The α1-adrenergic receptor in human erythrocyte membranes mediates interaction in vitro of epinephrine and thyroid hormone at the membrane Ca2+-ATPase

Sundquist, Janet; Blas, Susan D.; Hogan, James E.; Davis, Faith B.; Davis, Paul J.

doi:10.1016/0898-6568(92)90060-l

Cited by 23 publications

(15 citation statements)

References 27 publications

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“…Moreover, to facilitate these regulatory tasks, the erythrocyte is equipped with a plethora of signalling enzymes and second messengers that respond to stimuli as rapidly as their counterparts in other cells [34]. Although erythrocyte signalling components have been shown to be activated by such stimuli as insulin [35], prostaglandins [36], epinephrine [37], NO [38], platelet releasates [39], hypertensive agents [40], ADP [41] and H 2 O 2 [42], it is perhaps not surprising that one of the most prominent signalling molecules to modulate red cell biology is O 2 , the cell’s most important cargo.…”

Section: Discussionmentioning

confidence: 99%

Oxygen regulates the band 3–ankyrin bridge in the human erythrocyte membrane

Stefanovic

Puchulu-Campanella

Kodippili

et al. 2012

Biochemical Journal

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The oxygenation state of erythrocytes is known to impact several cellular processes. As the only known O2-binding protein in red blood cells, haemoglobin has been implicated in the oxygenation-mediated control of cell pathways and properties. Band 3, an integral membrane protein linked to the spectrin/actin cytoskeleton, preferentially binds deoxygenated haemoglobin at its N-terminus, and has been postulated to participate in the mechanism by which oxygenation controls cellular processes. Because the ankyrin-binding site on band 3 is located near the deoxyHb (deoxygenated haemoglobin)-binding site, we hypothesized that deoxyHb might impact the association between band 3 and the underlying erythrocyte cytoskeleton, a link that is primarily established through band 3–ankyrin bridging. In the present paper we show that deoxygenation of human erythrocytes results in displacement of ankyrin from band 3, leading to release of the spectrin/actin cytoskeleton from the membrane. This weakening of membrane–cytoskeletal interactions during brief periods of deoxygenation could prove beneficial to blood flow, but during episodes of prolonged deoxygenation, such as during sickle cell occlusive crises, could promote unwanted membrane vesiculation.

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Section: Discussionmentioning

confidence: 99%

Oxygen regulates the band 3–ankyrin bridge in the human erythrocyte membrane

Stefanovic

Puchulu-Campanella

Kodippili

et al. 2012

Biochemical Journal

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“…In recent years, evidence that suggests nongenomic effects of thyroid hormone is increasing Davis, 1996, 2002;Tapia et al, 2003). There is evidence to suggest that thyroid hormones stimulate transport across plasma membrane (Incerpi et al, 1999), modulate activities of enzymes like adenylate cyclase, Ca 2+ -ATPase, etc (Davis et al, 1989), regulate mitochondrial processes (Goglia et al, 1999) and induce acute changes in the electrical properties of the cell membrane (Sundquist et al, 1992). TRs are found to be expressed in lymphocytes (Arpin et al, 2000), and the role of thyroid hormones on B and T lymphocytes has been shown (Murphy et al, 1992).…”

Section: Introductionmentioning

confidence: 98%

Activation of NF-κB in lymphocytes and increase in serum immunoglobulin in hyperthyroidism: Possible role of oxidative stress

et al. 2008

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“…Over the past few years increasing evidence has been raised which suggests several nongenomic effects of thyroid hormone , such as the stimulation of plasma membrane transport (Huang et al 1999, Incerpi et al 1999, the modulation of enzyme activities (adenylate cyclase, Ca 2+ -ATPase; Davis et al 1989, Sakaguchi et al 1996, the regulation of mitochondrial processes (Goglia et al 1999), acute changes in the electrical properties of the cell membrane (Ribeiro et al 1998, Sundquist et al 1992, the activation of signal transduction pathways (Lanni et al 1994, Szabo et al 1996, Lin et al 1999a) and the activation of nuclear factor-B by the induction of oxidative stress (Tapia et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Nongenomic effect of thyroid hormone on free-radical production in human polymorphonuclear leukocytes

Mezősi¹,

Szabó²,

Nagy³

et al. 2005

Journal of Endocrinology

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Over the past few years increasing evidence has suggested the nongenomic effects of thyroid hormone, such as the activation of the signal transduction pathways and the activation of nuclear factor-B by the induction of oxidative stress. The present study was undertaken to investigate the effect of thyroid hormone on human polymorphonuclear leukocytes (PMNLs) which are known as important sources of reactive oxygen species in the circulation. The production of superoxide anion (O 2 ) and the activity of myeloperoxidase were determined in the presence and absence of several inhibitors of the signalling pathway. -Thyroxine (T 4 ), L-3,5,3 -tri-iodothyronine (T 3 ) and L-3,5-di-iodothyronine (T 2 ) stimulated O 2 production in PMNLs in a dose-dependent manner within a few minutes of addition to cells. Thyroid hormone-stimulated O 2 production was partially inhibited by pertussis toxin, an inhibitor of GTP-binding G protein, and was completely abolished by the protein kinase C inhibitors calphostin C and Ro-32-0432, and by a calcium chelator (BAPTA; bis-(o-aminophenoxy)ethane-N,N,N ,N -tetraacetic acid). Thyroid hormone stimulated myeloperoxidase activity and induced 125 I incorporation into PMNLs. Furthermore, thyroid hormone pre-incubation enhanced O 2 production for n-formyl-methionyl-leucylphenylalanine (FMLP) stimulation. In conclusion, novel nongenomic actions of thyroid hormone, the induction of superoxide anion production and the stimulation of myeloperoxidase activity in PMNLs were demonstrated. The induction of O 2 production requires calcium and is mediated by a pertussis toxin-sensitive G protein via stimulation of protein kinase C(s). These results suggest the existence of a membrane-bound binding site for thyroid hormone in PMNLs and a physiological role for thyroid hormone in the cellular defence mechanisms by stimulating free-radical production.

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The α1-adrenergic receptor in human erythrocyte membranes mediates interaction in vitro of epinephrine and thyroid hormone at the membrane Ca2+-ATPase

Cited by 23 publications

References 27 publications

Oxygen regulates the band 3–ankyrin bridge in the human erythrocyte membrane

Oxygen regulates the band 3–ankyrin bridge in the human erythrocyte membrane

Activation of NF-κB in lymphocytes and increase in serum immunoglobulin in hyperthyroidism: Possible role of oxidative stress

Nongenomic effect of thyroid hormone on free-radical production in human polymorphonuclear leukocytes

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