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PubMed1987

Identification of the complement decay-accelerating factor (DAF) on epithelium and glandular cells and in body fluids.

Decay-accelerating factor (DAF) is a 70 kD membrane regulatory protein that prevents the activation of autologous complement on cell surfaces. Using immunohistochemical methods and a radioimmunometric assay based on mAbs to DAF, we found large amounts of membrane-associated DAF antigen on the epithelial surface of cornea, conjunctiva, oral and gastrointestinal mucosa, exocrine glands, renal tubules, ureter and bladder, cervical and uterine mucosa, and pleural, pericardial and synovial serosa. Additionally, we detected soluble DAF antigen in plasma, tears, saliva, and urine, as well as in synovial and cerebrospinal fluids. While plasma, tear, and saliva DAF are larger than erythrocyte (Ehu) membrane DAF by Western blot analysis, urine DAF is slightly smaller (67,000) in Mr. Unlike purified Ehu DAF, however, urine DAF is unable to incorporate into the membrane of red cells. Although its inhibitory activity on the complement enzyme C3-convertase is lower than that of Ehu DAF, it is comparable to that of serum C4 binding protein (C4bp). Biosynthetic studies using cultured foreskin epithelium and Hela cells disclosed DAF levels (approximately 2 X 10(5) molecules/cell) exceeding those on blood cells. In addition, these studies revealed the synthesis of two DAF species, one with apparent Mr corresponding to that of epithelial cell membrane DAF and the other to urine DAF, suggesting that the urine DAF variant arises from adjacent epithelium. The function of DAF in body fluids is unknown, but the observation that urine DAF has C4bp-(or factor H-)like activity shows that it could inhibit the fluid phase activation of the cascade.

Body Fluids↗
PubMed1978

Alterations of body fluid compartments and distribution of tissue water and electrolytes in rhesus monkeys with rocky mountain spotted fever.

Chair-restrained rhesus monkeys (Macaca mulatta) were inoculated subcutaneously with 10(2)--10(3) plaque-forming units of virulent Rickettsia rickettsii. The latent period for fever and rickettsemia was three to four days; death occurred six to eight days after infection. Total circulatory electrolyte levels and fluid volumes, including plasma, red blood cell, true circulatory blood, and extracellular fluid, increased. The expansion of the extracellular and plasma volumes resembled findings reported during severe Rocky Mountain spotted fever in humans, guinea pigs, and rabbits. Total water content of the liver also increased. Intracellular concentrations of K+, as well as total Na+ and K+, decreased in the diaphragm. Both the lung and medulla oblongata showed increased levels of intracellular Na+ and water with simultaneously decreased levels of extracellular Na+ and water. Such an intracellular overhydration of the medulla oblongata could contribute to death as a result of depression of the cardiovascular and respiratory centers. On the basis of the findings in monkeys, the intravenous infusion of fluids and electrolytes during clinical therapy of severe rickettsial infections should be considered extremely dangerous.

Animals↗
PubMed1988

Radioimmunoassay of human epidermal growth factor--hEGF levels in human body fluids.

By immunizing rabbits with purified human epidermal growth factor (hEGF), which was synthesized by Escherichia coli constructed by a genetic engineering technique, high titer antiserum for hEGF was obtained. The antiserum has an excellent specificity to hEGFs (hEGF, hEGF [1-51], hEGF [1-47] and [Leu21] hEGF) and has almost no cross-reactivity with other biological peptides, such as mouse EGF and human platelet derived growth factor. Using radioiodinated hEGF, a radioimmunoassay (RIA) for hEGF was established by a double antibody-polyethylene glycol method. As little as 10 pg/tube of hEGF was successfully determined by the present RIA methods. The intra- and inter-assay coefficients of variation for hEGF in human plasma or serum were 2.4-4.9% and 3.7-6.2%, respectively. The hEGF levels in human body fluids determined by the present method were as follows: urine (11-100 ng/ml), serum (1.0-1.8 ng/ml), plasma (0.2-0.8 ng/ml), sperm (17-47 ng/ml), saliva (0.9-3.0 ng/ml) and tears (9.5-27 ng/ml).

Adult↗
PubMed1986

Long-term effects of enalapril monotherapy and enalapril/hydrochlorothiazide combination therapy on blood pressure, renal function, and body fluid composition.

Enalapril, a potent long-acting angiotensin-converting enzyme inhibitor, was prescribed either alone (n = 9) or in combination (n = 20) with hydrochlorothiazide for 96 weeks in essential hypertensive subjects. Blood pressure was well controlled following both monotherapy or combination therapy. Plasma renin activity was stimulated in all subjects; plasma aldosterone concentration was stimulated only in subjects receiving combination therapy. Glomerular filtration rate (assessed by inulin clearance) was unchanged in subjects with initial clearances greater than 80 ml/min/1.73 m2 but was significantly improved (55%) following either form of therapy in subjects with initial clearances less than or equal to 80 ml/min/1.73 m2. Neither monotherapy nor combination therapy adversely affected 24-hour urinary protein excretion, sodium excretion, or body fluid composition. These results suggest that enalapril, either alone or in combination with hydrochlorothiazide, is effective therapy for mild to moderate hypertension. There are no adverse effect on renal function; indeed, enalapril has the capability of improving renal function in those subjects whose renal function was initially impaired from long-standing hypertension.

