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Article ; Online: Prevalence of bacterial burden on macroscopic contaminants of orthopaedic surgical instruments following sterilization.

Wellington, I J / Schneider, T J / Hawthorne, B C / McCarthy, M B / Stelzer, J W / Connors, J P / Dorsey, C / Williams, V / Lindsay, A / Solovyova, O

The Journal of hospital infection

2022 Volume 130, Page(s) 52–55

Abstract: Background: Macroscopic contamination of orthopaedic instruments with particulates, including cortical bone and polymethyl methacrylate (PMMA) bone cement, that have previously undergone pre-operative sterilization is frequently encountered peri- or ... ...

Abstract	Background: Macroscopic contamination of orthopaedic instruments with particulates, including cortical bone and polymethyl methacrylate (PMMA) bone cement, that have previously undergone pre-operative sterilization is frequently encountered peri- or intraoperatively, calling into question the sterility of such instruments. Aim: To determine if macroscopic contaminants of orthopaedic surgical instrumentation maintain a bacterial burden following sterile processing, and to determine the most commonly contaminated instruments and the most common contaminants. Methods: Macroscopic contaminants in orthopaedic instrument trays were collected prospectively at a single tertiary referral centre over a 6-month period from August 2021 to May 2022. When identified, these specimens were swabbed and plated on sheep blood agar. All specimens were incubated at 37 °C for 14 days, and inspected visually for colony formation. When bacterial colony formation was identified, samples were sent for species identification. Results: In total, 33 contaminants were tested, and only one contaminant was found to be growing bacterial colonies (Corynebacterium sp.). The items most commonly found to have macroscopic contamination were surgical trays (N=9) and cannulated drills (N=7). The identifiable contaminants were bone (N=10), PMMA bone cement (N=4) and hair (N=4). Eleven macroscopic contaminants were not identifiable. Conclusion: This study found that 97% of macroscopic orthopaedic surgical instrument contaminants that underwent sterile processing did not possess a bacterial burden. Contaminants discovered during a procedure are likely to be sterile, and do not pose a substantially increased risk of infection to a patient.
MeSH term(s)	Animals ; Sheep ; Orthopedics/methods ; Polymethyl Methacrylate ; Bone Cements ; Prevalence ; Sterilization/methods ; Surgical Instruments/microbiology ; Bacteria
Chemical Substances	Polymethyl Methacrylate (9011-14-7) ; Bone Cements
Language	English
Publishing date	2022-09-08
Publishing country	England
Document type	Journal Article
ZDB-ID	779366-2
ISSN	1532-2939 ; 0195-6701
ISSN (online)	1532-2939
ISSN	0195-6701
DOI	10.1016/j.jhin.2022.08.010
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Article: The Journal and SI units.

Schneider, T J

The New England journal of medicine

1993 Volume 328, Issue 14, Page(s) 1040; author reply 1041

MeSH term(s)	International System of Units ; Periodicals as Topic ; United States
Language	English
Publishing date	1993-04-08
Publishing country	United States
Document type	Comment ; Letter
ZDB-ID	207154-x
ISSN	1533-4406 ; 0028-4793
ISSN (online)	1533-4406
ISSN	0028-4793
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Article: Similarities between the oxygen-sensing mechanisms regulating the expression of vascular endothelial growth factor and erythropoietin.

Goldberg, M A / Schneider, T J

The Journal of biological chemistry

1994 Volume 269, Issue 6, Page(s) 4355–4359

Abstract: The ability to adapt successfully to periods of relative hypoxia is crucial to the survival of all higher life forms. Several genes have previously been identified which are up-regulated in response to hypoxia; these include the genes encoding ... ...

