Related Experiment Video
Updated: Aug 15, 2026

Development and Identification of a Novel Subpopulation of Human Neutrophil-derived Giant Phagocytes In Vitro
Published on: January 25, 2017
GMP-140: a receptor for neutrophils and monocytes on activated platelets and endothelium
1Department of Medicine, St. Francis Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City.
Abstract:
GMP-140 is a membrane glycoprotein located in secretory granules of platelets and endothelium. When these cells are activated by agonists such as thrombin, GMP-140 is rapidly translocated to the plasma membrane. GMP-140, along with ELAM-1 and the peripheral lymph node homing receptor, defines the selectin family of structurally related molecules that regulate interactions of leukocytes with the blood vessel wall. Each of these molecules contains an N-terminal lectin-like domain, followed by an EGF-like region, a series of consensus repeats related to those in complement-binding proteins, a transmembrane domain, and a short cytoplasmic tail. The genomic structures of the selectins suggest that they arose by duplication and modification of exons encoding specific structural domains. GMP-140 is a receptor for neutrophils and monocytes when it is expressed on activated platelets and endothelium. This property facilitates rapid adhesion of leukocytes to endothelium at regions of tissue injury as well as platelet-leukocyte interactions at sites of inflammation and hemorrhage. Like other leukocyte adhesion molecules, GMP-140 may also participate in pathologic inflammation, thrombosis, and tumor metastasis. Confirmation of such pathologic roles may lead to design of new drugs that block adhesive receptor function in human disease.
Insights
Platelet activation causes GMP-140 (granulocyte-macrophage progenitor-140) to move to the cell surface, where it acts as a receptor for leukocytes. This molecule plays a role in inflammation and may be a target for new therapies.
Area of Science:
- Cell Biology
- Immunology
- Molecular Biology
Background:
- GMP-140 is a membrane glycoprotein found in platelets and endothelial cells.
- Activation of these cells leads to GMP-140 translocation to the plasma membrane.
Purpose of the Study:
- To describe the structure and function of GMP-140.
- To elucidate the role of GMP-140 in leukocyte adhesion and inflammatory processes.
Main Methods:
- The study describes the molecular structure of GMP-140 and its family, the selectins.
- It discusses the cellular localization and translocation of GMP-140 upon cell activation.
- The research highlights GMP-140's function as a receptor for neutrophils and monocytes.
Main Results:
- GMP-140 is a member of the selectin family, characterized by specific protein domains.
- Upon activation, GMP-140 is expressed on the surface of platelets and endothelium.
- GMP-140 mediates the adhesion of leukocytes to the blood vessel wall, particularly at sites of injury or inflammation.
Conclusions:
- GMP-140 functions as a key adhesion molecule regulating leukocyte interactions with activated platelets and endothelium.
- Its role in inflammation, thrombosis, and metastasis suggests potential as a therapeutic target for blocking adhesive receptor function in disease.
Related Concept Videos
G-protein Coupled Receptors
G Protein-coupled Receptors
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Activation and Inactivation of G Proteins
GPCRs Regulate Adenylyl Cylase Activity
Two...
IP3/DAG Signaling Pathway
Transducer Mechanism: G Protein–Coupled Receptors
GPCRs are also called heptahelical, 7TM, or...

