Dansyl cadaverine regulates ligand induced endocytosis of interleukin‐8 receptor in human polymorphonuclear neutrophils

Ray, Ena; Samanta, Abhishek

doi:10.1016/0014-5793(95)01462-4

Cited by 34 publications

(20 citation statements)

References 24 publications

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“…The enzymatic action of transglutaminase involves cross-linking of proteins by forming an isopeptide bond between a lysine residue of one protein and a glutamine residue of another protein during coated pit formation. MDC has been shown to block endocytosis of ␣ 2 -macroglobulin and many polypeptide hormones and cytokines like epidermal growth factor, hepatocyte growth factor, insulin-like growth factor-I, and IL-8 (37,38,40,43,44,58,60). MDC-mediated inhibition of transglutaminase has also been implicated in the blocking of endocytosis of vesicular stomatitis virus, Semliki Forest virus, and other types of endocytosis occurring through clathrincoated vesicles (61,62).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Receptor Internalization by Monodansylcadaverine Selectively Blocks p55 Tumor Necrosis Factor Receptor Death Domain Signaling

Schütze

Machleidt

Adam

et al. 1999

Journal of Biological Chemistry

192

142

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The 55-kDa receptor for tumor necrosis factor (TR55) triggers multiple signaling cascades initiated by adapter proteins like TRADD and FAN. By use of the primary amine monodansylcadaverine (MDC), we addressed the functional role of tumor necrosis factor (TNF) receptor internalization for intracellular signal distribution. We show that MDC does not prevent the interaction of the p55 TNF receptor (TR55) with FAN and TRADD. Furthermore, the activation of plasmamembrane-associated neutral sphingomyelinase activation as well as the stimulation of proline-directed protein kinases were not affected in MDC-treated cells. In contrast, activation of signaling enzymes that are linked to the "death domain" of TR55, like acid sphingomyelinase and c-Jun-N-terminal protein kinase as well as TNF signaling of apoptosis in U937 and L929 cells, are blocked in the presence of MDC. The results of our study suggest a role of TR55 internalization for the activation of select TR55 death domain signaling pathways including those leading to apoptosis.Tumor necrosis factor (TNF), 1 originally defined by its antitumoral activity, is now recognized as a pleiotropic cytokine exerting a wide variety of immunoregulatory activities (for review, see Refs. 1-3). TNF action is mediated by two types of cell surface receptors of 55 kDa (TR55) and 75 kDa (TR75) molecular masses, respectively. Both receptors mediate distinct TNF responses (4 -6). The majority of activities of soluble TNF appears to be mediated by TR55 (7-11). Like other cytokine receptors, the cytoplasmic domain of both TNF receptors lacks intrinsic enzymatic activities. The activation of intracellular signaling enzyme systems is initiated by a selective interplay between the cytoplasmic domain of the TNF receptors and a number of recently identified TNF receptor-associated proteins (see Ref. Results from numerous studies have revealed that TNF signaling further involves activation of downstream enzyme systems at multiple subcellular compartments such as the plasmamembrane, endosomes, mitochondria, the cytosol, and the nucleus (for review, see Refs. 11, 23, and 24). Membrane-associated enzyme systems transmitting TR55 signals include plasmamembrane-bound phospholipases such as phosphatidylcholine-specific phospholipase C (25), which generates the lipid second messenger molecule 1,2-diacylglycerol and a N-SMase (9), producing ceramide by sphingomyelin hydrolysis. Ceramide generated at the plasmamembrane triggers activation of a 97-kDa ceramide-activated protein kinase (26), recently suggested to be identical with the "kinase suppressor of ras" (27). Ceramide-activated protein kinase belongs to a family of proline-directed protein kinases (PDPK) (9), including members of the mitogen-activated protein kinases (28). TNF signaling further involves intracellular membrane compartments like caveolae and endosomes harboring an acid SMase (A-SMase) (9,29,30). In mitochondria, TNF induces reactive oxygen species that are generated at the level of the oxidative phosphorylation complex III (31). T...

