O.T.T. Scientific Data Sheet and Summary
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Dr. Ott’s Oxygen (O2) Treatment and Therapy™
Scientific Data Sheet and Summary
By A. True Ott, PhD, ND
To fully understand the incredible function of the Oxygen Treatment and Therapy in the human body, the practitioner, health care professional, and/or inquisitive lay person needs to familiarize themselves with the functions of a cellular enzyme called Myeloperoxidase (aka MPO for short), as well as the functions of hypochlorous acid (HCLO).
In the early 1920’s, Dr. William F. Koch discovered that all disease states are merely different manifestations of OXYGEN DEFICIENCIES at the cellular level. He called these oxygen deficiencies the “Least Common Denominator” in maintaining good health, which is of course synonymous with PREVENTING disease states from forming in the first place. Therefore, proper oxygenation via all-natural mineral precursors should be the 1st and primary goal of cellular nutrition advocates as well.
As a gifted bio-chemist, Dr. Koch discovered that combining certain carbonyl-group mineral elements in vitro quickly produced a unique form of hypochlorous acid that he named “glyoxilide”. I submit he named this catalyst glyoxilide because when it came in contact with the carbons in GLUCOSE (aka blood sugar) in vivo (in the body) – massive amounts of singlet, negatively charged oxygen molecules were produced. In turn, these oxygen molecules proved to be highly effective in eliminating anaerobic pathogens (harmful bacteria, viruses, fungi and parasites) from the body in a completely safe, non-obtrusive, and effective manner.
In 1925, Dr. Edward Carl Rosenow (who spent over 60 years conducting research at the Mayo Clinic) not only discovered that rheumatic fever was caused by a streptococcus germ – but that there are literally millions of tiny micro-organisms continually living and colonizing in the human body. Each different strain of “bug” causes different problems and health challenges. Some colonize in the hair and scalp resulting in dandruff. Others colonize in the mouth causing cavities and gum diseases.
Dr. Rosenow found that individuals with compromised immune systems were consistently low in blood oxygen. In turn, these microscopic critters would proliferate and be free to do such nasty things as: 1) consume the cartilage and sulfur of the joints causing painful rheumatoid arthritis 2) excrete waste material in the form of electron-deficient calcium that hardens bones and makes them brittle – and when lodged in the liver and kidneys would form stones 3) colonize in the lining of the heart arteries, leaving their excrement on the walls of the arteries in the form of plaque. 4) colonize in the Central Nervous System (CNS) of the spinal column and brain, making meals of the myelin sheath nerve coatings thus short-circuiting the central computer of the brain resulting in ALS, MS, ADHD, and Alzheimer’s. 5) attack individual cells and enter the cellular membrane, eventually building cocoons around the DNA-damaged cell; cutting off the oxygen-carrying blood so that the cell can only live and function as part of cancerous tumor. Thus, it is safe to say that disruption of the ability of the cells to produce MPO, HClO, and “glyoxilide” results in low oxygen levels, which in turn eventually forms a DISEASE STATE.
Dr. Koch quickly learned that such a simple formula providing powerful, life-giving OXYGEN to the cell would not only prevent disease states from forming, but had the strong potential to REVERSE so-called “incurable” disease states as well. So, like any honest medical professional, Dr. Koch proceeded to test his research and theory – and the results were immediate and dramatic to say the least. Cancer tumors shrunk and disappeared, diabetes mellitus vanished, mental disorders reversed, and viral plagues were eliminated. (See www.williamfkoch.com)
Sadly, however, Dr. Koch also became painfully aware that reversing such chronic disease states in such a permanent manner meant drastically decreased PROFITS in the bank accounts of the burgeoning PHARMACEUTICAL HOUSES owned and operated primarily by John D. Rockefeller. It meant that in order for “Big Pharma” to flourish, Dr. Koch’s research and results must be hidden and discredited at all costs. This is exactly what happened – and this vitally important NUTRITIONAL PRODUCT was lost to the world for over 50 years. Untold millions have needlessly suffered and died horrible deaths in order to enrich a few evil men.