Abstract	The ability to adapt successfully to periods of relative hypoxia is crucial to the survival of all higher life forms. Several genes have previously been identified which are up-regulated in response to hypoxia; these include the genes encoding erythropoietin (Epo), platelet-derived growth factor B chain, endothelin, interleukin-1 alpha, ornithine decarboxylase, and vascular endothelial growth factor (VEGF). However, the molecular mechanisms by which hypoxia is sensed remain enigmatic. In addition, it is unknown whether the genes mentioned share a common oxygen-sensing signal transduction pathway. In this report we demonstrate multiple similarities between the oxygen-sensing mechanisms regulating the expression of VEGF and Epo. The expression of both mRNAs is significantly up-regulated by hypoxia and cobalt chloride (CoCl2), and the half-life of both mRNAs is markedly prolonged by cycloheximide. In addition, hypoxic induction of both Epo and VEGF is inhibited by carbon monoxide. As part of our investigation into the signal transduction pathway responsible for the hypoxia and cobalt induction of these genes, we discovered that the expression of members of the jun and fos protooncogene families is also up-regulated early after exposure to either of these stimuli. These findings provide support for the hypothesis that the mechanism(s) by which hypoxia is sensed at a molecular level may be highly conserved and tightly regulated.
MeSH term(s)	Animals ; Cobalt/pharmacology ; Cycloheximide/pharmacology ; Endothelial Growth Factors/genetics ; Erythropoietin/genetics ; Gene Expression Regulation/drug effects ; Genes, fos ; Genes, jun ; Heme/physiology ; Humans ; Hypoxia/physiopathology ; In Vitro Techniques ; Lymphokines/genetics ; Oxygen/physiology ; RNA, Messenger/genetics ; Rats ; Tumor Cells, Cultured ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors
Chemical Substances	Endothelial Growth Factors ; Lymphokines ; RNA, Messenger ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors ; Erythropoietin (11096-26-7) ; Cobalt (3G0H8C9362) ; Heme (42VZT0U6YR) ; Cycloheximide (98600C0908) ; Oxygen (S88TT14065)
Language	English
Publishing date	1994-02-11
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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Article: Placental transfer of the thromboxane synthetase inhibitor ridogrel in the late-pregnant ewe.

Schneider, T J / Struijk, P C / Wallenburg, H C

European journal of obstetrics, gynecology, and reproductive biology

1999 Volume 86, Issue 1, Page(s) 83–87

Abstract: Objectives: To assess the occurrence of placental transfer of the thromboxane synthetase inhibitor ridogrel in the pregnant ewe and to determine its effect on prostanoid levels in the ewe and fetal lamb, on uterine contractility and on maternal and ... ...

Abstract	Objectives: To assess the occurrence of placental transfer of the thromboxane synthetase inhibitor ridogrel in the pregnant ewe and to determine its effect on prostanoid levels in the ewe and fetal lamb, on uterine contractility and on maternal and fetal hemodynamics. Study design: Five chronically instrumented pregnant ewes at 122 days of gestation received intravenous infusions of 5 mg/kg/3 h ridogrel and solvent. Maternal and fetal arterial samples were obtained at predetermined intervals to determine concentrations of ridogrel and prostaglandin metabolites TXB2, 6-keto-PGF1alpha, PGF2alpha, and PGE2. Maternal and fetal responses of blood flow and pressures were determined. Results: Fetal ridogrel levels were 25% of maternal concentrations. Ridogrel showed rapid and marked thromboxane synthetase inhibition and augmentation of levels of prostaglandin metabolites. There was no evidence of change in amniotic pressure, uterine blood flow, maternal and fetal blood pressure and heart rate. Conclusion: Ridogrel is a potent thromboxane synthetase inhibitor which passes the sheep placenta, does not influence maternal and fetal hemodynamics and uterine contractility, and shows similar antiplatelet activity in the ewe and the fetal lamb.
MeSH term(s)	6-Ketoprostaglandin F1 alpha/blood ; Animals ; Blood Pressure/drug effects ; Dinoprost/blood ; Dinoprostone/blood ; Enzyme Inhibitors/pharmacokinetics ; Enzyme Inhibitors/pharmacology ; Female ; Fetal Blood/metabolism ; Gestational Age ; Pentanoic Acids/pharmacokinetics ; Pentanoic Acids/pharmacology ; Placenta/metabolism ; Pregnancy ; Prostaglandins/blood ; Pyridines/pharmacokinetics ; Pyridines/pharmacology ; Sheep ; Thromboxane-A Synthase/antagonists & inhibitors ; Uterine Contraction/drug effects
Chemical Substances	Enzyme Inhibitors ; Pentanoic Acids ; Prostaglandins ; Pyridines ; 6-Ketoprostaglandin F1 alpha (58962-34-8) ; Dinoprost (B7IN85G1HY) ; Thromboxane-A Synthase (EC 5.3.99.5) ; Dinoprostone (K7Q1JQR04M) ; ridogrel (QTS5QOO42O)
Language	English
Publishing date	1999-09
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	190605-7
ISSN	1872-7654 ; 0301-2115 ; 0028-2243
ISSN (online)	1872-7654
ISSN	0301-2115 ; 0028-2243
DOI	10.1016/s0301-2115(99)00044-5
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Article: Modulators of protein kinase C inhibit hypoxia-induced erythropoietin production.

