Life-extension drugs

Life-extension drugs

Imunovir prescribing information


Imunovir Description

Imunovir is an immunomodulator and is approved for immunorestoration in chemotherapy in some countries. Patients on chemotherapy are particularly susceptible to different viral infections as a result of chemotherapy-induced immunodepression. Adjuvant therapy with Imunovir can restore the cell-mediated immune response to the individual's baseline levels.

It can therefore be prescribed during chemotherapy to restore the immune response and as a prophylaxis against reactivation of latent herpes simplex or herpes varicelliform zoster (shingles) infections, or for treatment or management of other secondary viral infections.

In these instances, the dosage used is the standard 50 mg/kg/day of lean body weight, up to a maximum of 3g daily (6x 500 mg tablets), divided evenly during waking hours. Schedule of treatment depends on the type of chemotherapeutic agent used. Imunovir is only administered after the infusion and only when the desired immune suppression against the cancerous cells has taken effect. At that point between infusions when it is desirable for the immune system to normalise, Imunovir treatment is initiated in order to enhance the normal immune response recovery. The number of treatment days depends on the length of time between infusions and also the immune profile of the individual patient.

Imunovir can also be administered for immunorestoration after chemotherapy, surgery or radiation.

Prescribing information, recommended dosage:
The prescribing physician will ultimately decide about the details of therapy (dosing, duration, etc.). According to dosing information obtained from published references; patients with cancer can take 2000 mg to 3000 mg of Imunovir daily for two months (4-6 tabs of 500 mg Imunovir per day). Then they may stop taking Imunovir for two months, and then resume taking it at the same dose for another two months.

How Does Imunovir work?
Imunovir is a synthetic purine derivative with immunomodulatory and antiviral properties, which result from an apparent in vivo enhancement of host immune responses due to the drug.

The action of Imunovir can be summarized as follows:
--- Normalizes the cell-mediated immunity by stimulating the differentiation of T-lymphocytes into T-cytotoxic cells and T-helper cells and increasing lymphokine production
--- Increases production of IL-1 (interleukin-1) and IL-2 (interleukin-2) and IFN-? (gamma interferon)
--- Increases NK cell (natural killer cell) function
--- Increases the humoral immune response by stimulating the differentiation of B- lymphocytes into plasma cells and by enhancing antibody production
--- Increases the number of IgG and complement surface markers
--- Potentiates neutrophil, monocyte and macrophage chemotaxis and phagocytosis
--- Inhibits viral growth by suppressing viral RNA synthesis while potentiating depressed lympocytic
--- RNA synthesis and translational ability

Other benefits of Imunovir treatment: Studies have documented the ability of to slow the progression of AIDS in HIV-infected persons by increasing the total number and activity of T-cells, T-helper cells and NK (natural killer) cells. The largest study, which was published in The New England Journal of Medicine on June 21, 1990 found that HIV infected people with CD4 cells count over 500 experienced significant benefits from Imunovir therapy. T-lymphocyte defects are common in cancer and AIDS patients according to a study in Medical Oncological Tumor Pharmacotherapy in 1989, which found that Imunovir and levamisole (another immune-boosting drug) mimic the actions of the thymic hormones to promote T-cell development. Combinations of Imunovir, low-dose Interleukin 1 and 2, and other immune-modulating hormones such as Melatonin are suggested as possibly effective cancer therapies.

50 tablets, 500 mg
150 ml syrop, 50 mg/ml

Caution! Before starting to take this medicine, it is vital that you should consult your doctor! Do not use it on your own initiative, without medical advice.

Imunovir Could Help in Chronic Fatigue Syndrome (ME/CFS) Doctors Report: In 1999 Dr. Byron Hyde reported that a small Imunovir study was 'milestone' in the treatment of ME/CFS. Dr. Paul Cheney calls Imunovir a 'very good immune-modulator' and appears to have used it extensively to boost NK cell functioning and reduce Th2 dominance in the immune system. In 2007 Dr. De Meirleir stated that he felt that Inosine - an amino acid available in health food stores - was as effective as Imunovir.

Chronic Fatigue Syndrome (ME/CFS) studies - Few studies have assessed Imunovir's effectiveness in ME/CFS. After a small single blind, placebo-controlled trial of 16 patients in 1999 Dr.Hyde's published study (2003) indicated that 6/10 patients improved and that their natural killer cell activity and T-helper cell numbers increased but no changes were seen in IFN-y, IL-1@, IL-10 and IL-12 levels. At the 2009 IACFS/ME conference Dr. Hone reported that Isoprinsine conferred 'significant (clinical)improvement' and increased NK cell functioning and reduced Epstein-Barr Virus levels in patients with reduced natural killer cell activity.