In simple, honest words, the O.T.T. (Oxygen Treatment and Therapy) produces the mineral catalyst that Dr. Koch named “glyoxilide”. When taken as instructed, the O.T.T. mineral catalyst is completely non-toxic and safe. When the catalyst is absorbed into the bloodstream and encounters carbon/glucose molecules, large amounts of OXYGEN is indeed created, and harmful NITROGEN is reduced. In turn, the free oxygen destroys anaerobic bacteria, viruses, yeast, and parasites the way NATURE intended – through the mechanism of OXIDATION in much the same way as OZONE IN WATER destroys the same harmful pathogens.
For those wishing to have more “3rd party” validation of this science and my claims, I am including a paper authored by Dr. Maureen Petersen, MD, Cecilia Mikita, MD, MPH, and Javed Sheikh, MD on a condition called Myeloperoxidase (MPO) Deficiency, (but what should actually be called serum oxygen deficiency) and Wikipedia’s detailed report on hypochlorous acid. I have highlighted in yellow the more relevant parts.
A. True Ott, PhD, ND
February 20, 2009
Maureen M Petersen, MD, Fellow in Allergy and Immunology, Walter Reed Army Medical Center
Cecilia P Mikita, MD, MPH, Assistant Professor of Pediatrics and Medicine, Uniformed Services University of the Health Sciences; Associate Program Director of Allergy-Immunology Fellowship, Chief of Clinical Services, Staff Allergist/Immunologist, Walter Reed Army Medical Center; Javed Sheikh, MD, Assistant Professor of Medicine, Harvard Medical School; Clinical Director, Division of Allergy and Inflammation, Beth Israel Deaconess Medical Center; Clinical Director, Center for Eosinophilic Disorders, Beth Israel Deaconess Medical Center
Updated: Oct 29, 2008
Myeloperoxidase (MPO) is a human enzyme in the azurophilic granules of neutrophils and in the lysosomes of monocytes. Its major role is to aid in microbial killing. Although MPO received little clinical attention until 1966, the enzyme was first isolated in 1941, and deficiency of MPO was first described in 1954. Some patients with MPO deficiency have impaired microbial killing, but most are asymptomatic.
The condition was initially believed to be very rare with only 15 cases were reported before the 1970s. However, modern laboratory techniques have allowed researchers to discover that MPO deficiency is actually more common than previously described but without clinical relevance.
Normal function of myeloperoxidase
MPO, a heme-containing protein, is found in the azurophilic granules of neutrophils and in the lysosomes of monocytes in humans; however, monocytes contain only about a third of the MPO present in neutrophils. When neutrophils become activated during phagocytosis, they undergo a process referred to as a respiratory burst. This respiratory burst causes production of superoxide, hydrogen peroxide, and other reactive oxygen derivatives, which are all toxic to microbes. During respiratory bursts, granule contents are released into the phagolysosomes and outside the cell, allowing released contents to come into contact with any microbes present. Experiments conducted in the 1960s showed that MPO catalyzes the conversion of hydrogen peroxide and chloride ions (Cl) into hypochlorous acid.1 Hypochlorous acid is 50 times more potent in microbial killing than hydrogen peroxide.
MPO also directly chlorinates phagocytosed bacteria; thus, the MPO-hydrogen peroxide-Cl system seems to have an important role in microbial killing. Although the exact mechanism by which microbial killing occurs is controversial, researchers are fairly certain that MPO is important for the process to optimally occur.
In addition to killing bacteria, the products of the MPO-hydrogen peroxide-Cl system are believed to play a role in killing fungi, parasites, protozoa, viruses, tumor cells, natural killer (NK) cells, red cells, and platelets. The MPO-hydrogen peroxide-Cl system is also believed to be involved in terminating the respiratory burst, because individuals with MPO deficiency have prolonged respiratory bursts. It may play a role in downregulating the inflammatory response by regulating NK cells, decreasing peptide binding to chemotactic receptors, and auto-oxidizing and inactivating products of polymorphonuclear leukocytes (PMNs), such as a1-proteinase inhibitor and chemotaxins.