Faquin, W C / Schneider, T J / Goldberg, M A

Experimental hematology

1993 Volume 21, Issue 3, Page(s) 420–426

Abstract: The human hepatoma cell line, Hep 3B, produces biologically active erythropoietin (Epo) in response to normal physiologic stimuli and thus provides a model system for the study of Epo regulation. The addition of phorbol 12-myristate 13-acetate (PMA) to ... ...

Abstract	The human hepatoma cell line, Hep 3B, produces biologically active erythropoietin (Epo) in response to normal physiologic stimuli and thus provides a model system for the study of Epo regulation. The addition of phorbol 12-myristate 13-acetate (PMA) to Hep 3B cells subsequently grown under hypoxic conditions resulted in a dose-dependent inhibition of hypoxia-induced Epo production by as much as 95 +/- 1% with half-maximal inhibition at 8 ng/mL. By Northern blot analysis, Epo mRNA levels were correspondingly decreased after treatment with PMA. Direct measurement of both membrane and cytosolic protein kinase C activity in Hep 3B cells following treatment with PMA demonstrated a biphasic response as a function of time. Membrane-associated protein kinase C activity initially increased but subsequently decreased to baseline levels by 12 hours. The PMA-induced inhibition of hypoxia-induced Epo production was shown to occur as early as 3 hours after PMA addition, suggesting that the initial activation, rather than the subsequent decrease in protein kinase C activity, is of primary importance. The relative specificity of the PMA-induced inhibition of Epo production was demonstrated by 1) the finding that overall protein and RNA synthesis were not similarly decreased as measured by 3H-leucine and 3H-uridine pulse labeling studies and 2) the observation that the biologically inactive phorbol ester, 4 alpha-phorbol didecanoate, failed to have any effect on hypoxia-induced Epo production. In addition, the synthetic analog of diacylglycerol, 1-oleoyl-2-acetylglycerol (OAG) and the calcium ionophore, A23187, inhibited hypoxia-induced Epo production up to 85 +/- 3% and 82 +/- 4%, respectively, in a dose-dependent manner. Taken together, these findings suggest that hypoxia-induced Epo production may be negatively regulated by activators of a protein kinase C-mediated pathway.
MeSH term(s)	Blotting, Northern ; Calcimycin/pharmacology ; Carcinoma, Hepatocellular/metabolism ; Carcinoma, Hepatocellular/pathology ; Carcinoma, Hepatocellular/physiopathology ; DNA/genetics ; DNA/metabolism ; Diglycerides/pharmacology ; Dose-Response Relationship, Drug ; Erythropoietin/genetics ; Erythropoietin/metabolism ; Gene Expression Regulation, Neoplastic/drug effects ; Humans ; Hypoxia/metabolism ; Hypoxia/physiopathology ; Leucine/metabolism ; Liver Neoplasms/metabolism ; Liver Neoplasms/pathology ; Liver Neoplasms/physiopathology ; Protein Kinase C/metabolism ; Protein Kinase C/physiology ; RNA/analysis ; RNA/genetics ; Radioimmunoassay ; Tetradecanoylphorbol Acetate/pharmacology ; Tritium ; Tumor Cells, Cultured ; Uridine/metabolism
Chemical Substances	Diglycerides ; Tritium (10028-17-8) ; Erythropoietin (11096-26-7) ; Calcimycin (37H9VM9WZL) ; RNA (63231-63-0) ; 1-oleoyl-2-acetylglycerol (86390-77-4) ; DNA (9007-49-2) ; Protein Kinase C (EC 2.7.11.13) ; Leucine (GMW67QNF9C) ; Tetradecanoylphorbol Acetate (NI40JAQ945) ; Uridine (WHI7HQ7H85)
Language	English
Publishing date	1993-03
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	185107-x
ISSN	1873-2399 ; 0301-472X ; 0531-5573
ISSN (online)	1873-2399
ISSN	0301-472X ; 0531-5573
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Article: Effect of inflammatory cytokines on hypoxia-induced erythropoietin production.

