Increasing neutrophil F‐actin corrects CD11b exposure in Type 2 diabetes

Advani, Andrew; Marshall, SM; Thomas, T.H.

doi:10.1111/j.1365-2362.2004.01346.x

Cited by 14 publications

(10 citation statements)

References 50 publications

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“…In this study, it was determined that WP supplementation reversed chemokine-mediated actin polymerization impairment in both B and T cells in diabetic mice. Similar observations have been made by [23], who observed actin polymerization impairment in type 2 diabetes. To our knowledge, we show for the first time that WP increased chemokine-mediated actin polymerization in these lymphocytes.…”

Section: Discussionsupporting

confidence: 90%

Effects of undenatured whey protein supplementation on CXCL12- and CCL21-mediated B and T cell chemotaxis in diabetic mice

2011

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BackgroundLong and persistent uncontrolled diabetes tends to degenerate the immune system and leads to an increased incidence of infection. Whey proteins (WPs) enhance immunity during early life and have a protective role in some immune disorders. In this study, the effects of camel WP on the chemotaxis of B and T cells to CXCL12 and CCL21 in diabetic mice were investigated.ResultsFlow cytometric analysis of the surface expressions of CXCR4 (CXCL12 receptor) and CCR7 (CCL21 receptor) on B and T cells revealed that the surface expressions of CXCR4 and CCR7 were not significantly altered in diabetic and WP-supplemented diabetic mice compared with control mice. Nevertheless, B and T lymphocytes from diabetic mice were found to be in a stunned state, with a marked and significant (P < 0.05) decrease in CXCL12- and CCL21-mediated actin polymerization and subsequently, a marked decrease in their chemotaxis. WP supplementation in the diabetes model was found to significantly increase CXCL12- and CCL21-mediated actin polymerization and chemotaxis in both B and T cells.ConclusionOur data revealed the benefits of WP supplementation in enhancing cytoskeletal rearrangement and chemotaxis in B and T cells, and subsequently improving the immune response in diabetic mice.

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Section: Discussionsupporting

confidence: 90%

Effects of undenatured whey protein supplementation on CXCL12- and CCL21-mediated B and T cell chemotaxis in diabetic mice

2011

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“…Several studies (1,2,9,49) provide clinical evidence that membrane and cytoskeletal defects occur in the prediabetic and diabetic states. As a deeper understanding of the role of membrane and cytoskeletal structure in insulin action emerges, studies to evaluate their involvement in the molecular pathogenesis of insulin resistance are providing considerable insight into this syndrome.…”

Section: Discussionmentioning

confidence: 99%

“…Although it has been hypothesized that defective insulin signaling through IR, IRS-1, phosphatidylinositol 3-kinase, and Akt contributes to the progression of type 2 diabetes, an important and unresolved issue is that chronic exposure to lower, relevant doses of insulin (0.5-5 nM) also impairs insulin sensitivity without manifesting any obvious signal transduction abnormalities (11,28,30,37). Interestingly, blood cells (neutrophils, mononuclear cells, erythrocytes) isolated from insulin-resistant individuals exhibit alterations in cortical actin structure and membrane lipid composition (1,2,9,49). Since a role for actin in insulin-stimulated GLUT4 translocation has been implicated by several studies, these observations suggest that hyperinsulinemia-induced insulin resistance may be a consequence of actin abnormalities.…”

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confidence: 98%

Loss of cortical actin filaments in insulin-resistant skeletal muscle cells impairs GLUT4 vesicle trafficking and glucose transport