Other functions of MPO include tyrosyl radical production and chlorination, generation of tyrosine peroxide, mediation of the adhesion of myeloid cells via b2-integrins, and oxidation of serum lipoproteins. MPO may have a role in atherosclerosis. Researchers have demonstrated that patients with stable coronary artery disease had an increased cardiovascular risk if plasma MPO levels were elevated.2 A small study demonstrated that MPO deficiency may protect against cardiovascular disease.3 MPO may also have a role in carcinogenesis and degenerative neurological diseases. The understanding of MPO biology remains incomplete; much more remains to be discovered.
Normal myeloperoxidase production
MPO is a dimeric molecule, consisting of a pair of heavy-chain and light-chain protomers and 2 iron atoms. MPO is encoded by a single gene located on band 17q22-23. The mature enzyme is synthesized from a single polypeptide product. Therefore, the expression of the gene and the synthesis of MPO primarily occurs during the promyelocytic stage of myeloid development, concurrent with development of the azurophilic granules. The MPO gene encodes for a primary translational product, which is glycosylated to yield an enzymatically inactive precursor, apopro-MPO.
Apopro-MPO reversibly binds to chaperone proteins, calreticulin and calnexin, during protein maturation. This results in the subsequent binding of heme.4 Heme insertion induces conformational changes in the protein yielding pro-MPO, an enzymatically active precursor.5 Pro-MPO undergoes several complex conversions and eventually becomes mature MPO in the azurophilic granules, but the exact mechanisms are still poorly understood.
MPO should be distinguished from eosinophilic peroxidase (EPO), a different enzyme produced by a different gene. Although patients with MPO deficiency have decreased MPO activity in the neutrophils and monocytes, these patients usually have normal levels of EPO in eosinophils.
Pathophysiology of hereditary myeloperoxidase deficiency
Hereditary MPO deficiency was initially thought to follow the classic autosomal recessive pattern. A number of genetic mutations resulting in MPO deficiency have been identified, and many others may still be undiscovered. Researchers now believe that most patients are compound heterozygotes, which means that they have a different mutation on each allele, one from each parent. As with several other genetic diseases, numerous allele combinations can lead to the phenotype of MPO deficiency, which partially explains the variability of clinical features. Some mutations result in posttranslational defects; others (which are not yet clearly defined) seem to cause pretranslational defects, possibly due to structural alterations in the regulatory parts of the MPO gene. See Causes for a discussion of individual mutations that have been identified and their effects.
Some authors have proposed a bigenic model involving the interaction of 2 genes, such as a production gene and a regulatory gene. Overall, the genetic basis of this condition is now thought to be quite heterogeneous and complex. Undoubtedly, much remains to be discovered.
Pathophysiology of acquired myeloperoxidase deficiency
MPO deficiency in acquired cases is usually transient and generally resolves once the inciting condition improves. In addition, acquired MPO deficiency is usually partial and involves only a fraction of the PMNs.6 The following conditions can lead to acquired MPO deficiency:
- Lead intoxication - Inhibits heme synthesis (a component of mature MPO)
- Iron deficiency
- Severe infection - Secondary to PMN activation and "consumption" of MPO
- Thrombotic diseases
- Renal transplantation
- Diabetes mellitus
- Neuronal lipofuscinosis
- Drugs - Cytotoxic agents and some anti-inflammatory agents such as dapsone, 5-aminosalicylic acid, and sulfapyridine
- Disseminated cancers - Probably related to administration of cytostatic agents
- Several hematologic disorders and neoplasms especially those involving the maturation of granulocytes:
- Acute myeloid leukemia (AML)
- Chronic myeloid leukemia (CML)
- Polycythemia vera
- Hodgkin disease
- Refractory megaloblastic anemia
- Aplastic anemia
- Myelofibrosis with myeloid metaplasia
- Myelodysplastic syndromes
Microbial killing in myeloperoxidase deficiency
MPO-deficient neutrophils are normally able to phagocytose most microbes. However, the ability of MPO-deficient neutrophils to kill bacteria seems impaired to varying degrees. For organisms such as Staphylococcus aureus, Serratia species, and Escherichia coli, killing is initially impaired but then reaches normal levels after a period of time. This suggests that an apparently slower, alternative mechanism of killing can take over in MPO-deficient neutrophils.
