by
- 12
- References
- 92
- Citations by year
- 2026: 1 · 2020: 1 · 2018: 1
- FWCI
- 0.24
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Hematology/Oncology Clinics of North America (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl024365-11, 5p01hl036579-05)
- National Heart, Lung, and Blood Institute (HL 24365, HL36579)
- Topics
- Health Sciences › Medicine › Hematology › Platelet Disorders and Treatments
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- platelet receptors, ADP receptor, collagen receptor, thromboxane A2 receptor, alpha2-adrenoceptors, protease-activated receptor 1, glycoprotein Ib, calpain, platelet aggregation, fibrinogen binding, stimulus-response coupling, platelet activation
- MeSH terms
- Adenosine Diphosphate, Animals, Blood Platelets, Collagen, Humans, Platelet Membrane Glycoproteins, Receptors, Adrenergic, alpha, Receptors, Cell Surface, Thrombin, Thromboxane A2, Platelet Activation
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