Výsledky vyhledávání - "M. L. Standaert"

Glucose activates protein kinase C-zeta /lambda through proline-rich tyrosine kinase-2, extracellular signal-regulated kinase, and phospholipase D: a novel mechanism for activating glucose transporter translocation

Autor: G, Bandyopadhyay, M P, Sajan, Y, Kanoh, M L, Standaert, M J, Quon, B C, Reed, I, Dikic, R V, Farese

Publikováno v: The Journal of biological chemistry. 276(38)

Insulin controls glucose uptake by translocating GLUT4 and other glucose transporters to the plasma membrane in muscle and adipose tissues by a mechanism that appears to require protein kinase C (PKC)-zeta/lambda operating downstream of phosphatidyli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::47e1893bd9c546c253c83b462b1a0423
https://pubmed.ncbi.nlm.nih.gov/11463795

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Effects of adenoviral gene transfer of wild-type, constitutively active, and kinase-defective protein kinase C-lambda on insulin-stimulated glucose transport in L6 myotubes

Autor: G, Bandyopadhyay, Y, Kanoh, M P, Sajan, M L, Standaert, R V, Farese

Publikováno v: Endocrinology. 141(11)

We used adenoviral gene transfer methods to evaluate the role of atypical protein kinase Cs (PKCs) during insulin stimulation of glucose transport in L6 myotubes. Expression of wild-type PKC-lambda potentiated maximal and half-maximal effects of insu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::308e582d8933cdf2ced614f0b2e1278b
https://pubmed.ncbi.nlm.nih.gov/11089544

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Effects of knockout of the protein kinase C beta gene on glucose transport and glucose homeostasis

Autor: M L, Standaert, G, Bandyopadhyay, L, Galloway, J, Soto, Y, Ono, U, Kikkawa, R V, Farese, M, Leitges

Publikováno v: Endocrinology. 140(10)

The beta-isoform of protein kinase C (PKC) has paradoxically been suggested to be important for both insulin action and insulin resistance as well as for contributing to the pathogenesis of diabetic complications. Presently, we evaluated the effects

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::83788387e389f9771a02f86252bd9f43
https://pubmed.ncbi.nlm.nih.gov/10499500

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Okadaic acid activates atypical protein kinase C (zeta/lambda) in rat and 3T3/L1 adipocytes. An apparent requirement for activation of Glut4 translocation and glucose transport

Autor: M L, Standaert, G, Bandyopadhyay, M P, Sajan, L, Cong, M J, Quon, R V, Farese

Publikováno v: The Journal of biological chemistry. 274(20)

Okadaic acid, an inhibitor of protein phosphatases 1 and 2A, is known to provoke insulin-like effects on GLUT4 translocation and glucose transport, but the underlying mechanism is obscure. Presently, we found in both rat adipocytes and 3T3/L1 adipocy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2d05403f3c97fe0cf03a4922c2cafd44
https://pubmed.ncbi.nlm.nih.gov/10318822

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Effects of transiently expressed atypical (zeta, lambda), conventional (alpha, beta) and novel (delta, epsilon) protein kinase C isoforms on insulin-stimulated translocation of epitope-tagged GLUT4 glucose transporters in rat adipocytes: specific interchangeable effects of protein kinases C-zeta and C-lambda

Autor: G, Bandyopadhyay, M L, Standaert, U, Kikkawa, Y, Ono, J, Moscat, R V, Farese

Publikováno v: The Biochemical journal. 337

Atypical protein kinase (PK)C isoforms, zeta and lambda, have been reported to be activated by insulin via phosphoinositide 3-kinase, and have been suggested to be required for insulin-stimulated glucose transport. Here, we have examined the effects

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5759fb8fd0f4f4d2a6ea428b5c09e08a
https://pubmed.ncbi.nlm.nih.gov/9895289

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Protein kinase C-zeta as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport

Autor: M L, Standaert, L, Galloway, P, Karnam, G, Bandyopadhyay, J, Moscat, R V, Farese

Publikováno v: The Journal of biological chemistry. 272(48)

Insulin provoked rapid increases in enzyme activity of immunoprecipitable protein kinase C-zeta (PKC-zeta) in rat adipocytes. Concomitantly, insulin provoked increases in 32P labeling of PKC-zeta both in intact adipocytes and during in vitro assay of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8ec598a904f0e4c63987df63ae9d886c
https://pubmed.ncbi.nlm.nih.gov/9374484

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Activation and translocation of Rho (and ADP ribosylation factor) by insulin in rat adipocytes. Apparent involvement of phosphatidylinositol 3-kinase

Autor: P, Karnam, M L, Standaert, L, Galloway, R V, Farese

Publikováno v: The Journal of biological chemistry. 272(10)

Insulin reportedly (Standaert, M. L., Avignon, A., Yamada, K., Bandyopadhyay, G., and Farese, R. V. (1996) Biochem. J. 313, 1039-1046) activates phospholipase D (PLD)-dependent hydrolysis of phosphatidylcholine (PC) in plasma membranes of rat adipocy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::642a55d94c5d6c5662c9e91de0a18a3d
https://pubmed.ncbi.nlm.nih.gov/9045624

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Activation of protein kinase C (alpha, beta, and zeta) by insulin in 3T3/L1 cells. Transfection studies suggest a role for PKC-zeta in glucose transport

Autor: G, Bandyopadhyay, M L, Standaert, L, Zhao, B, Yu, A, Avignon, L, Galloway, P, Karnam, J, Moscat, R V, Farese

Publikováno v: The Journal of biological chemistry. 272(4)

We presently studied (a) insulin effects on protein kinase C (PKC) and (b) effects of transfection-induced, stable expression of PKC isoforms on glucose transport in 3T3/L1 cells. In both fibroblasts and adipocytes, insulin provoked increases in memb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::832c22af10b513c8493e9fd3545c84a5
https://pubmed.ncbi.nlm.nih.gov/8999972

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Insulin translocates PKC-epsilon and phorbol esters induce and persistently translocate PKC-beta 2 in BC3H-1 myocytes

Autor: M L, Standaert, A, Avignon, T, Arnold, S I, Saba-Siddique, D R, Copper, J, Watson, X, Zhou, L, Galloway, R V, Farese

Publikováno v: Cellular signalling. 8(4)

Initial studies suggested that insulin increases diacylglycerol and activates protein kinase C (PKC) in BC3H-1 myocytes. In these earlier studies, insulin was found to translocate PKC-beta, but the presence of PKC-epsilon was not appreciated. More re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::69b80f7da9c6e58e8dc4c7a7d3aba8a5
https://pubmed.ncbi.nlm.nih.gov/8842533

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Insulin increases mRNA levels of protein kinase C-alpha and -beta in rat adipocytes and protein kinase C-alpha, -beta and -theta in rat skeletal muscle

Autor: A, Avignon, M L, Standaert, K, Yamada, H, Mischak, B, Spencer, R V, Farese

Publikováno v: The Biochemical journal. 308

Effects of insulin of levels of mRNA encoding protein kinase C (PKC)-alpha, PKC-beta, PKC-epsilon and PKC-theta were examined by ribonuclease protection assay in primary cultures of rat adipocytes in vitro, and in rat adipose tissue and gastrocnemius

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::200073ef7562026b74f95fa75dc151bb
https://pubmed.ncbi.nlm.nih.gov/7755564

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