Because of its immunomodulatory properties Dr. Cheney recommends staggering dosages:
First Month:
•Week One: 6 tablets a day (M-F)
•Week Two: 2 tables a day (M-F)
•Week Three: Repeat Week One
•Week Three: Repeat Week Two
Second Month: Repeat first month
Third Month: Stop Imunovir
Four Month: Repeat Month 1
Fifth Month: Repeat Month 1
Six Month: Stop Isopoprinosine

Clinical trial results:

Isoprinosine notes

Isoprinosine having generic name Inosiplex (or Immunovir) is an old drug that has been extensively used for herpes, genital warts, influenza, melanomas, other tumors, hepatitis B, a rare brain inflammation in children caused by the zoster virus (subacute sclerosing panencephalitis) and cancer. This medication is approved in Canada and many other countries as an anti-viral drug. It is also used to treat chronic fatigue syndrome called as fibromyalgia. According to a clinical study, Isoprinosine was successfully used to treat viral infections in patients with acute leukemia, chronic leukemia and Hodgkin’s disease. It was also used to evaluate the immune function in cancer patients receiving pelvic radiation. Many studies have published indicating Isoprinosine’s antiviral and immunostimulatory effects benefiting AIDS patients. Isoprinosine is reported to have fewer side effects. Some of them are dizziness, stomach pain, digestion problem and itching. When this medication is given with ribavarin it causes drop in the white blood cells count of patient. Intake of Isoprinosine may results in certain allergic reactions like tightness in the chest or throat, skin hives, rashes, chest pain and itchy skin. The recommended dosage of Isoprinosine is as prescribed by doctor. Generally it is taken as 1 – 4 gms per day i.e. 2 – 8 tablets per day. Isoprinosine is available in 500 mg tablets form. This medication can also be given as syrup. The price of Isoprinosine syrup for 150ml package is USD 67. Consult doctor before taking this medication if you are pregnant or planning to become pregnant during the treatment. Physician's advice is necessary for lactating women if taking Isoprinosine. This medicine should not be taken by children.

Ther Drug Monit. 2010 Jun 25. [Epub ahead of print]
Petrova DT, Brandhorst G, Brehmer F, Gross O, Oellerich M, Armstrong VW.
From the Departments of *Clinical Chemistry and daggerNephrology and Rheumatology, University Hospital Goettingen, Goettingen, Germany.

Mycophenolic Acid Displays IMPDH-Dependent and IMPDH-Independent Effects on Renal Fibroblast Proliferation and Function.

The aim of this study was to elucidate the role of mycophenolic acid (MPA) in cellular pathways of renal fibrosis. Different assays were applied in a renal fibroblast model using COS-7 cells: assays for cell proliferation, scratch wound closure and collagen matrix contraction, gene quantification, and Western blotting. The results indicate that MPA treatment leads to inosine monophosphate dehydrogenase (IMPDH)-dependent inhibition of fibroblast proliferation and wound closure as well as an unexpected IMPDH-independent inhibition of collagen matrix contraction. Interestingly, the IMPDH-independent expression of CTGF after 6 hours incubation with MPA was significantly decreased; however, it became significantly increased and IMPDH-dependent after 24 hours of incubation and longer. Increased mRNA level of COL1A1, TGFbeta1, and TNFalpha was observed after MPA treatment. An unanticipated finding was the divergent and late MPA effect leading to a significant increase of TGFbeta1 and CTGF gene expression. The results suggest that long-term incubation with MPA alters signals located upstream of transforming growth factor-beta. Furthermore, the protein expression of the apoptotic marker ANXA5 was analyzed in the cell line to exclude apoptosis-related effects using 0.1 to 100 mumol/L MPA. Moreover, in COL4A3-deficient mice treated with different doses of mycophenolate mofetil, we found no significant differences in the gene expression of the same genes supporting the idea of a TGFbeta-independent pathway of tubulointerstitial fibrosis in this model for progressive renal disease. In conclusion, the current study indicates that MPA displays IMPDH-dependent and IMPDH-independent effects on renal fibroblast proliferation and function as well as complex signal transduction in COS-7-cells. Alternative inhibitory pathways may contribute to antifibrotic effect of MPA.

J Chromatogr A. 2010 Jun 9. [Epub ahead of print]
Viñas P, Campillo N, Melgarejo GF, Vasallo MI, López-García I, Hernández-Córdoba M.
Department of Analytical Chemistry, Faculty of Chemistry, University of Murcia, E-30071 Murcia, Spain.

Ion-pair high-performance liquid chromatography with diode array detection coupled to dual electrospray atmospheric pressure chemical ionization time-of-flight mass spectrometry for the determination of nucleotides in baby foods.