The capacity to kill certain fungi, however, seems completely absent in MPO-deficient neutrophils. In vitro studies have shown that Candida albicans, Candida krusei, Candida stellatoidea, and Candida tropicalis cannot be killed by MPO-deficient PMNs. In contrast, an MPO-independent mechanism can kill Candida glabrata, Candida parapsilosis, and Candida pseudotropicalis. Even more interesting is that the hyphal elements of Aspergillus fumigatus and C albicans cannot be killed, but the spores of A fumigatus and the yeast phase of C albicans can be killed by an independent mechanism. This leads to the conclusion that bacterial killing may not necessarily be a problem for patients with MPO deficiency, but the killing of certain fungi may be a problem, depending on the severity of the deficiency.
Incidence rates from screening studies range from 1 case per 1400-2000 population.
One series found the prevalence of total or subtotal MPO deficiency to be 1 case per 2727 population.7 Prevalence rates in Japan have been reported to be much lower, with one study finding the prevalence of total and partial deficiency to be 1 case per 57,135 population and 1 case per 17,501 population, respectively.8
Until the 1970s, only 15 cases of MPO deficiency had been reported worldwide. Because most cases are asymptomatic, very few people were evaluated for the deficiency. However, modern laboratory techniques, particularly the wider application of automated flow cytometry for determining WBC differentials, have allowed the screening of large study populations to determine the true prevalence of MPO deficiency.7
European researchers evaluated patients with complete MPO deficiency and found that about half of the patients had infectious complications; the other half were asymptomatic. Approximately 10% of the cases involved life-threatening infectious complications. Other studies have reported that severe infections occur in fewer than 5% of patients with MPO deficiency; however, this frequency may be based on the inclusion of both complete and partial deficiencies. Generally, infections only occur in patients who have concomitant diabetes mellitus.
- Recurrent infections
- Most individuals with partial or total myeloperoxidase (MPO) deficiency have no increased frequency of infections, probably because MPO-independent mechanisms in the polymorphonuclear leukocytes (PMNs) can take over. In general, it is considered a relatively benign immunodeficiency and was removed from the Classification of Primary Immunodeficiency Disease by the Primary Immunodeficiency Disease Classification Committee of the International Union of the Immunologic Societies in 2005.
- Severe infections are uncommon, occurring in fewer than 5% of patients with MPO deficiency. If infectious disease occurs, it is usually a fungal infection (particularly candidal, such as C albicans or C tropicalis) that occurs in a patient who also has diabetes mellitus. Patients without diabetes mellitus rarely have problems, although the reason for this is unknown. Possibly, MPO deficiency becomes clinically significant only in the presence of an additional defect in the host defense, or perhaps the MPO-independent system is defective in some patients with diabetes mellitus.
- Physicians should entertain the diagnosis of MPO deficiency in cases of invasive fungal infection in a patient with no known predisposing immune defects (eg, chemotherapy, corticosteroid treatment) or in a patient with concomitant diabetes mellitus. Some consider peroxidase staining of the peripheral blood smear to be part of the complete evaluation of a patient with a suspected immunodeficiency.
- Increased incidence of malignancy
- A strong association between total MPO deficiency and malignancies has been reported by several independent investigators. In vitro, MPO-deficient neutrophils have decreased destruction of malignant cells demonstrating that the MPO system plays a central role in tumor surveillance.6
- MPO is released from neutrophils in lung tissue in response to pulmonary insult including damage secondary to tobacco smoke exposure. MPO has been shown to convert the metabolites of benzo[a]pyrene from tobacco smoke into a highly reactive carcinogen. Researchers have demonstrated that decreased MPO can decrease lung cancer risk.9
- Hereditary cases can be caused by a number of mutations, including R569W, Y173C, M251T, G501S, and R499C.
