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About Erythropoietin

Erythropoietin is a glycoprotein hormone, more precisely cytokine, the main regulator of erythropoiesis, which stimulates the formation of erythrocytes from the late precursor cells and increases the yield of bone marrow reticulocytes depending on oxygen intake. As long as tissue oxygenation is not impaired, the concentration of erythropoietin, as well as the number of circulating red blood cells, remains constant. Erythropoietin production is regulated at the level of gene transcription, and since the only physiological incentive to increase the number of cells synthesizing erythropoietin is hypoxia, neither production nor metabolism of erythropoietin depend on its concentration in plasma. A healthy person has approximately 2.3*10^13 red blood cells in his or her body, with an average lifetime of 120 days. Therefore, the erythrocyte pool should be constantly renewed in the body at a rate of approximately 2.3 cells per second. The erythroid cell differentiation system should be strictly regulated to maintain a constant level of circulating erythrocytes under normal conditions. In addition, this system should be highly sensitive to changes in the amount of oxygen in the body. At present, there is a lot of evidence that the key factor that provides control of differentiation of cells of erythroid range is erythropoietin circulating in the blood.

Erythropoietin is an extremely active hormone that acts in the body in picomolar concentrations. Small fluctuations in its concentration in the blood lead to significant changes in the rate of erythropoiesis, and the normal range of its concentrations varies from up to 4 to 26 IU/l. Therefore, until the concentration of hemoglobin is lower than 105 g/l, the concentration of erythropoietin does not go beyond this range and it is impossible to detect its increase (unless you know its initial values). Erythrocytosis leads to the suppression of erythropoietin production by the negative feedback mechanism. This is due not only to the increased oxygen delivery to the tissues due to the increased number of circulating red blood cells, but also to the increased blood viscosity. For an athlete, this means a decrease in the production of his own hormone during the introduction of exogenous and violation of the mechanisms of regulation of erythrocyte production. Therefore, using erythropoietin as a doping agent in sport, the athlete should consider the future of erythrocyte production in the body.

Doping tests

Usually, erythropoietin is found in urine or blood samples. Blood is more likely to be detected than urine. The half-life is 5-9 hours, i.e. the probability of detection decreases significantly after 2-3 days.

Heparin is used as a masking agent. Protease injection into the bladder through a catheter is also used.

Physiological role of erythropoietin

For a long time, the question of cells producing erythropoietin remained open. This was primarily due to the lack of direct methods of identification of cells synthesizing the hormone. Cell identification was performed by indirect methods, including the ability of tissue cultures to synthesize the product in vitro. It was believed that the main candidates for the role of EPO-producing cells were the glomer cells and the cells of the proximal part of the tubules. Cloning of the erythropoietin gene, as well as the development of in situ hybridization methods that allow to identify directly those cells in which the expression of certain genes takes place, changed the idea of the nature of cells synthesizing erythropoietin. In situ hybridization has shown that the cells in which erythropoietin mRNA is synthesized are not glomerular or tubular. Apparently, the main place of EPO synthesis in kidneys is the interstitial cells or capillary endothelial cells. As already noted, hypoxia is the main factor regulating EPO production. In the conditions of hypoxia the number of EPO circulating in plasma increases approximately in 1000 times and reaches 5-30 units/ml. Numerous experiments with isolated kidneys have shown that it contains sensors that react to changes in oxygen concentration.

As early as 1987, J. Schuster and his colleagues investigated the kinetics of erythropoietin products in response to hypoxia. It was shown that approximately 1 h after the establishment of hypoxia, the amount of erythropoietin mRNA in the kidney increases and the mRNA continues to accumulate for 4 h. When hypoxia is removed, the level of EPO mRNA decreases rapidly. Changes in the amount of plasma and renal erythropoietin detected by erythropoietin-specific antibodies are strictly parallel to changes in the amount of mRNA with the corresponding lag period. The results obtained in this study indicate that de novo production of EPO is stimulated during.

In the S lab. Konry in 1989 investigated the process of induction of EPO synthesis by means of the method of hybridization in situ on tissue sections of the kidney cortical substance. It was found that under anemia, the production of EPO was significantly increased, although the intensity of hybridization with EPO mRNA in individual cells remained unchanged. It is shown that the increase of EPO production is connected with the increase of the number of cells synthesizing hormone. As the normal hematocrit is restored, the number of erythropoietin synthesizing cells decreases rapidly, and the kinetics of the change correlates with the kinetics of the decrease in the number of mRNA EPO and circulating hormone. Histological analysis data indicate that the EPO is synthesized by the interstitial cells of the cortical part of the kidney.

