Treatment outcomes after combination interventional and cognitive motivational counseling on analgesic medication use in patients with chronic spine pain.

Background: Pain interventionists can interrupt pain through anesthetic blockade of neural transmission to virtually any part of the body. Temporary pain relief can be achieved by the direct application of targeted anesthetic. Diagnostically, nerve blocks help identify specific pain generators, refine differential diagnosis, and disrupt the neural transmission mechanisms to stop pain generation peripherally.

Disulfide bond reduction: A powerful, chemical probe for the study of structure-function relationships in the hemocyanins.

The copper-containing hemocyanins are a class of oxygen-transport proteins whose structures differ in arthropods and molluscs. Crystal structure analyses and amino acid sequence comparisons show that disulfide bonding is a common feature in both arthropod and mollusc hemocyanins. Reduction of the disulfide bonds of a representative set of arthropod and mollusc hemocyanins results in complete loss of their oxygen-binding capacities.

Outcomes of sudden cardiac arrest treated with defibrillation by emergency medical technicians (EMT-Ds) or paramedics in a two-tiered urban EMS system.

Objective: Controversy exists as to the effectiveness of defibrillation by emergency medical technicians (EMT-Ds) in reducing mortality from cardiac arrest in two-tiered EMS systems. This study was performed to assess the impact of EMT-Ds on outcome of sudden cardiac death in a small, urban, modified two-tiered EMS system.

Methods: This was a retrospective, unmatched case-control study comparing the outcomes of patients suffering sudden cardiac death treated by EMT-Ds with paramedic (EMT-P) backup with the outcomes of patients treated by EMT-Ps as first responders.

Active-site disruption in native Limulus hemocyanin and its subunits by disulfide-bond reductants: a chemical probe for the study of structure-function relationships in the hemocyanins.

The crystal structure analysis of Subunit II of Limulus hemocyanin has shown that its polypeptide chain is folded into three distinct structural domains. The oxygen-binding, dinuclear copper center is located deep in the core of Domain 2. Two disulfide bonds are located in a bridging domain, Domain 3.

Xanthine oxidase: an efficient promoter of the iron loading of apoferritin.

Xanthine oxidase exhibits ferroxidase activity and previously has been shown to catalyze the oxidative incorporation of iron into apotransferrin, the iron transport protein of plasma. These studies demonstrate that xanthine oxidase also efficiently promotes the oxidative incorporation of iron into apoferritin, the major iron storage protein of vertebrates, and that the ferroxidase activity of intestinal xanthine oxidase could be important in determining the fraction of iron within the intestinal mucosa cell partitioned to ferritin versus the iron that remains in a transient pool for rapid transport to plasma.

Comparison of changes in the uptake and mucosal processing of iron in riboflavin-deficient rats.

Riboflavin deficiency in rats resulted in a reduction in the transfer of 59Fe from an intragastric dose to plasma compared to age-matched or weight-matched controls. The uptake of iron by brush-border membrane vesicles made from intestinal mucosa of riboflavin-deficient rats was much less than identically-prepared vesicles from control groups. Although the mucosal content of 59Fe was smaller in riboflavin-deficient rats thirty minutes after dosing, the relative distribution of 59Fe between the mucosal iron-binding proteins, ferritin and transferrin, was not changed compared to the control groups.

Alterations in the mucosal processing of iron in response to very-short-term dietary iron depletion and repletion.

The transfer of control rats to a low-iron diet for only 24 h resulted in a 2-fold increase in iron uptake by brush-border membrane vesicles. Extension of the low-iron feeding period to 72 h or 2 weeks resulted in only small additional increases in iron uptake by vesicle preparations. In contrast, the transfer of iron-deficient rats to a control diet resulted in a progressive decrease in iron uptake by vesicles that reached a level equivalent to that of control rats in 2 weeks.

Epidermal growth factor in the neonatal mouse salivary gland and kidney.

In the adult mouse, epidermal growth factor (EGF) is synthesized in granular convoluted tubule (intralobular) duct cells of the submandibular gland and in distal tubule cells of the kidney. The presence of EGF in developing tissues and maternal milk and the localization of EGF receptors in developing tissues suggest a role for EGF in developmental processes. The primary aims of the present study were to: (1) localize EGF and EGF-binding sites in the kidney and submandibular gland during neonatal development and (2) to determine the effect of exogenously administered EGF on cell proliferation in these two developing organs.

Comparison of changes in uptake and mucosal processing of iron in short and long-term iron depletion.

Thirty minutes following an intragastric dose of [59]Fe, rats subjected to short-term and long-term iron depletion showed a similar increase in [59]Fe in plasma and a similar decrease in the retention of [59]Fe in mucosal cytosol compared to controls. With both low-iron groups, a two-fold increase in [59]Fe uptake by brush-border membrane vesicles and a six-fold reduction in the [59]Fe incorporated into the ferritin of the mucosal cytosol were observed. These studies indicate that short-term exposure to a low-iron diet triggers changes in both the uptake of iron by the brush-border membrane and the processing of iron within the mucosal cell prior to major changes in body iron status.