Faquin, W C / Schneider, T J / Goldberg, M A

Blood

1992 Volume 79, Issue 8, Page(s) 1987–1994

Abstract: The effects of the inflammatory cytokines interleukin-1 alpha (IL-1 alpha), IL-1 beta, IL-6, transforming growth factor-beta (TGF-beta), and tumor necrosis factor-alpha (TNF-alpha) on erythropoietin (Epo) production in Hep3B cells were examined. The ... ...

Abstract	The effects of the inflammatory cytokines interleukin-1 alpha (IL-1 alpha), IL-1 beta, IL-6, transforming growth factor-beta (TGF-beta), and tumor necrosis factor-alpha (TNF-alpha) on erythropoietin (Epo) production in Hep3B cells were examined. The addition of IL-1 alpha, IL-1 beta, or TNF-alpha resulted in a dose-dependent inhibition of hypoxia-induced Epo production by as much as 89%. IL-1 beta was the most effective cytokine tested, demonstrating half-maximal inhibition at 0.4 U/mL compared with 1.0 and 10.0 U/mL for IL-1 alpha and TNF-alpha, respectively. TGF-beta also inhibited hypoxia-induced Epo production, but only by as much as 56%. In contrast to IL-1 alpha, IL-1 beta, TNF-alpha, and TGF-beta, the addition of IL-6 to hypoxic Hep3B cells resulted in a dose-dependent stimulation of hypoxia-induced Epo production by as much as 81%. However, IL-6 did not stimulate Epo synthesis in the absence of hypoxia, and was thus synergistic with hypoxia in inducing Epo production. Combinations of IL-1 alpha, TNF-alpha, and IL-6 were found to be additive in their effects on hypoxia-induced Epo production. By Northern blot analysis, Epo messenger RNA levels in Hep3B cells grown in 1% O2 were decreased when concurrently exposed to either IL-1 alpha or TNF-alpha. The effects that IL-1 alpha, IL-1 beta, TGF-beta, TNF-alpha, and IL-6 have on hypoxia-induced Epo production may provide new insights into the signal transduction pathway by which hypoxia leads to changes in gene expression. In addition, the effects of these inflammatory cytokines on hypoxia-induced Epo production in vitro suggest that in various inflammatory disorders these cytokines may affect Epo production in vivo and may play a significant role in the pathogenesis of the anemia of chronic disease.
MeSH term(s)	Blotting, Northern ; Cell Hypoxia ; Cell Line ; Cytokines/pharmacology ; Dose-Response Relationship, Drug ; Erythropoietin/biosynthesis ; Erythropoietin/genetics ; Humans ; Inflammation ; Interleukin-1/pharmacology ; Interleukin-6/pharmacology ; Kinetics ; Protein Biosynthesis ; RNA/biosynthesis ; RNA/genetics ; RNA/isolation & purification ; Radioimmunoassay ; Recombinant Proteins/pharmacology ; Transforming Growth Factor beta/pharmacology ; Tritium ; Tumor Necrosis Factor-alpha/pharmacology
Chemical Substances	Cytokines ; Interleukin-1 ; Interleukin-6 ; Recombinant Proteins ; Transforming Growth Factor beta ; Tumor Necrosis Factor-alpha ; Tritium (10028-17-8) ; Erythropoietin (11096-26-7) ; RNA (63231-63-0)
Language	English
Publishing date	1992-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	80069-7
ISSN	1528-0020 ; 0006-4971
ISSN (online)	1528-0020
ISSN	0006-4971
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Uh III Zs.140: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article: An alternatively spliced long form of Fas apoptosis inhibitory molecule (FAIM) with tissue-specific expression in the brain.

Zhong, X / Schneider, T J / Cabral, D S / Donohoe, T J / Rothstein, T L

Molecular immunology

2001 Volume 38, Issue 1, Page(s) 65–72

Abstract: The gene encoding Fas apoptosis inhibitory molecule (FAIM) was cloned by differential display using RNA obtained from Fas-resistant and Fas-sensitive primary murine B lymphocytes. FAIM is highly evolutionarily conserved and broadly expressed, suggesting ... ...

