Purification of Prostaglandin E1/Prostacyclin Receptors of Human Blood Platelets

Duttaroy, Asim K.; Sinha, Asru K.

doi:10.1007/978-1-4612-0477-0_20

Cited by 31 publications

(51 citation statements)

References 15 publications

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“…Our data suggest that PGI, competes with high affinity for PGE, binding sites on rabbit erythrocyte membranes. However, in contrast to the above, PGE, did not compete for PGE, binding sites in rabbit erythrocyte membranes, suggesting that PGE, binding sites are related to a 'PGEJPGI,' receptor type [2,8,11,261.…”

Section: Discussioncontrasting

confidence: 64%

“…Components [I] and [11] of the equation show the true 'specific' and 'non-specific' contributions of the total binding, respectively. By substituting the values of n,, K, = 1/ K,,,, n2, and K 2 = 1/Kd,2 in the above equation, the specific and non-specific binding of [3H]PGE, to erythrocyte membranes in the absence and presence of various concentrations of insulin was found to be within 15 ?…”

Section: R =mentioning

confidence: 99%

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Prostaglandin‐E₁‐binding sites in rabbit erythrocyte membranes

Duttaroy¹,

Hoque²,

Paterson³

1993

European Journal of Biochemistry

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Prostaglandin El (PGE,) binding sites have been identified on rabbit erythrocyte membranes. The binding of PGE, to the membranes was found to be highly specific, reversible, and saturable.The high-affinity binding sites had a dissociation constant (Kd,,) of 5.6 * 1.2 nM with a binding capacity of 210 5 51 fmol/mg protein, whereas the low-affinity binding sites had a dissociation constant (&) of 22 2 6.4 pM, and a binding capacity of 321 ? 78 pmol/mg protein. Incubation with PGE, did not activate adenylate cyclase in the membranes. Preincubation of rabbit erythrocyte membranes with physiological amounts of insulin (1.5 nM) resulted in an increase of PGE, binding to the membranes from 241 ? 65 to 429 ? 85 fmoumg protein. The insulin-induced increase in PGE, binding was due to an increase in binding sites (both high-affinity and low-affinity binding sites) rather than to an increase in the affinity of the binding sites. Treatment of erythrocyte membranes with PGE, at concentrations (4.0-7.5 nM) which were within the Kd,, value of the high-affinity binding sites, resulted in a significant reduction in membrane fluorescence anisotropy (0.27 ? 0.005-0.21 ? 0.003). Use of higher concentrations (> 15 nM) of PGE, reversed the effect of its lower concentration on the membrane anisotropy.

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Section: Discussioncontrasting

confidence: 64%

Section: R =mentioning

confidence: 99%

Prostaglandin‐E₁‐binding sites in rabbit erythrocyte membranes

Duttaroy¹,

Hoque²,

Paterson³

1993

European Journal of Biochemistry

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“…PKA activity is mainly regulated by cAMP, the level of which is determined by adenylate cyclase (12) and phosphodiesterases (13) in platelets. Endothelium-derived prostacyclin (PGI 2 ) has been determined to be the main physiologic stimulator of cAMP production through activation of adenylate cyclase in platelets, which are marginalized to the periphery of the vessel, facilitating constant exposure to PGI 2 released by endothelial cells ( Figure 5F) (43). PGI 2 exists in plasma with a half-life of only 8.4 to 13.0 minutes, after which it is converted to an inactive stable form (44).…”

Section: Discussionmentioning

confidence: 99%

Protein kinase A determines platelet life span and survival by regulating apoptosis

Zhao

et al. 2017

Journal of Clinical Investigation

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“…Binding of the agonist to the low-a nity receptors (Kd in mM ranges) increases the cAMP level in platelets, which inhibits platelet aggregation. 137,138 Binding of the agonist to the high-a nity receptors also increases cAMP levels, probably in a compartmentalized manner and in a smaller quantity when compared with the synthesis of the compound through the lowa nity binding. 140 Also, the synthesis of cAMP by high-a nity prostaglandin binding is under feedback inhibition by the nucleotide itself.…”