Adult↗
PubMed1985

Effects of enalapril alone, and in combination with hydrochlorothiazide, on renin-angiotensin-aldosterone, renal function, salt and water excretion, and body fluid composition.

Enalapril is a new, oral, long-acting nonsulfhydral angiotensin converting enzyme inhibitor. Thirty-nine patients with primary hypertension were entered into a randomized, double-blind protocol to assess the efficacy of enalapril (10 to 20 mg bid), hydrochlorothiazide (25 to 50 mg bid), or combined drug therapy. Enalapril, either alone or in combination with hydrochlorothiazide, effectively controlled blood pressure. Enalapril monotherapy was associated with an increase in plasma renin activity and a decrease in angiotensin II concentration; in patients with an initial inulin clearance less than or equal to 80 mL/min/1.73 m2, inulin and para-aminohippurate clearances were markedly improved, without producing adverse effects on salt and water excretion or body fluid composition. Combination therapy was associated with a marked increase in plasma renin activity; however, only those patients with an initial inulin clearance less than or equal to 80 mL/min/1.73 m2 demonstrated suppression of angiotensin II concentration and marked improvement in inulin and para-aminohippurate clearances. These observations suggest that enalapril, either alone or in combination with a diuretic, has the potential to reverse renal function abnormalities encountered in the hypertensive state.

Body Fluids↗
PubMed1992

Human urine deoxyribonuclease II (DNase II) isoenzymes: a novel immunoaffinity purification, biochemical multiplicity, genetic heterogeneity and broad distribution among tissues and body fluids.

Deoxyribonuclease II (DNase II) was purified from the urine of a 48-year-old male (a single individual) using a column chromatography series, including concanavalin A-agarose and an immunoaffinity column utilizing anti-human spleen DNase II antibody, and was then characterized. Based on the catalytic properties of the purified enzyme, we have devised a technique of isoelectric focusing by thin-layer polyacrylamide gel electrophoresis (IEF-PAGE) combined with a specific zymogram method, for investigating the possible molecular heterogeneity of human DNase II. DNase II in urine as well as the purified form was found to exist in multiple forms with different pI values separable by IEF-PAGE within a pH range of 5-7. Since sialidase treatment of the urine sample induced simplification of the isoenzyme patterns with diminishment of anodal bands, it was clear that the multiplicity of the enzyme was in part due to differences in the sialic acid content. On screening of DNase II isoenzyme patterns in urine samples from more than 200 Japanese individuals, only the common isoenzyme pattern was observed and no electrophoretic variations were detected. However, genetic studies of urinary enzyme activity and comparative studies on the activity in urine, semen and leukocytes from the same individuals suggest that the enzyme activity level of DNase II may be under genetic control. The enzyme was widely distributed in human tissues and showed high activities in secretory body fluids such as breast milk, saliva, semen and urine, and leukocyte lysates.

Body Fluids↗
PubMed2000

Influence of preparation conditions on the microstructure and bioactivity of alpha-CaSiO(3) ceramics: formation of hydroxyapatite in simulated body fluid.

Two different reagents, NaOH and NH(4)OH, were used to precipitate CaSiO(3) precursor powders from ethanol solutions of Ca(NO(3))(2). 4H(2)O and Si(OC(2)H(5))(4). The resultant powders of different Ca/Si ratio and residual Na(2)O content exhibited significant differences in the microtexture of the resulting sintered alpha-CaSiO(3) ceramics. The microtexture of the ceramics from the NaOH system (CS-Na) contained smaller grain sizes and a thicker glassy phase at the grain boundaries than those produced using NH(4)OH (CS-NH). The CS-Na ceramics were soaked in a simulated body fluid (SBF) at 36.5 degrees C for 2 h and 1, 5, 6, 10, 21, and 30 days while the CS-NH ceramics were soaked for 1, 5, 7, 15, 20, and 25 days using the same conditions. Hydroxyapatite (HAp) formed on the surfaces of both samples but at different formation rates due to differences in the microstructure. The CS-Na ceramics showed faster HAp formation because their smaller alpha-CaSiO(3) grains dissolved more readily, allowing the calcium concentration in the SBF quickly to approach the appropriate condition for nucleation of HAp. In addition, the thicker glassy phase at the grain boundaries facilitated a faster formation of silanol on the surface of the amorphous SiO(2) interlayer, a reaction that is considered to be a prerequisite for HAp formation. The formation of the HAp layer on the CS-Na ceramics therefore was very fast (12 microm/day), and their surfaces were covered completely within 5 days. A layer thickness of about 110 microm was achieved in 30 days, in contrast with the CS-NH ceramics, which took about 25 days to be fully covered with a 60-microm layer of HAp.

