Related Experiment Video
Updated: Jul 19, 2026
11:25
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Stabilin-1, a homeostatic scavenger receptor with multiple functions
Julia Kzhyshkowska1, A Gratchev, S Goerdt
1Department of Dermatology, University Medical Centre Mannheim, University of Heidelberg, Theodor-Kutzer Ufer 1-3, D-68167 Mannheim, Germany. julia.kzhyshkowska@haut.ma.uni-heidelberg.de
Journal of Cellular and Molecular Medicine
|September 23, 2006
Summary
Stabilin-1 is a scavenger receptor involved in intracellular trafficking and the uptake of molecules by macrophages. Its expression is upregulated during inflammation and cancer, impacting macrophage function.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Background:
- Stabilin-1 (STAB1) is a multifunctional scavenger receptor identified as the MS-1 antigen.
- It is expressed by sinusoidal endothelial cells and tissue macrophages, with expression induced during inflammation and tumorigenesis.
- In vitro, glucocorticoids induce STAB1 expression in macrophages.
Purpose of the Study:
- To investigate the role of stabilin-1 in intracellular trafficking pathways.
- To elucidate the mechanisms of stabilin-1 trafficking and its interaction with other molecules.
- To understand the function of stabilin-1 in alternatively activated macrophages.
Main Methods:
- Histological studies to determine STAB1 expression patterns.
- In vitro induction of STAB1 in macrophages using glucocorticoids.
- Analysis of intracellular trafficking pathways involving GGAs and the DDSLL motif.
- Investigation of STAB1-mediated uptake and degradation of acLDL and SPARC.
- Study of STAB1 interaction with chitinase-like protein (SI-CLP).
Main Results:
- Stabilin-1 mediates receptor-mediated endocytosis, recycling, and shuttling between endosomes and the trans-Golgi network (TGN).
- GGAs and the DDSLL motif are involved in stabilin-1 trafficking.
- In alternatively activated macrophages, STAB1 facilitates the uptake and degradation of acLDL and SPARC.
- Stabilin-1 is involved in the lysosomal delivery of SI-CLP.
Conclusions:
- Stabilin-1 acts as a homeostatic receptor linking extracellular signals to intracellular vesicular processes.
- Its rapid recycling and low surface expression suggest a limited role in universal cell adhesion.
- Stabilin-1 influences the macrophage secretion profile, with implications for inflammation and tumorigenesis.
Related Concept Videos
01:30Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
01:28The Early Endosome: Endocytosis of Transferrin
Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
02:17Microtubule Instability
Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated assembly and...
01:15Receptor Downregulation in MVBs
Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR activation may...
The EGFR can initiate signaling pathways that lead to cell proliferation, migration, and differentiation. Overexpression of EGFR stimulates cells to proliferate. Excessive EGFR activation may...
01:20The JAK-STAT Signaling Pathway
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
01:45Regulation of Nuclear Protein Sorting
Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...