p38 Mitogen-activated protein kinase inhibition attenuates intercellular adhesion molecule–1 up-regulation on human pulmonary microvascular endothelial cells

Tamura, Douglas Y.; Moore, Ernest E.; Johnson, Jeffrey L.; Zallen, Garret; Aiboshi, Junichi; Silliman, Christopher C.

doi:10.1016/s0039-6060(98)70147-3

Cited by 85 publications

(52 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…*p < 0.001 compared to the respective control, #p < 0.001 compared to the cells treated with high insulin alone A B A B C ated by high insulin were attenuated by pretreatment with a MAP kinase inhibitor, PD98 059 but not a PI 3-kinase inhibitor, wortmannin. These results are consistent with a previous report [10], showing that MAP kinase activation is integral to the increase in endothelial ICAM-1.…”

Section: Discussionsupporting

confidence: 94%

High insulin exacerbates neutrophil-endothelial cell adhesion through endothelial surface expression of intercellular adhesion molecule-1 via activation of protein kinase C and mitogen-activated protein kinase

et al. 2002

View full text Add to dashboard Cite

The risk of cardiovascular diseases in diabetic patients and even in those with IGT are associated with insulin resistance, two-to threefold higher than that in control subjects [1]. The United Kingdom Prospective Diabetes Study (UKPDS) and other similar studies indicated that intensive control of blood glucose in diabetic patients prevents and slows the progression of microvascular complications, but has little effect on the prevention of macrovascular complications i. e. acute myocardial infarction (AMI) [2]. Excessive macrovascular diseases in diabetes have thus been considered to be due to insulin resistance and/or hyperinsulinaemia.A recent study has shown that vascular inflammation with atherosclerosis is responsible for the onset of AMI [3]. Adhesion of leukocytes to the endothelium, which is regulated by several endothelial adhesion molecules such as intercellular adhesion molecule-1 (ICAM-1), E-selectin and P-selectin, is the first and crucial step in both atherosclerosis and vascular inflammation. Whereas endothelial dysfunction induced by insulin resistance and/or hyperinsulin- AbstractAims/hypothesis. The association of insulin resistance and compensatory hyperinsulinaemia with increased coronary events in diabetic patients is poorly understood. There are few publications about the direct atherogenic actions of insulin on the endothelium compared with those on vascular smooth muscle cells. The aim of this study was to elucidate whether high insulin directly affects neutrophil-endothelial cell adhesion and surface expression of endothelial adhesion molecules. We also examined what intracellular mechanisms are involved in these events. Methods. Studies of adhesion between neutrophils from healthy volunteers and human umbilical vein endothelial cells incubated in insulin-rich medium were carried out. Adhered neutrophils were quantified by measuring their myeloperoxidase activities and surface expression of endothelial adhesion molecules was examined using an enzyme immunoassay. Results. High insulin enhanced neutrophil-endothelial cell adhesion with an increase in the expression of intercellular adhesion molecule-1 but not E-selectin or P-selectin. Both phenomena were attenuated by pretreatment with protein kinase C inhibitors and a mitogen activated protein kinase inhibitor. Conclusions/interpretation. These results suggest that hyperinsulinaemia causes vascular injury by directly exacerbating neutrophil-endothelial cell adhesion through increasing endothelial expression of intercellular adhesion molecule-1 via activation of protein kinase and mitogen activated protein kinase pathways. [Diabetologia (2002) 45:556±559]

show abstract

Section: Discussionsupporting

confidence: 94%

High insulin exacerbates neutrophil-endothelial cell adhesion through endothelial surface expression of intercellular adhesion molecule-1 via activation of protein kinase C and mitogen-activated protein kinase

et al. 2002

View full text Add to dashboard Cite

show abstract

“…Evidence demonstrates that both a Rac-1 (3) and a p38 MAP kinase dependent pathway (51) are activated after LPS or LTA interactions with TLRs. Endothelial cell secretion of IL-8 in response to LPS is dependent upon both pathways (29), which is consistent with other studies that have shown a key role for p38 MAP kinase in endothelial cells responses to E. coli LPS (27,41,52,59). However, LPSs obtained from different bacterial species have significant variations in their abilities to activate host cells (5,9,16,22,40,57), and it is not known if this correlates to their ability to activate p38 MAP kinase.…”

Section: Fig 4 Inhibition Of P38 Map Kinase Phosphorylation By P Gsupporting

confidence: 91%

“…This superfamily includes the extracellular signal response kinases (ERKs), c-jun N-terminal kinases, and the p38 family of kinases. Although LPS facilitates the activation of all three of these MAP kinases, numerous studies employing p38 MAP kinase-specific inhibitors have provided good evidence that many cellular responses to LPS require p38 activation (1,2,11,41), consistent with a primary role for p38 activation in response to LPS (12,26,27,29,59). In this study the p38 MAP kinase response to P. gingivalis LPS was examined.…”

mentioning

confidence: 83%

Porphyromonas gingivalisLipopolysaccharide Is Both Agonist and Antagonist for p38 Mitogen-Activated Protein Kinase Activation