- R569W: This is the most common defect identified to date. Tryptophan is substituted for arginine at codon 569. Tryptophan cannot form electrostatic bonds. Most patients described have been compound heterozygotes, but one has been homozygous for this mutation. The mutation results in a maturational arrest at the stage of apopro-MPO that is unprocessed, enzymatically inactive, and undelivered to the azurophilic granules.10
- Y173C: Cysteine is substituted for tyrosine at codon 173. This leads to an additional site for intramolecular disulfide bonds, which presumably leads to abnormal folding of the protein. Apopro-MPO is converted into pro-MPO, which is malfolded. This malfolded pro-MPO seems to be sequestered by calnexin (a molecular chaperone) and retained in the endoplasmic reticulum. The trapped precursor then undergoes degradation in the endoplasmic reticulum. Pro-MPO is prevented from entering the secretory pathway and cannot proceed to become mature MPO in the azurophilic granules. Therefore, MPO deficiency resulting from this mutation occurs because of an abnormality of protein folding. Interestingly, abnormalities in protein folding have also been described in cystic fibrosis and protein C deficiency.
- M251T: In this defect, mature subunits are formed, but their enzymatic activity is markedly low.
- G501S: This mutation is a missense mutation within part of the heme-binding pocket. It has been identified in a Japanese patient with complete MPO deficiency.11
- R499C: This mutation is a nonsynonymous mutation that results in an arginine to cysteine substitution in the exon 9 coding region. The mutation was identified in a Japanese patient with complete MPO deficiency. Further genetic analysis revealed mRNA was transcribed into an appropriate peptide sequence, but no MPO protein was evident on Western blot findings.12
- As time goes on and more cases are analyzed, more mutations are being identified. Some pretranslational defects have been described that could be caused by mutations in the regulatory portion of the MPO gene or by the presence of mutations in other genes involved in the regulation of the MPO gene.
- Acquired MPO deficiency is less common than the hereditary form. This condition can be transient. The enzyme defect is corrected when the underlying condition has resolved. In most cases of acquired deficiency, the deficiency is partial and affects only a proportion of neutrophils (see Pathophysiology).
Chronic Granulomatous Disease
Glycogen-Storage Disease Type I
Hyperimmunoglobulinemia E (Job) Syndrome
Leukocyte Adhesion Deficiency
Other Problems to Be Considered
Neutropenia (of any cause)
Neutrophil actin dysfunction
Specific granule deficiency
Lazy leukocyte syndrome
Any of the conditions that can cause acquired (secondary) myeloperoxidase (MPO) deficiency
- The presence of myeloperoxidase (MPO) can be determined using numerous techniques, including histochemical staining, immunocytochemistry, and flow cytometry. Depending on the assay used, one must ensure that eosinophilic peroxidase (EPO) from eosinophils does not cause false-positive results.
- The easiest technique is to perform direct visualization of neutrophils on a peripheral blood smear that has been stained for peroxidase. The clinician can ask the pathologist to examine the neutrophils for peroxidase when a peripheral smear is requested.13
- Dihydrorhodamine 123 (DHR) assay, a flow cytometric assay, is often used to measure the presence of reactive oxygen intermediates in the work-up of a patient with suspected immunodeficiency. This assay is easier, more reliable, and more sensitive than nitroblue tetrazolium dye reduction assay in the diagnosis of chronic granulomatous disease (CGD). At this time, a DHR assay should not be used as a screen for MPO deficiency because of variable results and poor sensitivity in detecting partial MPO deficiency. If a DHR assay is consistent with a diagnosis of CGD but the clinical history is more consistent with MPO deficiency, further laboratory testing should be performed (eg, genetic sequencing or intracellular staining with anti-MPO antibody).14
In general, routine treatment with prophylactic antibiotics is not recommended because most patients with myeloperoxidase (MPO) deficiency have no increased incidence of infections.
- Exercise caution in patients with concomitant diabetes mellitus. If infection does occur, initiate prompt and aggressive treatment with antimicrobials. Every effort should be made to identify causative agents and administer specific antimicrobial therapy.
- If possible, avoid any treatments that might increase the likelihood of developing fungal infection (eg, use of broad-spectrum antibiotics, prolonged courses of antibiotics).
See Medical Care.
