Endocytosis

Mammalian cells take up extracellular material by a variety of different mechanisms that are collectively termed endocytosis. Endocytic mechanisms serve many important cellular functions including the uptake of extracellular nutrients, regulation of cell-surface receptor expression, maintenance of cell polarity, and antigen presentation. Endocytic pathways are also utilized by viruses, toxins, and symbiotic microorganisms to gain entry into cells. One of the best-characterized endocytic mechanisms is receptor-mediated endocytosis via clathrin-coated pits. This type of endocytosis constitutes the major emphasis of this review, with a brief discussion of other endocytic mechanisms and their comparison with the receptor-mediated pathway. This review describes and evaluates critically current understanding of the mechanisms of entry of plasma membrane components such as the receptor-ligand complexes and membrane lipids as well as the extracellular fluid into cells. The intracellular sorting and trafficking of these molecules upon internalization are also described. The roles of endocytosis in physiological and pathological processes are discussed. These include maintenance of cell polarization, antigen presentation, glucose transport, atherosclerosis, Alzheimer's disease, and the endocytosis of toxins and viruses.

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Drebrin 1 in dendritic cells regulates phagocytosis and cell surface receptor expression through recycling for efficient antigen presentation

Immunology ◽

10.1111/imm.13010 ◽

2018 ◽

Vol 156 (2) ◽

pp. 136-146 ◽

Cited By ~ 4

Author(s):

Diana M. Elizondo ◽

Temesgen E. Andargie ◽

Naomi L. Haddock ◽

Thomas A. Boddie ◽

Michael W. Lipscomb

Keyword(s):

Dendritic Cells ◽

Cell Surface ◽

Antigen Presentation ◽

Receptor Expression ◽

Cell Surface Receptor ◽

Surface Receptor

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Faculty Opinions recommendation of Cell surface receptor expression patterns in osteosarcoma.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.13200010.14542130 ◽

2011 ◽

Author(s):

Maria Michelagnoli ◽

Harriet Holme

Keyword(s):

Cell Surface ◽

Expression Patterns ◽

Receptor Expression ◽

Cell Surface Receptor ◽

Surface Receptor

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Endocytic Delivery of Vancomycin Mediated by a Synthetic Cell Surface Receptor: Rescue of Bacterially Infected Mammalian Cells and Tissue Targeting In Vivo

Journal of the American Chemical Society ◽

10.1021/ja067674f ◽

2007 ◽

Vol 129 (2) ◽

pp. 268-269 ◽

Cited By ~ 30

Author(s):

Siwarutt Boonyarattanakalin ◽

Jianfang Hu ◽

Sheryl A. Dykstra-Rummel ◽

Avery August ◽

Blake R. Peterson

Keyword(s):

Cell Surface ◽

Mammalian Cells ◽

Cell Surface Receptor ◽

Synthetic Cell ◽

Tissue Targeting ◽

Surface Receptor

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Porcine Breast Extracellular Matrix Hydrogel for Spatial Tissue Culture

International Journal of Molecular Sciences ◽

10.3390/ijms19102912 ◽

2018 ◽

Vol 19 (10) ◽

pp. 2912 ◽

Cited By ~ 5

Author(s):

Girdhari Rijal ◽

Jing Wang ◽

Ilhan Yu ◽

David Gang ◽

Roland Chen ◽

...

Keyword(s):

Extracellular Matrix ◽

Human Mammary Epithelial Cell ◽

Tumor Formation ◽

Receptor Expression ◽

Cell Surface Receptor ◽

Breast Diseases ◽

Porous Scaffolds ◽

Ecm Proteins ◽

Surface Receptor

Porcine mammary fatty tissues represent an abundant source of natural biomaterial for generation of breast-specific extracellular matrix (ECM). Here we report the extraction of total ECM proteins from pig breast fatty tissues, the fabrication of hydrogel and porous scaffolds from the extracted ECM proteins, the structural properties of the scaffolds (tissue matrix scaffold, TMS), and the applications of the hydrogel in human mammary epithelial cell spatial cultures for cell surface receptor expression, metabolomics characterization, acini formation, proliferation, migration between different scaffolding compartments, and in vivo tumor formation. This model system provides an additional option for studying human breast diseases such as breast cancer.

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Selective inhibition of the growth of human erythroid bursts by monoclonal antibodies against transferrin or the transferrin receptor

Blood ◽

10.1182/blood.v67.6.1631.1631 ◽

1986 ◽

Vol 67 (6) ◽

pp. 1631-1638 ◽

Cited By ~ 16

Author(s):

KM Shannon ◽

JW Larrick ◽

SA Fulcher ◽

KB Burck ◽

J Pacely ◽

...