Section: Platelet Abnormalities After Scimentioning

confidence: 99%

Risk factors for atherogenesis and cardiovascular autonomic function in persons with spinal cord injury

et al. 1999

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Persons with spinal cord injury (SCI) have been recognized to have several metabolic changes that adversely impact their risk for cardiovascular disease. An increased prevalence of disorders of carbohydrate metabolism and dyslipidemia may be related predominantly to paralysis with immobilization and associated loss of lean body tissue and gain in relative adiposity. Studies have reported an increased risk of vascular disease in those with SCI. As such, an understanding of the constellation of carbohydrate and lipid changes that occur after SCI is relevant to the clinical practice of medicine in this population. Oral glucose tolerance testing and associated studiesImpaired glucose tolerance and diabetes mellitus are more prevalent in individuals with SCI than in those who are able-bodied. 1 ± 4 In most of the individuals with SCI and abnormal carbohydrate tolerance, resistance to insulin mediation of glucose uptake by peripheral tissues may be demonstrable. In the presence of insulin resistance, the normal homeostatic response to glucose challenge is increased pancreatic b-cell secretion of insulin. If the compensatory response of the pancreas is insu cient to control the serum glucose concentration, worsening of carbohydrate tolerance will ensue.Bauman et al 3 performed a 75 g oral glucose tolerance test in 100 male veterans with SCI and in 50 able-bodied veteran controls. According to criteria established by the World Health Organization, 5 22% of those with SCI were diabetic whereas only 6% of the control group were diabetic. Eighty-two per cent of the controls had normal oral glucose tolerance, compared with 38% of those with quadriplegia and 50% of those with paraplegia. Subjects with SCI had signi®cantly higher mean plasma glucose and insulin values at several points during the oral glucose tolerance test when compared with controls ( Figure 1). In subgroups, determinants of insulin sensitivity were measured: per cent lean body mass, per cent fat mass, and cardiopulmonary ®tness. Values for insulin sensitivity were linearly related with those of ®tness (VO 2 max) determined from a progressive incremental upper-body exercise stress test. Insulin sensitivity was suggestively correlated with lean body mass, and negatively correlated with body fat. Thus, in a relatively small subgroup of untrained subjects with paraplegia, the strongest determinant of insulin sensitivity was cardiopulmonary ®tness.In 201 non-veteran subjects with SCI, Bauman et al 2 studied the relationship of oral carbohydrate tolerance after a 75 g glucose load to several variables, including level and completeness of lesion, gender, ethnicity, age, duration of injury, and anthropometric measures. Of the total group, 27 (13%) had diabetes mellitus and 56 (29%) had impaired glucose tolerance. 2,6 The subjects with complete tetraplegia had sign®cantly worse carbohydrate tolerance (Figure 2) and were more frequently classi®ed with a disorder of carbohydrate tolerance than the other neurological de®cit subgroups. 2 There were no signi®cant gend...

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Purification of Prostaglandin E1/Prostacyclin Receptors of Human Blood Platelets

Cited by 31 publications

References 15 publications

Prostaglandin‐E₁‐binding sites in rabbit erythrocyte membranes

Prostaglandin‐E₁‐binding sites in rabbit erythrocyte membranes

Protein kinase A determines platelet life span and survival by regulating apoptosis

Risk factors for atherogenesis and cardiovascular autonomic function in persons with spinal cord injury

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Purification of Prostaglandin E1/Prostacyclin Receptors of Human Blood Platelets

Cited by 31 publications

References 15 publications

Prostaglandin‐E1‐binding sites in rabbit erythrocyte membranes

Prostaglandin‐E1‐binding sites in rabbit erythrocyte membranes

Protein kinase A determines platelet life span and survival by regulating apoptosis

Risk factors for atherogenesis and cardiovascular autonomic function in persons with spinal cord injury

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Product

Resources

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Prostaglandin‐E₁‐binding sites in rabbit erythrocyte membranes

Prostaglandin‐E₁‐binding sites in rabbit erythrocyte membranes