Inpatient & Outpatient Medications
- A group from Europe who studied patients with complete myeloperoxidase (MPO) deficiency found that about half had infectious complications, while the other half were asymptomatic. Infectious complications were life threatening in about 10% of cases.
- Others have reported severe infections occurring in fewer than 5% of patients with MPO deficiency (this frequency may be based on the inclusion of both complete and partial deficiencies). Infections generally occur only in patients who have concomitant diabetes mellitus.
- Because most patients with myeloperoxidase (MPO) deficiency do not have serious or life-threatening infections, failure to diagnose MPO deficiency may have no adverse consequences. Indeed, because at least half of patients with MPO deficiency are asymptomatic, most cases are undiagnosed. However, failure to make the diagnosis in a patient with MPO deficiency with recurrent serious infections could lead to medicolegal consequences.
- If an infectious disease occurs in a patient with MPO deficiency who also has diabetes mellitus, it is usually a fungal infection (particularly candidal species such as C albicans or C tropicalis). Patients without diabetes mellitus rarely have problems. Consider the possibility of MPO deficiency in a case of invasive fungal infection in a patient with no known predisposing immune defects (eg, chemotherapy, corticosteroid treatment) or in a patient with concomitant diabetes mellitus.
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2. Stefanescu A, Braun S, Ndrepepa G, et al. Prognostic value of plasma myeloperoxidase concentration in patients with stable coronary artery disease. Am Heart J. Feb 2008;155:356-360. [Medline].
3. Kutter D, Devaquet P, Vanderstocken G, et al. Consequences of total and subtotal myeloperoxidase deficiency: risk or benefit?. Acta Haematol. 2000;104(1):10-5. [Medline].
4. Nauseef WM. Insights into myeloperoxidase biosynthesis from its inherited deficiency. J Mol Med. Sep 1998;76(10):661-8. [Medline].
5. Nauseef WM. Lessons from MPO deficiency about functionally important structural features. Jpn J Infect Dis. Oct 2004;57(5):S4-5. [Medline].
6. Lanza F. Clinical manifestation of myeloperoxidase deficiency. J Mol Med. Sep 1998;76(10):676-81. [Medline].
7. Kutter D. Prevalence of myeloperoxidase deficiency: population studies using Bayer-Technicon automated hematology. J Mol Med. Sep 1998;76(10):669-75. [Medline].
8. Nunoi H, Kohi F, Kajiwara H, Suzuki K. Prevalence of inherited myeloperoxidase deficiency in Japan. Microbiol Immunol. 2003;47(7):527-31. [Medline].
9. Taioli E, Benhamou S, Bouchardy C, et al. Myeloperoxidase G463A polymorphism and lung cancer: a HuGE genetic susceptibility to environmental carcinogens pooled analysis. Genet Med. Feb 2007;9:67-73. [Medline].
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11. Ohashi YY, Kameoka Y, Persad AS, et al. Novel missense mutation found in a Japanese patient with myeloperoxidase deficiency. Gene. Mar 3 2004;327(2):195-200. [Medline].
12. Persad AS, Kameoka Y, Kanda S, Niho Y, Suzuki K. Arginine to cysteine mutation (R499C) found in a Japanese patient with complete myeloperoxidase deficiency. Gene Expr. 2006;13(2):67-71. [Medline].
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14. Mauch L, Lun A, O'Gorman MRG, et al. Chronic granulomatous disease (CGD) and complete myeloperoxidase deficiency both yield strongly reduced dihydrorhodamine 123 test signals but can be easily discerned in routine testing for CGD. Clin Chem. Mar 2007;53:890-896. [Medline].
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20. Molin L, Stendahl O. The effect of sulfasalazine and its active components on human polymorphonuclear leukocyte function in relation to ulcerative colitis. Acta Med Scand. 1979;206(6):451-7. [Medline].
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25. Petrides PE. Molecular genetics of peroxidase deficiency. J Mol Med. Sep 1998;76(10):688-98. [Medline].