Darveau¹,

Arbabi

Garcia

et al. 2002

Infect Immun

View full text Add to dashboard Cite

Lipopolysaccharide (LPS) is a key inflammatory mediator. It has been proposed to function as an important molecule that alerts the host of potential bacterial infection. Although highly conserved, LPS contains important structural differences among different bacterial species that can significantly alter host responses. For example, LPS obtained from Porphyromonas gingivalis, an etiologic agent for periodontitis, evokes a highly unusual host cell response. Human monocytes respond to this LPS by the secretion of a variety of different inflammatory mediators, while endothelial cells do not. In addition, P. gingivalis LPS inhibits endothelial cell expression of E-selectin and interleukin 8 (IL-8) induced by other bacteria. In this report the ability of P. gingivalis LPS to activate p38 mitogen-activated protein (MAP) kinase was investigated. It was found that p38 MAP kinase activation occurred in response to P. gingivalis LPS in human monocytes. In contrast, no p38 MAP kinase activation was observed in response to P. gingivalis LPS in human endothelial cells or CHO cells transfected with human Toll-like receptor 4 (TLR-4). In addition, P. gingivalis LPS was an effective inhibitor of Escherichia coli-induced p38 MAP kinase phosphorylation in both endothelial cells and CHO cells transfected with human TLR-4. These data demonstrate that P. gingivalis LPS activates the LPS-associated p38 MAP kinase in monocytes and that it can be an antagonist for E. coli LPS activation of p38 MAP kinase in endothelial and CHO cells. These data also suggest that although LPS is generally considered a bacterial component that alerts the host to infection, LPS from P. gingivalis may selectively modify the host response as a means to facilitate colonization.The innate host defense system protects mammalian hosts against microbial infection through an orchestrated response to the presence of nonself components (31, 32). Lipopolysaccharide (LPS), a component of the gram-negative bacterial cell wall, is a key structure recognized by a variety of different innate host defense proteins, allowing the host to "sense" a potential bacterial infection (8,62). LPS is evolutionarily an ideal target, since it is a conserved structure found on a wide variety of pathogenic bacteria and is sufficiently different from host components to allow a safe selective response (38). However, there are important structural differences in LPS composition between different bacterial species, such as fatty acid acyl chain composition and charge, which can significantly affect the host response (33,36,42,49,64). Different binding affinities for LPS binding protein and CD14 may only partly explain the lowered inflammatory response to some LPS species that has been observed (14), consistent with the notion that the major role of LPS binding protein and CD14 is to concentrate LPS at host cell surfaces (65). Recently it has been demonstrated that cell surface Toll-like receptor (TLR) proteins participate in the ability of the host to discriminate different LPS structural f...

show abstract

“…Until present, it is reported that p38 cascade participates in the production of TNFa and IL-1 in monocyte [20]. JNK and p38 cascade participate in the control of IL-3 mRNA [21], and p38 cascade also participates in the induction of VCAM-1 expression by TNFa at human umbilical vein endothelial cells [11] and in the ICAM-1 expression of human pulmonary microvascular endothelial cells [10]. Also, there was a report that protein tyrosine kinase participates in the adhesion molecule expression of human umbilical vein endothelial cells by TNFa and IL-1a [22], but there have not been any reports on the signal transduction pathway of HDMEC ICAM-1 expression on HDMEC which is induced by AECA.…”

Section: Discussionmentioning

confidence: 99%

“…There are at least three subtypes of MAPK cascades, including extracellular signal regulated kinase (ERK)1/2, c-Jun NH2 terminal kinase (JNK), and p38 cascades, and they regulate various cellular processes such as cell growth, differentiation, inflammation and apoptosis. There are several papers reporting that p38 pathway contributes to TNFa stimulated ICAM-1 expression on human pulmonary microvascular endothelial cells [10] and tumor necrosis factor a (TNFa) stimulated VCAM-1 expression on human umbilical vein endothelial cells [11], but the signal transduction pathway of ICAM-1 expression on HDMEC stimulated with IgM-AECA has never been reported. We examined the involvement of MAPK in ICAM-1 expression on HDMEC and the production of TNFa or interleukin-1a (IL-1a) in HDMEC after stimulation with IgM-AECA.…”

Section: Introductionmentioning

confidence: 99%

Activation of extracellular signal regulated kinase 1/2 in human dermal microvascular endothelial cells stimulated by anti-endothelial cell antibodies in sera of patients with Behçet's disease

Lee

Cho

Kim

et al. 2002

Journal of Dermatological Science

View full text Add to dashboard Cite

p38 Mitogen-activated protein kinase inhibition attenuates intercellular adhesion molecule–1 up-regulation on human pulmonary microvascular endothelial cells

Cited by 85 publications

References 22 publications

High insulin exacerbates neutrophil-endothelial cell adhesion through endothelial surface expression of intercellular adhesion molecule-1 via activation of protein kinase C and mitogen-activated protein kinase

High insulin exacerbates neutrophil-endothelial cell adhesion through endothelial surface expression of intercellular adhesion molecule-1 via activation of protein kinase C and mitogen-activated protein kinase

Porphyromonas gingivalisLipopolysaccharide Is Both Agonist and Antagonist for p38 Mitogen-Activated Protein Kinase Activation

Activation of extracellular signal regulated kinase 1/2 in human dermal microvascular endothelial cells stimulated by anti-endothelial cell antibodies in sera of patients with Behçet's disease

Contact Info

Product

Resources

About