It is shown that 5 to 15% of plasma erythropoietin in adults is of extracellular origin. And if the main place of erythropoietin synthesis in embryos is the liver, the liver in an adult body is also the main organ producing EPO, but extrarenal. This conclusion has been confirmed in recent experiments to detect mRNA EPO in various organs. Apparently, the change of the main place of EPO synthesis during ontogenesis is a genetically determined event.

Synthesis of erythropoietin in the body is mediated by a significant number of biochemical cofactors and stimulants. It is assumed that hypoxia leads to a decrease in the oxygen level in specific sensory cells of the kidney, which causes an increase in the production of prostaglandins in nodule cells. It is shown that prostaglandins play an important role in stimulation of erythropoietin production. Inhibitors of prostaglandin synthesis have an overwhelming effect on the production of EPO in case of hypoxia. The main contribution to prostaglandin biosynthesis in hypoxia is probably made by the cyclooxygenase system. At hypoxia (and also at introduction of ions of cobalt) release of neutral proteases and lysosomal hydrolases in kidneys which, as it has been shown, also stimulate production of EPO occurs. The release of lysosomal enzymes seems to be associated with an increase in cGMF production. It is shown that lysosomal enzymes are activated by protein kinases, which in turn are activated by cAMP.

In hypoxia, induction of phospholipase A2 activity is observed, which leads to an increase in the level of arachidonates, which turn into endoperoxides with the participation of cyclooxygenase. It has been noted that hypoxia is the optimal condition for cyclooxygenase activity. Probably, an important role in these biochemical events is played by the calcium system: calcium ions stimulate the activity of phospholipase A, and the formation of prostaglandin. Prostonoids, in turn, can induce adenylate cyclase activity and trigger a cascade of biochemical events leading to phosphorylation and hydrolase activation. The role of the hydrolase and the chain that eventually leads to increased EPO synthesis remains unclear. Some hormones of the hypothalamic-pituitary system, thyroid hormones and some steroid hormones are also active in stimulating the biosynthesis of EPO. Cobalt ions are a specific inductor of EPO production, and their mechanism of action on the EPO biosynthesis system is not yet clear. This system is an attractive experimental model for the study of EPO biosynthesis induction.

The human erythropoietin molecule, in which the carbohydrate component accounts for 40-50 % of the molecular weight (the molecular weight of the glycoprotein is 32-36*10^3 a. m., and the estimated molecular weight of the protein part is 18 399*10^3 u), consists of 193 amino acid residues. The EPO isoelectric point value is low (pH 3.5-4.0), which is caused by the presence of sialic acids in the terminal positions of erythropoietin carbohydrate chains. The isoelectric focusing of plasma EPO in polyacrylamide gel allows to reveal several fractions, identical in molecular weight, but differing in size of their isoelectric points, that testifies to heterogeneity in the structure of carbohydrate part of hormone. Chipping off sialic acids during neuraminidase treatment or acid hydrolysis leads to loss of hormone stability in vivo, but does not affect its activity in vitro. In four sites glycoside residues are attached to the protein chain, which can represent different sugars, so there are several varieties of EPO with the same biological activity, but slightly different in their physical and chemical properties.

Analysis of the human erythropoietin amino acid sequence revealed three potential N-glycosylation sites, which include the Asn-X-Ser/Thr consensus sequence. In experiments on the treatment of the hormone with N-glycosidase, which specifically chipped away the oligosaccharide chains associated with the asparagine residue of the N-glycosidic bond, it was confirmed that three N-glycosylation sites were found in the EPO molecule. As a result of experiments on the processing of the hormone O-glycosidase it was found that it also contains oligosaccharide chains associated with the protein part by means of O-glycosidic bonds.

The erythropoietin gene (Gene: [07q21/EPO] erythropoietin) consists of five exons and four introns. The gene encodes a protein consisting of 193 amino acid residues. Four types of rnAs involved in the interaction with the erythropoietin gene have been identified, two of which are represented in extracts after the introduction of cobalt chloride in a much smaller number of copies than in normal extracts. These data indicate the presence of negative regulatory factors (probably, ribonucleoproteins) involved in the regulation of erythropoietin gene expression. The assumption of negative regulation of EPO gene expression was confirmed by Semenza G. and colleagues in 1990, who obtained a series of transgenic mice encoding the human EPO gene and various fragments of the S-flanking region. Analysis of gene expression in different transgens allowed to identify three regulatory elements of human erythropoietin gene:

a positive regulatory element required for the induction of erythropoietin gene expression in the liver;
negative regulatory element;
regulatory element required for inducible expression of the gene in kidneys.