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myeloperoxidase deficiency, MPO, MPO deficiency, lead toxicity, iron deficiency, diabetes mellitus, renal transplantation, acute myeloid leukemia, AML, chronic myeloid leukemia, CML, polycythemia vera, Hodgkin disease, Hodgkin's disease, refractory megaloblastic anemia, aplastic anemia, myelofibrosis with myeloid metaplasia, myelodysplastic syndrome, Staphylococcus aureus, Serratia, Escherichia coli, Candida albicans, Candida krusei, Candida stellatoidea, Candida tropicalis, atherosclerosis
Contributor Information and Disclosures
Maureen M Petersen, MD, Fellow in Allergy and Immunology, Walter Reed Army Medical Center
Maureen M Petersen, MD is a member of the following medical societies: American Academy of Allergy Asthma and Immunology, American Academy of Pediatrics, American College of Allergy, Asthma and Immunology, American Thoracic Society, and Clinical Immunology Society
Disclosure: Nothing to disclose
Cecilia P Mikita, MD, MPH, Assistant Professor of Pediatrics and Medicine, Uniformed Services University of the Health Sciences; Associate Program Director of Allergy-Immunology Fellowship, Chief of Clinical Services, Staff Allergist/Immunologist, Walter Reed Army Medical Center
Cecilia P Mikita, MD, MPH is a member of the following medical societies: American Academy of Allergy Asthma and Immunology, American Academy of Pediatrics, American College of Allergy, Asthma and Immunology, and Clinical Immunology Society
Disclosure: Nothing to disclose
Javed Sheikh, MD, Assistant Professor of Medicine, Harvard Medical School; Clinical Director, Division of Allergy and Inflammation, Beth Israel Deaconess Medical Center; Clinical Director, Center for Eosinophilic Disorders, Beth Israel Deaconess Medical Center
Javed Sheikh, MD is a member of the following medical societies: American Academy of Allergy Asthma and Immunology and American College of Allergy, Asthma and Immunology
Disclosure: UCB Honoraria for Speaking and teaching; Sanofi-Aventis Honoraria for Speaking and teaching; GlaxoSmithKline Grant/research funds for Clinical Trial funding; GlaxoSmithKline Consulting fee for Review panel membership; Novartis Honoraria for Speaking and teaching; Genentech Honoraria for Speaking and teaching; MedPointe Pharmaceuticals Honoraria for Speaking and teaching
C Lucy Park, MD, Director, Allergy and Asthma Center, Associate Professor, Department of Pediatrics, University of Illinois at Chicago
C Lucy Park, MD is a member of the following medical societies: American Academy of Allergy Asthma and Immunology, American Academy of Pediatrics, American Medical Association, Clinical Immunology Society, and Illinois State Medical Society
Disclosure: Nothing to disclose
Mary L Windle, PharmD, Adjunct Assistant Professor, University of Nebraska Medical Center College of Pharmacy, Pharmacy Editor, eMedicine
Disclosure: Pfizer Inc Stock for Investment from broker recommendation; Avanir Pharma Stock for Investment from broker recommendation
David J Valacer, MD, Consulting Staff, Hoffman La Roche Pharmaceuticals
David J Valacer, MD is a member of the following medical societies: American Academy of Allergy Asthma and Immunology, American Academy of Pediatrics, American Association for the Advancement of Science, American Thoracic Society, and New York Academy of Sciences
Disclosure: Nothing to disclose
David Pallares, MD, Clinical Assistant Professor, Department of Pediatrics, Division of Allergy and Immunology, University of Louisville
David Pallares, MD is a member of the following medical societies: American Academy of Allergy Asthma and Immunology
Disclosure: Nothing to disclose
Harumi Jyonouchi, MD, Associate Professor, Division of Pulmonary Allergy/Immunology and Infectious Diseases, Department of Pediatrics, UMDNJ-New Jersey Medical School
Harumi Jyonouchi, MD is a member of the following medical societies: American Academy of Allergy Asthma and Immunology, American Academy of Pediatrics, American Association of Immunologists, American Medical Association, Clinical Immunology Society, New York Academy of Sciences, Society for Experimental Biology and Medicine, Society for Mucosal Immunology, and Society for Pediatric Research
Disclosure: Nothing to disclose