Abstract	The gene encoding Fas apoptosis inhibitory molecule (FAIM) was cloned by differential display using RNA obtained from Fas-resistant and Fas-sensitive primary murine B lymphocytes. FAIM is highly evolutionarily conserved and broadly expressed, suggesting that its gene product plays a key role in cellular physiology. Here we report the identification of a new, longer form of FAIM (FAIM-L) and characterization of the genomic locus that clarifies its origin. The murine FAIM gene is located at chromosome 9f1, a region syntenic to the corresponding location of the human FAIM gene. The gene consists of six exons and contains putative translation initiation sites within exons II and III. The long form of FAIM is generated by all six exons, whereas the originally cloned form of FAIM, now termed FAIM-Short (FAIM-S) is generated from five exons by alternative splicing. FAIM-L is dominantly expressed in the brain whereas FAIM-S is widely expressed in many tissues.
MeSH term(s)	Alternative Splicing ; Amino Acid Sequence ; Animals ; Apoptosis ; Apoptosis Regulatory Proteins ; Brain/metabolism ; Chromosome Mapping ; Gene Expression ; Humans ; Mice ; Molecular Sequence Data ; Protein Isoforms/genetics ; Proteins/genetics ; fas Receptor
Chemical Substances	Apoptosis Regulatory Proteins ; FAIM protein, human ; Faim protein, mouse ; Protein Isoforms ; Proteins ; fas Receptor
Language	English
Publishing date	2001-05-14
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	424427-8
ISSN	1872-9142 ; 0161-5890
ISSN (online)	1872-9142
ISSN	0161-5890
DOI	10.1016/s0161-5890(01)00035-9
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Article: Placental transfer and maternal and fetal hemodynamic effects of ketanserin in the pregnant ewe.

Schneider, T J / Struijk, P C / Lotgering, F K / Wallenburg, H C

European journal of obstetrics, gynecology, and reproductive biology

1996 Volume 68, Issue 1-2, Page(s) 179–184

Abstract: Objective: To determine placental transfer of ketanserin and to assess the effect of serotonin-2 receptor blockade by ketanserin on serotonin- and phenylephrine-induced vasoconstriction.: Study design: Five chronically instrumented pregnant ewes at ... ...

Abstract	Objective: To determine placental transfer of ketanserin and to assess the effect of serotonin-2 receptor blockade by ketanserin on serotonin- and phenylephrine-induced vasoconstriction. Study design: Five chronically instrumented pregnant ewes at 120 days gestation were injected with 20 mg ketanserin i.v., and fetal and maternal arterial samples were obtained at predetermined intervals to assess placental transfer. Maternal and fetal responses of blood flows and pressures were determined after injected of serotonin (20 micrograms/kg) or phenylephrine (10 micrograms/kg) before and after ketanserin (0.75 mg/kg). Results: In the ewe, ketanserin is transferred across the placenta and reaches measurable levels in the fetal lamb. Ketanserin blocks the maternal and fetal serotonin-induced rise in arterial pressure, but not the serotonin-induced reduction in uterine blood flow. Conclusion: In the pregnant ewe, the serotonin-induced rise in maternal and fetal blood pressure is effectively antagonized by ketanserin, whereas the serotonin-induced reduction in uterine blood flow is not.
MeSH term(s)	Adrenergic alpha-Antagonists/pharmacology ; Animals ; Female ; Fetus/blood supply ; Half-Life ; Hemodynamics/drug effects ; Hydrogen-Ion Concentration ; Ketanserin/pharmacokinetics ; Ketanserin/pharmacology ; Maternal-Fetal Exchange ; Phenylephrine/pharmacology ; Placenta/metabolism ; Pregnancy ; Receptors, Adrenergic, alpha/physiology ; Receptors, Serotonin/physiology ; Serotonin Antagonists/pharmacology ; Sheep
Chemical Substances	Adrenergic alpha-Antagonists ; Receptors, Adrenergic, alpha ; Receptors, Serotonin ; Serotonin Antagonists ; Phenylephrine (1WS297W6MV) ; Ketanserin (97F9DE4CT4)
Language	English
Publishing date	1996-09
Publishing country	Ireland
Document type	Journal Article
ZDB-ID	190605-7
ISSN	1872-7654 ; 0301-2115 ; 0028-2243
ISSN (online)	1872-7654
ISSN	0301-2115 ; 0028-2243
DOI	10.1016/0301-2115(96)02478-5
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Article: A novel gene coding for a Fas apoptosis inhibitory molecule (FAIM) isolated from inducibly Fas-resistant B lymphocytes.