A liquid chromatography with diode array detection coupled to dual electrospray atmospheric pressure chemical ionization time-of-flight mass spectrometry (HPLC/ESI-APCI-TOF-MS) method is described for the rapid determination of five monophosphate nucleotides (cytidine 5'-monophosphate, uridine 5'-monophosphate, adenosine 5'-monophosphate, inosine 5'-monophosphate and guanosine 5'-monophosphate) in baby foods. The method is based on the deproteinisation of foods and direct analysis of nucleotides by ion-pair HPLC using isocratic elution with a mobile phase of 5% (v/v) methanol and 95% (v/v) 0.1M formate buffer (pH 5.5) containing 0.01M N,N-dimethylhexylamine (DMHA) at a flow-rate of 0.7mLmin(-1). The HPLC was hyphenated with two different detection systems, photodiode-array (DAD) and ESI-APCI-TOF-MS in negative mode. The method was validated for linearity, detection and quantitation limits, selectivity, accuracy and precision. The recoveries obtained for spiked samples were satisfactory for all the analytes. The method was successfully applied to the analysis of nucleotides in different baby and/or functional food samples, as cereals, purees and dairy products. A study was also carried out on the stability of nucleotides in acidified dairy infant food with pasteurized yoghourt and follow-on formulae samples stored at room temperature and at 30 degrees C.

PLoS One. 2010 Jun 21;5(6):e11173.
Osenberg S, Paz Yaacov N, Safran M, Moshkovitz S, Shtrichman R, Sherf O, Jacob-Hirsch J, Keshet G, Amariglio N, Itskovitz-Eldor J, Rechavi G.
Cancer Research Center, Chaim Sheba Medical Center, Tel Hashomer, Israel.

Alu sequences in undifferentiated human embryonic stem cells display high levels of A-to-I RNA editing.

Adenosine to Inosine (A-to-I) RNA editing is a site-specific modification of RNA transcripts, catalyzed by members of the ADAR (Adenosine Deaminase Acting on RNA) protein family. RNA editing occurs in human RNA in thousands of different sites. Some of the sites are located in protein-coding regions but the majority is found in non-coding regions, such as 3'UTRs, 5'UTRs and introns - mainly in Alu elements. While editing is found in all tissues, the highest levels of editing are found in the brain. It was shown that editing levels within protein-coding regions are increased during embryogenesis and after birth and that RNA editing is crucial for organism viability as well as for normal development. In this study we characterized the A-to-I RNA editing phenomenon during neuronal and spontaneous differentiation of human embryonic stem cells (hESCs). We identified high editing levels of Alu repetitive elements in hESCs and demonstrated a global decrease in editing levels of non-coding Alu sites when hESCs are differentiating, particularly into the neural lineage. Using RNA interference, we showed that the elevated editing levels of Alu elements in undifferentiated hESCs are highly dependent on ADAR1. DNA microarray analysis showed that ADAR1 knockdown has a global effect on gene expression in hESCs and leads to a significant increase in RNA expression levels of genes involved in differentiation and development processes, including neurogenesis. Taken together, we speculate that A-to-I editing of Alu sequences plays a role in the regulation of hESC early differentiation decisions.

Proc Natl Acad Sci U S A. 2010 Jun 21. [Epub ahead of print]
Paz-Yaacov N, Levanon EY, Nevo E, Kinar Y, Harmelin A, Jacob-Hirsch J, Amariglio N, Eisenberg E, Rechavi G.
Cancer Research Center, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel.

Adenosine-to-inosine RNA editing shapes transcriptome diversity in primates.

Human and chimpanzee genomes are almost identical, yet humans express higher brain capabilities. Deciphering the basis for this superiority is a long sought-after challenge. Adenosine-to-inosine (A-to-I) RNA editing is a widespread modification of the transcriptome. The editing level in humans is significantly higher compared with nonprimates, due to exceptional editing within the primate-specific Alu sequences, but the global editing level of nonhuman primates has not been studied so far. Here we report the sequencing of transcribed Alu sequences in humans, chimpanzees, and rhesus monkeys. We found that, on average, the editing level in the transcripts analyzed is higher in human brain compared with nonhuman primates, even where the genomic Alu structure is unmodified. Correlated editing is observed for pairs and triplets of specific adenosines along the Alu sequences. Moreover, new editable species-specific Alu insertions, subsequent to the human-chimpanzee split, are significantly enriched in genes related to neuronal functions and neurological diseases. The enhanced editing level in the human brain and the association with neuronal functions both hint at the possible contribution of A-to-I editing to the development of higher brain function. We show here that combinatorial editing is the most significant contributor to the transcriptome repertoire and suggest that Alu editing adapted by natural selection may therefore serve as an alternate information mechanism based on the binary A/I code.