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Section: Discussionmentioning

confidence: 99%

Inhibition of Receptor Internalization by Monodansylcadaverine Selectively Blocks p55 Tumor Necrosis Factor Receptor Death Domain Signaling

Schütze

Machleidt

Adam

et al. 1999

Journal of Biological Chemistry

192

142

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“…Upon ligand binding, many receptors, such as the interleukin-8 receptor, the -opioid receptor, and the pattern recognition receptor, undergo internalization (57)(58)(59). Like these receptors, CCR2 is also expected to translocate from the plasma membrane to intracellular vesicles upon MCP1 binding (60).…”

Section: Discussionmentioning

confidence: 99%

The C Terminus of Mouse Monocyte Chemoattractant Protein 1 (MCP1) Mediates MCP1 Dimerization while Blocking Its Chemotactic Potency

Yao

Tsirka

2010

Journal of Biological Chemistry

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The extracellular protease plasmin cleaves mouse MCP1 (monocyte chemoattractant protein 1) at lysine 104, releasing a 50-amino acid C-terminal domain. The cleavage event increases the chemotactic activity of MCP1 and, by doing so, promotes the progression of excitotoxic injury in the central nervous system in pathological settings. The mechanism through which the cleavage event enhances MCP1-mediated chemoattraction is unknown; to investigate it, we use wild-type and mutant forms of recombinant MCP1. Full-length MCP1 (FL-MCP1) is secreted by cells as a dimer or multimer. We show that a mutant truncated at the C terminus, K104Stop-MCP1, does not dimerize, revealing that the C terminus mediates the interaction. Microglia, the immune-like cells normally present in the brain, derive from the bone marrow (1-5), enter the central nervous system (CNS) early during development, and reside in the parenchyma in a resting state characterized by ramified morphology. In the healthy brain, they continually extend and retract their processes to sense changes in the surrounding microenvironment (6). However, when there is an injury in the CNS, microglia switch to an activated state characterized by changes in gene expression, morphology, and proliferation (6 -16). The activated microglia then migrate to the site of injury and modify the injury outcome.The migration of microglia to the site of injury is stimulated by the local release of chemokines, a superfamily of structurally related small proteins that function as chemoattractants. A potent chemoattractant for monocytes/microglia (17), MCP1 (monocyte chemoattractant protein-1; also called CCL2), is upregulated in many types of CNS injury, including ischemia, hemorrhage, trauma, infection, hypoxia, and peripheral nerve axotomy (18 -24). The MCP1 protein is highly conserved in the N terminus among different species, whereas the C terminus is much more variable. The rodent MCP1 C terminus is decorated extensively with O-linked carbohydrates (25), which bind both soluble glycosaminoglycans (GAGs) and GAGs immobilized on the cell surface. Soluble GAGs inhibit the binding of MCP1 to its high affinity receptor CCR2 (30), which is expressed by microglia, astrocytes, and microvascular endothelial cells in the brain (26,27). Cell surface GAGs, on the other hand, have been reported to concentrate MCP1 locally, promote MCP1 oligomerization, and thus facilitate the binding of MCP1 to CCR2 (28 -31). Whether MCP1 functions as a monomer or homodimer, however, is still under debate. Although it is believed that MCP1 exerts its function as a homodimer (25,32), it has also been suggested that MCP1 can bind to CCR2 and induce downstream signaling as a monomer (33,34). It should be noted, however, that these experiments were conducted using human MCP1, not rodent MCP1, which contains a heavily glycosylated C-terminal extension.Previous studies in our laboratory have shown that 1) the highly glycosylated C-terminal extension of mouse MCP1 is removed by plasmin, the active protease of plasminogen,...