Schneider, T J / Fischer, G M / Donohoe, T J / Colarusso, T P / Rothstein, T L

The Journal of experimental medicine

1999 Volume 189, Issue 6, Page(s) 949–956

Abstract: The sensitivity of primary splenic B cells to Fas-mediated apoptosis is modulated in a receptor-specific fashion. Here we used a differential display strategy to detect cDNAs present in B cells rendered Fas resistant but absent in those rendered Fas ... ...

Abstract	The sensitivity of primary splenic B cells to Fas-mediated apoptosis is modulated in a receptor-specific fashion. Here we used a differential display strategy to detect cDNAs present in B cells rendered Fas resistant but absent in those rendered Fas sensitive. This led to the cloning and characterization of a novel 1.2-kb gene that encodes a Fas apoptosis inhibitory molecule (FAIM). faim-transfected BAL-17 B lymphoma cells were less sensitive by half or more to Fas-mediated apoptosis than were vector-transfected controls, using Fas ligand-bearing T cells or a cytotoxic anti-Fas antibody to trigger Fas, and this was associated with inhibition of Fas- induced poly-ADP ribose polymerase (PARP) cleavage. In primary B cells, the time course of faim mRNA and FAIM protein expression correlated with the induction of Fas resistance by surface (s)Ig engagement. Thus, FAIM is an inducible effector molecule that mediates Fas resistance produced by sIg engagement in B cells. However, faim is broadly expressed in various tissues and the faim sequence is highly conserved evolutionarily, suggesting that its role extends beyond lymphocyte homeostasis. As FAIM has no significant regions of homology to other gene products that modulate Fas killing, it appears to represent a distinct, new class of antiapoptotic protein.
MeSH term(s)	Amino Acid Sequence ; Animals ; Apoptosis/drug effects ; B-Lymphocytes/metabolism ; Conserved Sequence ; DNA, Complementary/isolation & purification ; Male ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Poly(ADP-ribose) Polymerases/metabolism ; fas Receptor/physiology
Chemical Substances	DNA, Complementary ; fas Receptor ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
Language	English
Publishing date	1999-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.189.6.949
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Article: Clinical validation of an RIA for natural and recombinant erythropoietin in serum and plasma.

Goldberg, M A / Schneider, T J / Khan, S / Petersen, J R

Clinical biochemistry

1993 Volume 26, Issue 3, Page(s) 183–189

Abstract: A sensitive radioimmunoassay (RIA) for the detection of erythropoietin (EPO) was developed using antibody directed against EPO from human urine. With 100 microL of sample, the assay is sensitive to 7 U/L, well below the mean EPO level in normal males (15. ...

Abstract	A sensitive radioimmunoassay (RIA) for the detection of erythropoietin (EPO) was developed using antibody directed against EPO from human urine. With 100 microL of sample, the assay is sensitive to 7 U/L, well below the mean EPO level in normal males (15.1 +/- 3.5 U/L) or females (15.4 +/- 4.8 U/L). Dilutions of a variety of human serum samples show a parallel relationship with the standard EPO. Clinical validation of the RIA was confirmed by appropriate increases or decreases of EPO levels in various types of anemia and polycythemia. Serum EPO levels were also measured in volunteers participating in an autologous blood donation study. The RIA proved to be quite sensitive, detecting small increases even after a single unit phlebotomy. This RIA of human EPO meets all the requirements of a routine clinical assay in terms of specificity and clinical sensitivity and can be easily conducted in routine clinical laboratories.
MeSH term(s)	Erythropoietin/blood ; Female ; Hematologic Diseases/blood ; Humans ; Kidney Failure, Chronic/blood ; Male ; Radioimmunoassay ; Recombinant Proteins/blood ; Reference Values ; Sensitivity and Specificity
Chemical Substances	Recombinant Proteins ; Erythropoietin (11096-26-7)
Language	English
Publishing date	1993-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	390372-2
ISSN	0009-9120
ISSN	0009-9120
DOI	10.1016/0009-9120(93)90024-z
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In stock of ZB MED Cologne/Königswinter

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