Nucleosides Nucleotides Nucleic Acids. 2009 May;28(5):678-94.
Leonard P, Ingale SA, Ding P, Ming X, Seela F.
Laboratory of Bioorganic Chemistry and Chemical Biology, Center for Nanotechnology, Munster, Germany.

Studies on the glycosylation of pyrrolo[2,3-d] pyrimidines with 1-O-acetyl-2,3,5-tri-O-benzoyl-beta-D-ribofuranose: the formation of regioisomers during toyocamycin and 7-deazainosine syntheses.

Anim Sci J. 2009 Aug;80(4):411-7.
Iwamoto E, Oka A, Iwaki F.
Hyogo Prefectural Technology Center of Agriculture, Forestry, and Fisheries, Kasai, Japan.

Effects of the fattening period on the fatty acid composition of fat deposits and free amino acid and inosinic acid contents of the longissimus muscle in carcasses of Japanese Black steers.

Drug Metab Pharmacokinet. 2009;24(6):557-64.
Kudo M, Saito Y, Sasaki T, Akasaki H, Yamaguchi Y, Uehara M, Fujikawa K, Ishikawa M, Hirasawa N, Hiratsuka M.
Department of Clinical Pharmaceutics, Tohoku Pharmaceutical University, Sendai, Miyagi 980-8578, Japan.

Genetic variations in the HGPRT, ITPA, IMPDH1, IMPDH2, and GMPS genes in Japanese individuals.

Environ Monit Assess. 2009 Dec 15. [Epub ahead of print]
Wang J, Pant HK.
Department of Environmental Geographic and Geological Sciences, Lehman College, City University of New York, 250 Bedford Park Blvd. W., Bronx, NY, 10468, USA,

Identification of organic phosphorus compounds in the Bronx River bed sediments by phosphorus-31 nuclear magnetic resonance spectroscopy.

Fiziol Zh. 2008;54(6):5-14.
Nadtochiy SM, Nauduri D, Shimanskaya TV, Sagach VF, Brookes PS.
Department of Anesthesiology, University of Rochester Medical Center, Rochester, NY 14642, USA.

Purine release: a protective signaling mechanism of the mitochondrial permeability transition pore in ischemia.

Ann Acad Med Stetin. 2008;54(1):53-9.
Doma?ski L, Sulikowski T, Romanowski M, Safranow K, Pawlik A, Jakubowska K, Dziedziejko V, Wi?niewska M, Doma?ski M, Chlubek D, Olszewska M, Ciechanowski K.
Klinika Nefrologii, Transplantologii i Chor?b Wewnetrznych Pomorskiej Akademii Medycznej w Szczecinie al. Powsta?c?w Wlkp. 72, 70-111 Szczecin.

The effect of preservation solutions UW and EC on purine concentration in rat kidney.

FEMS Microbiol Lett. 2008 Dec;289(1):20-6.
M?dici R, Lewkowicz ES, Iribarren AM.
Biotransformation Laboratory, Universidad Nacional de Quilmes, Bernal, Buenos Aires, Argentina.

Arthrobacter oxydans as a biocatalyst for purine deamination.

Liver Int. 2008 Dec;28(10):1332-43.
Hofmann WP, Herrmann E, Sarrazin C, Zeuzem S.
Department of Internal Medicine 1, Johann Wolfgang Goethe-University Hospital, Frankfurt, Germany.

Ribavirin mode of action in chronic hepatitis C: from clinical use back to molecular mechanisms.

Genome Inform. 2007;18:287-98.
Driscoll ME, Romine MF, Juhn FS, Serres MH, McCue LA, Beliaev AS, Fredrickson JK, Gardner TS.
Boston University, St. Boston, MA 02215, USA.

Identification of diverse carbon utilization pathways in Shewanella oneidensis MR-1 via expression profiling.

Folia Biol (Krakow). 2007;55(3-4):153-60.
Ra? ME, Safranow K, Do?egowska B, Machoy Z.
Department of Biochemistry and Medical Chemistry, Pomeranian Medical University, Powsta?c?w Wielkopolskich 72, 70-111 Szczecin, Poland.

Guanine and inosine nucleotides, nucleosides and oxypurines in snail muscles as potential biomarkers of fluoride toxicity.

Genomics Proteomics Bioinformatics. 2007 Dec;5(3-4):143-51.
Xiao JF, Yu J.
CAS Key Laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing 100029, China.

A scenario on the stepwise evolution of the genetic code.

Pharmacogenomics. 2007 Jul;8(7):703-12.
Oliveira E, Marsh S, van Booven DJ, Amorim A, Prata MJ, McLeod HL.
University of Porto, Institute of Pathology and Molecular Immunology, 4200-465 Porto, Portugal.

Pharmacogenetically relevant polymorphisms in Portugal.

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