Purification and characterization of an iron-binding protein from the blue crab (Callinectes sapidus).

The presence of an iron-binding protein in the hemolymph of the blue crab (Callinectes sapidus) was detected by gel filtration of 59Fe-labeled hemolymph. The iron-binding protein was purified to homogeneity by ion exchange chromatography. 2.

The mobilization of ferritin iron by liver cytosol. A comparison of xanthine and NADH as reducing substrates.

Considerable evidence suggests that the release of iron from ferritin is a reductive process. A role in this process has been proposed for two hepatic enzymes, namely xanthine oxidoreductase and an NADH oxidoreductase. The abilities of xanthine and NADH to serve as a source of reducing power for the enzyme-mediated release of ferritin iron (ferrireductase activity) were compared with turkey liver and rat liver homogenates.

Isolation, purification and characterization of an iron-binding protein from the horseshoe crab (Limulus polyphemus).

The presence of an iron-binding protein in the haemolymph of the horseshoe crab, Limulus polyphemus, was detected by gel filtration of 59Fe-labelled haemolymph. Lysis of amoebocytes did not change the amount of iron-binding protein in haemolymph samples. The protein was purified to homogeneity by ion-exchange chromatography.

Active-site heterogeneity in Limulus hemocyanin as revealed by reaction with peroxides.

Previously reported differences in the reactivities toward active-site ligands such as hydrogen peroxide indicate that the active-site geometries of the arthropod and mollusc hemocyanins are significantly different. Results are presented which demonstrate that the purified subunits composing the native hemocyanin of an arthropod show comparable active-site heterogeneity. Neither whole nor stripped samples of Limulus oxyhemocyanin are completely oxidized by reaction with hydrogen peroxide.

The effect of epidermal growth factor on neonatal incisor differentiation in the mouse.

The effect of epidermal growth factor (EGF) on cellular differentiation of the neonatal mouse mandibular incisor was examined autoradiographically using tritiated thymidine ([3H]TDR) and tritiated proline ([3H]PRO). On days 0 (day of birth), 1, and 2, EGF was administered (3 micrograms/g body wt) sc to neonates. Mice were killed on Days 1, 4, 7, 10, and 13 after birth and were injected with either [3H]TDR or [3H]PRO 1 hr before death.

Studies of the ferroxidase activity of native and chemically modified xanthine oxidoreductase.

The O2-utilizing (type O, oxidase) form of xanthine oxidoreductase is primarily responsible for its ferroxidase activity. This form of xanthine oxidoreductase has 1000 times the ferroxidase activity of the serum ferroxidase caeruloplasmin. It has the ability to catalyse the oxidative incorporation of iron into transferrin at very low Fe2+ and O2 concentrations.

The effect of short-term exposure to low-iron diets on the mucosal processing of ionic iron.

Short-term alterations in the amount of iron in the diets of rats caused substantial differences in the distribution of a test dose of radioiron between mucosal transferrin and mucosal ferritin, and also caused a change in the relative amounts of these two proteins in mucosal tissue without resulting in any detectable change in liver iron stores. These differences correlated with changes in the retention of radioiron by the intestinal mucosa and the transport of radioiron to the blood stream. These studies emphasize the importance of local changes in the intestinal mucosa in the regulation of dietary iron absorption.

Purification and characterization of the serum ferroxidase inhibitor.

The inhibitor of the serum ferroxidases, recently detected in rabbit serum, has been purified to homogeneity from human serum by a combination of gel-filtration and ion-exchange chromatography. The molecular weight, chromatographic behavior, electrophoretic mobility, electrofocusing pH, carbohydrate content, and reactivity with anti-human albumin during immunodiffusion indicate that the ferroxidase inhibitor is serum albumin. Copper-binding studies, proteolytic fragmentation studies, and a comparison of the inhibitory potencies of several albumin species which differ in their affinity for copper strongly indicate that albumin elicits its inhibitory effect on the serum ferroxidases by interacting with the functional copper of these enzymes.

Purification and characterization of the intestinal promoter of iron(3+)-transferrin formation.

The nonceruloplasmin enzyme located in the intestinal mucosa which promotes the incorporation of iron into transferrin has been resolved into a small, heat-stable component and a heat-labile protein component. The small, heat-stable component was purified from the high-speed supernatant of intestinal mucosal homogenates by ion-exchange chromatography and gel filtration and identified as xanthine. The heat labile protein component was purified from the high-speed supernatant of intestinal mucosal homogenates by heat treatment, gel filtration, and ion-exchange chromatography.

Dissociation and reconstitution of human ferroxidase II.

The ferroxidase II protein from human serum is large and structurally complex. It possesses protein-bound lipid and copper components which are essential for the maintenance of its catalytic activity. Treatment of ferroxidase II with 8 M urea, 6 M guanidine hydrochloride, or 6 M guanidine hydrochloride and alkylation does not result in the dissociation of the enzyme into subunits.