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Rensen, A. J. M. L. Van; Taams, Leonie S.; Grosfeld-Stulemeyer, M. C.; Eden, Willem van; Crommelin, Daan J.A.; Wauben, Marca H. M.

doi:10.1023/a:1007586400631

Cited by 9 publications

(1 citation statement)

References 27 publications

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“…It is well known that electron transfer at PS II can be stimulated by bicarbonate [19], which binds to several sites in PS II (e.g. non-heme iron complex, Q B binding site, water-oxidizing complex) [20]. In contrast, carboxylate anions (^COO 3 ) including formate (HCOO 3 ) can slow the rate of electron trans- fer because these anions can replace bound bicarbonate at these binding sites [19].…”

Section: Discussionmentioning

confidence: 99%

Reversible inhibition of photophosphorylation in chloroplasts by nitric oxide

Takahashi¹,

Yamasaki²

2002

FEBS Letters

113

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Nitric oxide (NO) is a bioactive molecule involved in diverse physiological functions in plants. Here we demonstrate that NO is capable of regulating the activity of photophosphorylation in chloroplasts. The electron transport activity in photosystem II determined from chlorophyll a fluorescence was inhibited by NO. NO also inhibited light-induced v vpH formation across the thylakoid membrane. High concentrations of nitrite and nitrate did not show such inhibitory effects, suggesting that the inhibition is not due to uncoupling effects of the oxidized products of NO. ATP synthesis activity upon illumination was severely inhibited by NO (IC 50 = 0.7 W WM). The inhibition was found to be temporary and the activity was completely recovered by removing NO. Bovine hemoglobin and bicarbonate were effective in preventing NO-dependent inhibition of photophosphorylation. These results indicate that NO is a reversible inhibitor of photosynthetic ATP synthesis. ß

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Section: Discussionmentioning

confidence: 99%

Reversible inhibition of photophosphorylation in chloroplasts by nitric oxide

Takahashi¹,

Yamasaki²

2002

FEBS Letters

113

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Uptake of membrane molecules from T cells endows antigen‐presenting cells with novel functional properties

et al. 2004

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Although intercellular transfer of cell surface molecules has been observed between several cells of the immune system, the physiological relevance of this phenomenon remained obscure. Until now the transfer of molecules between antigen-presenting cells (APC) and T cells has been described as a unidirectional process from APC to T cells. However, here we show that T cells in turn donate molecules to APC, and that T cell-derived vesicles can mediate this transfer. The transferred proteins are incorporated into the APC as active molecules. Our data provide evidence that T cells use intercellular molecule transfer to mediate cell contact-dependent regulation of T cell responses via modulation of the APC.

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