McCarthy¹,

Spisak²,

Brozinick³

et al. 2006

American Journal of Physiology-Cell Physiology

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Study has demonstrated an essential role of cortical filamentous actin (F-actin) in insulin-regulated glucose uptake by skeletal muscle. Here, we tested whether perturbations in F-actin contributed to impaired insulin responsiveness provoked by hyperinsulinemia. In L6 myotubes stably expressing GLUT4 that carries an exofacial myc-epitope tag, acute insulin stimulation (20 min, 100 nM) increased GLUT4myc translocation and glucose uptake by approximately 2-fold. In contrast, a hyperinsulinemic state, induced by inclusion of 5 nM insulin in the medium for 12 h decreased the ability of insulin to stimulate these processes. Defects in insulin signaling did not readily account for the observed disruption. In contrast, hyperinsulinemia reduced cortical F-actin. This occurred concomitant with a loss of plasma membrane phosphatidylinositol 4,5-bisphosphate (PIP(2)), a lipid involved in cytoskeletal regulation. Restoration of plasma membrane PIP(2) in hyperinsulinemic cells restored F-actin and insulin responsiveness. Consistent with these in vitro observations suggesting that the hyperinsulinemic state negatively affects cortical F-actin structure, epitrochlearis skeletal muscle from insulin-resistant hyperinsulinemic Zucker fatty rats displayed a similar loss of F-actin structure compared with that in muscle from lean insulin-sensitive littermates. We propose that a component of insulin-induced insulin resistance in skeletal muscle involves defects in PIP(2)/F-actin structure essential for insulin-regulated glucose transport.

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“…Accumulating in vitro and in vivo evidence highlights that membrane and cytoskeletal abnormalities may render the control of GLUT4 ineffective. Interestingly, blood cells (neutrophils, mononuclear cells, erythrocytes) isolated from insulin-resistant individuals exhibit alterations in cortical actin structure and membrane lipid composition [1][2][3][4]. These phospholipid and cytoskeletal irregularities in human blood cells raise the question whether similar changes are present in human muscle and fat cells and explain, at least in part, their insulin-resistant state.…”

Section: Introductionmentioning

confidence: 96%

“Actin”g on GLUT4: Membrane & Cytoskeletal Components of Insulin Action

Brozinick¹,

Berkemeier²,

Elmendorf

2007

CDR

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The dissection of mechanisms that regulate glucose transport by insulin has revealed an intricate network of signaling molecules scattered from the insulin receptor to the intracellular glucose transporter GLUT4. It is also appreciated that some insulin receptor signals jaunt in different directions to regulate events essential for the efficient redistribution of GLUT4 to the plasma membrane. Moreover key assists in the process appear to be arranged by membrane lipids and cytoskeletal proteins. Following current considerations of insulin signals regulating GLUT4, this review will focus on in vitro and in vivo evidence that supports an essential role for phosphoinositides and actin filaments in the control of glucose transport. The discussion will visit recent cell culture, whole animal, and human data highlighting membrane and cytoskeletal aspects of insulin resistance.

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Increasing neutrophil F‐actin corrects CD11b exposure in Type 2 diabetes

Cited by 14 publications

References 50 publications

Effects of undenatured whey protein supplementation on CXCL12- and CCL21-mediated B and T cell chemotaxis in diabetic mice

Effects of undenatured whey protein supplementation on CXCL12- and CCL21-mediated B and T cell chemotaxis in diabetic mice

Loss of cortical actin filaments in insulin-resistant skeletal muscle cells impairs GLUT4 vesicle trafficking and glucose transport

“Actin”g on GLUT4: Membrane & Cytoskeletal Components of Insulin Action

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Increasing neutrophil F‐actin corrects CD11b exposure in Type 2 diabetes

Cited by 14 publications

References 50 publications

Effects of undenatured whey protein supplementation on CXCL12- and CCL21-mediated B and T cell chemotaxis in diabetic mice

Effects of undenatured whey protein supplementation on CXCL12- and CCL21-mediated B and T cell chemotaxis in diabetic mice

Loss of cortical actin filaments in insulin-resistant skeletal muscle cells impairs GLUT4 vesicle trafficking and glucose transport

&#x201C;Actin&#x201D;g on GLUT4: Membrane & Cytoskeletal Components of Insulin Action

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“Actin”g on GLUT4: Membrane & Cytoskeletal Components of Insulin Action