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“…Lower molecular weight bands in the 50-to 70-kD range were also observed; however, these were unaffected by 5-HT. Prominent protein binding in the 220-240-kD range was blocked by the TGase inhibitor, dansylcadaverin (DSC), which binds to the enzyme active site of TGase and inactivates the transmidation activity (29)(30)(31). Figure 2B shows that the formation of the 220-to 240-kD TGase-modified protein was significantly reduced in the presence of the calcium chelator, EGTA, demonstrating that it is Ca 21 dependent.…”

Section: -Ht Induces Transglutamidation Of Proteins In Bovine Pulmonmentioning

confidence: 99%

Role of Protein Transamidation in Serotonin-Induced Proliferation and Migration of Pulmonary Artery Smooth Muscle Cells

Liu

Lin²,

Laskin³

et al. 2011

Am J Respir Cell Mol Biol

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Pulmonary hypertension is characterized by elevated pulmonary artery pressure and pulmonary artery smooth muscle cell (SMC) proliferation and migration. Clinical and experimental evidence suggests that serotonin (5-HT ) is important in these responses. We previously demonstrated the participation of the 5-HT transporter and intracellular 5-HT (5-HTi) in the pulmonary vascular SMCproliferative response to 5-HT. However, the mechanism underlying the intracellular actions of 5-HT is unknown. We speculated that 5-HTi activates SMC growth by post-translational transamidation of proteins via transglutaminase (TGase) activity, a process referred to as serotonylation. To test this hypothesis, serotonylation of pulmonary artery SMC proteins, and their role in 5-HT-induced proliferative and migratory responses, were assessed. 5-HT caused dose-and time-dependent increase in serotonylation of multiple proteins in both bovine and rat pulmonary artery SMCs. Inhibition of TGase with dansylcadaverin blocked this activity, as well as SMCproliferative and migratory responses to 5-HT. Serotonylation of proteins also was blocked by 5-HT transporter inhibitors, and was enhanced by inhibition of monoamine oxidase, an enzyme known to degrade 5-HTi, indicating that 5-HTi levels regulate serotonylation. Immunoprecipitation assays and HPLC-mass spectral peptide sequencing revealed that a major protein serotonylated by TGase was fibronectin (FN). 5-HT-stimulated SMC serotonylation and proliferation were blocked by FN small interfering (si) RNA. These findings, together with previous observations that FN expression in the lung strongly correlates with the progression of pulmonary hypertension in both experimental animals and humans, suggest an important role of FN serotonylation in the pathogenesis of this disease.Keywords: serotonin; transglutaminase; fibronectin; protein serotonylation; smooth muscle cell growth Serotonin (also known as 5-hydroxytryptamine ) is one of the most potent naturally occurring pulmonary vasoconstrictors (1). Clinical, experimental, and human genetic data support a relationship between 5-HT, pulmonary artery remodeling, and pulmonary hypertension. Our laboratories and others have demonstrated the importance of both the 5-HT transporter (5-HTT) and 5-HT receptors in pulmonary vascular smooth muscle cell (SMC)-proliferative and migratory responses to 5-HT (2-7). We also have shown that 5-HT transport via the 5-HTT triggers activation of platelet-derived growth factor receptor-b and mitogen-activated protein kinase, which participate in proliferation of pulmonary artery SMCs (2, 8). Furthermore, inhibition of intracellular monoamine oxidase (MAO), which degrades 5-HT, markedly enhances 5-HT-induced proliferation of SMCs (9-11). These data indicate that intracellular 5-HT (5-HTi) is an important signal for SMC proliferation; however, the mechanism underlying this activity is unknown.Transglutaminases (TGases), which are abundant in blood and vascular SMCs (12, 13), catalyze post-translational modifications of protei...

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Dansyl cadaverine regulates ligand induced endocytosis of interleukin‐8 receptor in human polymorphonuclear neutrophils

Cited by 34 publications

References 24 publications

Inhibition of Receptor Internalization by Monodansylcadaverine Selectively Blocks p55 Tumor Necrosis Factor Receptor Death Domain Signaling

Inhibition of Receptor Internalization by Monodansylcadaverine Selectively Blocks p55 Tumor Necrosis Factor Receptor Death Domain Signaling

The C Terminus of Mouse Monocyte Chemoattractant Protein 1 (MCP1) Mediates MCP1 Dimerization while Blocking Its Chemotactic Potency

Role of Protein Transamidation in Serotonin-Induced Proliferation and Migration of Pulmonary Artery Smooth Muscle Cells

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