Keyword(s):

Monoclonal Antibodies ◽

Transferrin Receptor ◽

Thymidine Incorporation ◽

Selective Inhibition ◽

Receptor Expression ◽

Cell Surface Receptor ◽

Transferrin Receptors ◽

Human Erythropoietin ◽

Surface Receptor ◽

Transferrin Receptor Expression

Abstract The relative requirements of colonies derived from erythroid (BFU-E) and myeloid (CFU-c) progenitors for transferrin were examined using monoclonal antibodies directed against the transferrin molecule (TF-6) or its cell surface receptor (TFR-A12, TFR1–2B). Growth of erythroid bursts was profoundly reduced at concentrations of all three antibodies that had no effect on CFU-c-derived colonies. When TFR1–2B was layered over cultures established one to seven days previously, further burst development was inhibited, and degeneration of early erythroid colonies was observed. Addition of erythropoietin augmented transferrin receptor expression on cells harvested after 1 to 2 weeks in culture and analyzed by flow cytometry. Recombinant human erythropoietin gave results comparable to those obtained in experiments using human urinary erythropoietin. Analysis of erythroblasts plucked directly from culture plates confirmed the presence of transferrin receptors on BFU-E-derived colonies. Thymidine incorporation was maximal early in the second week of culture and coincided with high transferrin receptor expression. These data demonstrate that transferrin must be available into the second week of culture to support the growth and differentiation of BFU- E-derived erythroid bursts, that the generation of erythroid colonies from BFU-E is more dependent on transferrin than myeloid colony formation from CFU-c, and that erythropoietin modulates the expression of transferrin receptors on growing bursts.

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Neutrophils from Preterm Neonates and Adults Show Similar Cell Surface Receptor Expression: Analysis Using a Whole Blood Assay

Neonatology ◽

10.1159/000244139 ◽

1995 ◽

Vol 67 (1) ◽

pp. 26-33 ◽

Cited By ~ 10

Author(s):

A.E. Falconer ◽

R. Carr ◽

S.W. Edwards

Keyword(s):

Cell Surface ◽

Expression Analysis ◽

Whole Blood ◽

Receptor Expression ◽

Cell Surface Receptor ◽

Preterm Neonates ◽

Whole Blood Assay ◽

Blood Assay ◽

Surface Receptor ◽

Similar Cell

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Neuropilin-1 and heparan sulfate proteoglycans cooperate in cellular uptake of nanoparticles functionalized by cationic cell-penetrating peptides

Science Advances ◽

10.1126/sciadv.1500821 ◽

2015 ◽

Vol 1 (10) ◽

pp. e1500821 ◽

Cited By ~ 36

Author(s):

Hong-Bo Pang ◽

Gary B. Braun ◽

Erkki Ruoslahti

Keyword(s):

Cell Surface ◽

Heparan Sulfate ◽

Vascular Permeability ◽

Mammalian Cells ◽

Cell Penetrating Peptides ◽

Proteolytic Processing ◽

Cell Surface Receptor ◽

Neuropilin 1 ◽

Cell Penetrating ◽

Surface Receptor

Cell-penetrating peptides (CPPs) have been widely used to deliver nanomaterials and other types of macromolecules into mammalian cells for therapeutic and diagnostic use. Cationic CPPs that bind to heparan sulfate (HS) proteoglycans on the cell surface induce potent endocytosis; however, the role of other surface receptors in this process is unclear. We describe the convergence of an HS-dependent pathway with the C-end rule (CendR) mechanism that enables peptide ligation with neuropilin-1 (NRP1), a cell surface receptor known to be involved in angiogenesis and vascular permeability. NRP1 binds peptides carrying a positive residue at the carboxyl terminus, a feature that is compatible with cationic CPPs, either intact or after proteolytic processing. We used CPP and CendR peptides, as well as HS- and NRP1-binding motifs from semaphorins, to explore the commonalities and differences of the HS and NRP1 pathways. We show that the CendR-NRP1 interaction determines the ability of CPPs to induce vascular permeability. We also show at the ultrastructural level, using a novel cell entry synchronization method, that both the HS and NRP1 pathways can initiate a macropinocytosis-like process and visualize these CPP-cargo complexes going through various endosomal compartments. Our results provide new insights into how CPPs exploit multiple surface receptor pathways for intracellular delivery.

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