Body Fluids↗
PubMed1991

Characterization of macrophage colony-stimulating factor in body fluids by immunoblot analysis.

We characterized the molecular species of human macrophage colony-stimulating factor (hM-CSF) found in serum and urine, using immunoblot analysis after partial purification on an antibody-bound affinity column. Although antibodies were prepared using the recombinant product of the large form of hM-CSF with a molecular weight (MW) of 85 Kd as the antigen, this immunoblot system was also capable of detecting the small form of hM-CSF with a MW of 40 to 60 Kd. A single band with a MW of 43 Kd, which reacted with anti-recombinant hM-CSF IgG but not with control IgG, was found when serum and urine from normal adults underwent electrophoresis on reduced sodium dodecyl sulfate-polyacrylamide gel and subsequent immunoblotting. This band represented a subunit of the large form of hM-CSF, because the large form of hM-CSF is a homodimer of a subunit with a MW of 43 Kd and the small form of hM-CSF is a homodimer of a subunit with a MW of 20 to 30 Kd. Analysis of serum and urine from leukemic patients and pregnant women, who had higher serum levels of hM-CSF than normal adults, showed only a single band with a MW of 43 Kd as a hM-CSF-specific molecule. These results suggest that the large form of hM-CSF is the major species in human body fluids.

Body Fluids↗
PubMed1997

Morphine, morphine-3-glucuronide, morphine-6-glucuronide, and 6-monoacetylmorphine determined by means of atmospheric pressure chemical ionization-mass spectrometry-liquid chromatography in body fluids of heroin victims.

Morphine, morphine-3-glucuronide (M3G), morphine-6-glucuronide (M6G), and 6-monoacetylmorphine (6-MAM) were isolated from body fluids using solid-phase extraction and determined by means of atmospheric pressure chemical ionization-mass spectrometry-liquid chromatography (APCI-LC-MS) in selected ion monitoring mode. The following ions were monitored: m/z 286 for morphine; m/z 286 and 462 for M3G and M6G; m/z 211, 268, and 328 for 6-MAM; and m/z 289 for morphine-d3 (internal standard). The recoveries ranged from 82 to 89% The limits of detection were as follows: 0.1 ng/mL (morphine), 0.5 ng/mL (6-MAM), and 1 ng/mL (M3G and M6G). The analytes were determined in samples taken from 21 heroin-overdose victims. Twenty-one blood samples, 11 cerebrospinal fluid (CSF) samples, 12 vitreous humor (VH) samples, and 6 urine samples were investigated. Blood concentrations (ng/mL) of morphine ranged from 8 to 1539, of M3G from 111 to 941, of M6G from 32 to 332, and of 6-MAM from 0 to 73. The levels of morphine were correlated with glucuronide values and with 6-MAM. The concentrations of morphine, M3G, and M6G in CSF were, as a rule, lower than in blood and lower in VH than in CSF. The concentrations of morphine and molar ratios of M6G-morphine in blood and CSF were correlated. Low ratios of M3G-morphine and M6G-morphine in blood of heroin-overdose victims indicated short survival time after drug intake.

Adolescent↗
PubMed1988

Estimation of body fluid volumes using tetrapolar bioelectrical impedance measurements.

Mathematical equations using tetrapolar bioelectrical resistive (R) and reactive (Xc) impedance measures were developed and crossvalidated to predict total body water (TBW) and corrected bromide space (CBS) in two independent samples (n = 110). Height2 per low R was the best predictor of TBW (R = 0.96) and CBS (R = 0.92). When the influence of TBW was removed from CBS and dependent variables, height2 per low Xc was the best predictor (R = 0.50) of CBS. Double crossvalidation of each sample showed that observed and predicted TBW (R = 0.978 and 9.986) and CBS (0.937 and 0.907) were significantly related (p less than 0.001), and there was no difference (p greater than 0.05) between the values. The lines representing the relationships between observed and predicted values had regression coefficients not different than the line of identity. Data from both samples were combined to give a representative multiple regression equation to predict TBW and CBS. This study establishes the validity of the tetrapolar bioelectrical impedance method to assess body fluid volumes in humans.

Adult↗
PubMed1997

Determination of morphine and its 3- and 6-glucuronides, codeine, codeine-glucuronide and 6-monoacetylmorphine in body fluids by liquid chromatography atmospheric pressure chemical ionization mass spectrometry.

