The stimulation by thrombin of glucose oxidation in human platelets.

Warshaw, Andrew L.; Laster, Leonard; Shulman, N. Raphael

doi:10.1172/jci105497

Cited by 88 publications

(38 citation statements)

References 24 publications

(32 reference statements)

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“…The capacity of platelets to oxidize long-chain fatty acids and glucose, as is shown in Fig. 1, is in accord with the observations of other investigators (16)(17)(18)(19)(20).…”

Section: Resultssupporting

confidence: 92%

See 1 more Smart Citation

Energy substrate metabolism in fresh and stored human platelets

Cohen¹,

Wittels²

1970

J. Clin. Invest.

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A B S T R A C T The latent capacity of human platelets for oxidizing several important energy-yielding substrates has been revealed by hypoosmolaric incubation conditions.The data show that the human platelet has a considerable capacity to oxidize both glucose and long-chain fatty acids. Long-chain fatty acids appear to rank favorably with glucose as a potential energy substrate. In a number of mammalian tissues, (-)-carnitine serves to regulate the rate at which long-chain fatty acids are oxidized. Evidence was obtained which suggests that (-)-carnitine functions in a similar role in the platelet.After storage of human platelets at 4VC for 24 hr, the oxidative capacity for glucose was reduced by approximately 25% and for long-chain fatty acids by almost 50%. Investigation of the component parts of the metabolic pathways indicated that a marked decrease in the capacity of the Krebs cycle could be responsible for the decrement in energy substrate oxidation. INTRODUCTIONHuman platelets are readily obtainable in large quantities as suspensions of intact, discrete cells. As such, they are eminently suitable models with which to study the control that permeability of the outer cell membrane exerts on mitochondrial function. Obviously, mitochondria which do not "see" substrates cannot utilize them. Likewise, an enormous reserve capacity of mitochondria for energy substrate utilization may only be revealed if the outer membrane and then the mitochondrial membrane are altered so as to admit larger-than-usual

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“…The capacity of platelets to oxidize long-chain fatty acids and glucose, as is shown in Fig. 1, is in accord with the observations of other investigators (16)(17)(18)(19)(20).…”

Section: Resultssupporting

confidence: 92%

“…The major potential energy-yielding substrates utilized by human platelets appear to be glucose and long-chain fatty acids (16)(17)(18)(19)(20). In most tissues, the rate of usage of these substrates is subject to some form of regulatory control (35).…”

Section: Resultsmentioning

confidence: 99%

Energy substrate metabolism in fresh and stored human platelets

Cohen¹,

Wittels²

1970

J. Clin. Invest.

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“…[69][70][71] Notably, platelets stored in blood banks increase synthesis of integrin-␤3. 72 Work from the Provost laboratory has demonstrated that human platelets also contain miRNA processing machinery, including Dicer, TAR RNA-binding protein 2, and Ago2, and that platelets are able to process pre-miRNA into mature miRNA.…”

Section: Platelet Mirnasmentioning

confidence: 99%

MicroRNAs in platelet production and activation

Edelstein

Bray

2011

Blood

121

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“…Although thrombin stimulates a variety of metabolic changes in platelets (13)(14)(15)(16), these reactions occur in response to most agonists that stimulate the release reaction. One reason for the paucity of information on the sequence of events that takes place after thrombin binding is the rapidity with which secretion occurs.…”

Section: Introductionmentioning

confidence: 99%

Thrombin-Induced Platelet Secretion

Shuman¹,

Botney²,

Fenton³

1979

J. Clin. Invest.

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A B S T R A C T We have studied the interaction between thrombin and washed, human platelets using prostacyclin, a reversible inhibitor ofplatelet secretion. The effect of thrombin is limited to those reactions that are not inhibited by an increased concentration ofplatelet cyclic adenosine 3',5'-monophosphate, because prostacyclin is a potent inducer of the latter. Prostacyclin-treated platelets were briefly (15-30 s) exposed to low concentrations of human thrombin (0.01-0.2 U/ml). After removal of the prostacyclin and thrombin, the platelets were incubated with fresh thrombin. Although they had not undergone the release reaction after the first thrombin incubation, these platelets had a diminished capacity to secrete [3H]serotonin when exposed to thrombin the second time. Refractoriness was concentration dependent: the higher the initial thrombin concentration, the greater the degree of inhibition of serotonin secretion on subsequent thrombin exposure. Inhibition was closely related to the ability of thrombin to induce platelet secretion and not to its esterase or fibrinogen clotting activity. Diisopropyl fluorophosphate-inactive thrombin did not induce refractoriness. Refractoriness to thrombin did not increase when the time of the initial incubation with thrombin was lengthened, nor was it reversible.Inhibition was thrombin specific: serotonin secretion induced by collagen, wheat germ agglutinin, and the ionophore A23187 was minimally affected. For an equivalent amount of thrombin bound, a decrease was observed in serotonin secretion by thrombin-pretreated platelets compared to control platelets. Thus, there is at least one step in the secretory pathway between thrombin binding and regulation of adenylate cyclase. This step appears to transmit the signal that leads to extrusion of intracellular granular contents.A preliminary report of this work was presented at the Annual Meeting of the American Federation for Clinical Research, San Francisco, Calif., 1978, and was published in abstract form in Clin. Res. 26: 357A. (Abstr.)

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The stimulation by thrombin of glucose oxidation in human platelets.

Cited by 88 publications

References 24 publications

Energy substrate metabolism in fresh and stored human platelets

Energy substrate metabolism in fresh and stored human platelets

MicroRNAs in platelet production and activation

Thrombin-Induced Platelet Secretion

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