A selective assay of morphine-3-glucuronide (M3G), morphine-6-glucuronide (M6G), morphine, codeine, codeine-6-glucuronide (C6G) and 6-monoacetylmorphine (6-MAM) based on liquid chromatography atmospheric pressure chemical ionization mass spectrometry (LC-APCI-MS) is described. The drugs were extracted from serum, autopsy blood, urine, cerebrospinal fluid or vitreous humor using C18 solid-phase extraction cartridges and subjected to LC-APCI-MS analysis. The separation was performed on an ODS column in acetonitrile-50 mM ammonium formate buffer, pH 3.0 (5:95), using a flow-rate gradient from 0.6 to 1.1 ml/min (total analysis time was 17 min). The quantitative analysis was done using deuterated analogues of each compound. Selected-ion monitoring detection was applied: m/z 286 (for morphine, M3G-aglycone and M6G-aglycone), 289 (for morphine-d3, M3G-d3-aglycone and M6G-d3-aglycone), 300 (for codeine and C6G-aglycone), 303 (for C6G-d3-aglycone), 306 (for codeine-d6), 328 (for 6-MAM), 334 (for 6-MAM-d6), 462 (for M3G and M6G), 465 (for M3G-d3 and M6G-d3), 476 (for C6G) and 479 (for C6G-d3). The limits of quantitation were: 1 microg/l for morphine, 2 microg/l for 6-MAM, 5 microg/l for M3G, M6G and codeine and 200 microg/I for C6G. The recovery ranged from 85 to 98% for each analyte. The method appeared very selective and may be used for the routine determination of opiates in body fluids of heroin abusers and patients treated with opiates.

Analgesics, Opioid↗
PubMed2005

Transient body fluid accumulation and enhanced NKCC2 expression in gerbils with brain infarction.

BACKGROUND: Enhanced expression of a kidney-specific sodium co-transporter (NKCC2: Na-K-2Cl co-transporter) in the thick ascending limb of Henle has been identified in rat models of congestive heart failure and liver cirrhosis, suggesting that high NKCC2 expression underlies edema formation. An increased abundance of NKCC2, however, has also been noted in rats with the syndrome of inappropriate secretion of antidiuretic hormone; hyponatremia without edema. In the present study, we examined NKCC2 expression in non-edematous disease, such as a brain infarction, and investigated the physiological and/or pathological characterization of NKCC2 expression. METHODS: We initially examined NKCC2 expression in an animal model of brain infarction. Mongolian gerbils (around 60 g body weight) underwent bilateral clamping of the common carotid arteries for 5 min for the induction of brain infarction. NKCC2 and apical water channel (AQP2) protein levels in the collecting duct were examined by Western blotting in kidney tissues 2, 7, and 14 days after the brain infarction. Gerbils with brain infarction were then fed either a normal low-sodium diet (0.3 g/kg/day) or a high-sodium diet (3.0 g/kg/day), and body weight, urine volume and urinary osmolality were examined daily. Blood parameters were measured on day 14 after the brain infarction. RESULTS: Histochemical examination of the brain confirmed the presence of brain infarction, as manifested by altered cresyl violet staining in the hippocampus. Protein levels of NKCC2 were significantly increased in gerbils with brain infarction on days 2 and 7 after brain infarction, whereas AQP2 protein signals remained unaltered. However, the increased NKCC2 intensity disappeared on day 14. Body weight gain was slightly, but significantly greater in gerbils with brain infarction than in sham-operated gerbils up to 7 days after the brain infarction. The high-sodium diet resulted in significant urinary concentration and enhanced weight gain in infarcted gerbils. CONCLUSION: We noted increased NKCC2 abundance in non-edematous disease, which enhanced body fluid accumulation, likely via the sodium loading-dependent concentration of the urine. These results suggest that the physiological process of edema formation is based on specific NKCC2 expression. The transient duration of these findings in the present animal model suggests two different characteristics of specific NKCC2 expression, an immediate, transient appearance as a common response in serious conditions and more chronic expression that leads to edema formation.

Animals↗
PubMed1983

High-performance liquid chromatographic quantitation of trimethoprim, sulfamethoxazole, and N4-acetylsulfamethoxazole in body fluids.

We describe a rapid, precise and simple procedure for the quantitative determination of trimethoprim, sulfamethoxazole, and N4-acetylsulfamethoxazole in body fluids by reversed-phase high-performance liquid chromatography. This method utilizes antipyrine as an internal standard with the compounds detected by dual-wavelength monitoring at 225 nm and 254 nm after a single-step extraction. Precision, sensitivity, and accuracy of this assay are within the range of clinical utility; the coefficient of variation is less than or equal to 3%, sensitivity less than 0.5 micrograms/ml for all compounds, and recovery greater than 97%. The short time for performance and small sample size makes the assay ideal for clinical drug monitoring and pharmacokinetic studies.

Chromatography, High Pressure Liquid↗