It has been experimentally shown that there are two sites for the initiation of the erythropoietin transcription gene that carry many initiation sites. Under normal conditions, transcription is initiated from a limited number of sites located in both sites. When anemia is induction or cobalt chloride treatment, the number of functioning transcription initiation sites at both sites increases. In all cases, erythropoietin production is limited by difficulties related to cell isolation and cultivation, instability of hormone production and, finally, its low concentration in cultural fluids.

A fundamentally different approach to obtaining large amounts of highly purified EPO was associated with the use of methods of genetic and cellular engineering. An attempt was made to create a bacterial producer of erythropoietin. The protein produced in Escherichia coli is recognized by antibodies against EPO and has a molecular mass approximately corresponding to the deglycosylated human EPO. Bacterial cells are known to have a glycosylation system that is fundamentally different from that of eukaryotic cells. Therefore, it is impossible to obtain correctly glycosylated protein in bacterial cells. In the case of EPO, obtaining a correctly glycosylated glycoprotein is of fundamental importance. Therefore, the creation of a hormone producer on the basis of bacterial cells is inexpedient. Effective production of biologically active in vitro and in vivo erythropoietin can be obtained only on the basis of cells of higher animals.

In the study of the properties of recombinant EPO it was shown that the presence of incomplete carbohydrate component (the molecular weight of erythropoietin synthesized in this system is equal to 23*10^3 u) does not affect the activity of the hormone in vitro, but significantly reduces its activity in vivo. At the same time, complete carbohydrate detachment with glycosidase leads to 80% loss of biological activity of the hormone in the test in vitro. These data contradict the existing ideas that the carbohydrate component of EPO is not strictly necessary for its activity in vitro.

Historical note

In 1989, a detailed analysis of the structure of recombinant EPO obtained by transfection of cells from the Chinese hamster ovary into the human EPO genome was performed. It has been established that two types of EPO (called bi- and tetra-formes) are synthesized in cells, which differ in the degree of branching of N-bound carbohydrate chains. The bi-form of an EPO containing a less branched carbohydrate component differs significantly in its biological activity from the native erythropoietin used as a standard: the biological activity of the bi-form of an EPO in vivo is 7 times lower, and in vitro - 3 times higher. Biological activity of tetra-form EPO is very close to that of native EPO. These data indicate a significant role of the carbohydrate component structure in the biological activity of erythropoietin in vivo. Apparently, higher in vitro activity of those forms of erythropoietin containing incomplete carbohydrate component is associated with facilitation of erythropoietin interactions with receptors. At the same time, it seems that it is the carbohydrate component that provides stability of the hormone in the body and, accordingly, a high level of biological activity in vivo tests.

By the mid-1980s, the first recombinant erythropoietin was obtained by introducing the human EPO gene (localized in humans on the seventh chromosome in the 11q-12q region) into hamster ovarian cells. The recombinant human p-EPO obtained by genetic engineering (recombination) is identical in amino acid composition to the natural human EPO. Recorpone provides a flexible and cost-effective method of effective anemia treatment combined with a high safety profile and excellent tolerability. Thanks to the use of recormone, the need for hemotransfusions, which are the most common method of anaemia correction today, is significantly reduced. Thus, according to numerous studies, the use of recormone allows to restore the normal level of hemoglobin and eliminate the need for substitutional hemotransfusions in cancer patients suffering from anemia. At the same time, there is a significant improvement in the quality of life of these patients; the risk of infection, which exists during the correction of anemia with the help of hemotransfusions in the treatment of viral infectious diseases such as HIV and hepatitis C, is significantly reduced. Recorpone is available as a convenient device for administration and indication of the drug (pen syringe).

At the same time, there are insignificant differences in the composition of glycoside residues, which affect the physicochemical properties of the entire hormone molecule. Thus, for example, certain differences in the distribution of electric charge for certain types of erythropoietin have been found. Erythropoietin is produced by various pharmaceutical companies in five types: alpha, beta, retard (NESP and CERA), theta and omega.

Alpha EPO and beta EPO have been used since 1988. With subcutaneous injection, their bioavailability is about 25%, the maximum concentration in the blood is 12-18 hours, the half-life is up to 24 hours (with intravenous injection - 5-6 hours). Erythropoietin retard (NESP and CERA) has been in use for the last few years and is more effective than other EPO drugs. Today, theta EPO is considered to be the most effective and least allergenic, with the highest degree of purity. This is due to the fact that it is obtained by genetic engineering methods in human cells (some unscrupulous athletes and sports physicians believe that this makes it undetectable). In fact, theta EPO is only 99% identical to that of humans. The omega-epo, which is obtained from hamster kidneys, is the most different from other EPO drugs in humans, so it is the easiest to detect. Sold only in Eastern Europe and South America.

Erythropoietin preparations

Recombinant biosimilar a-EPOs from different manufacturers, even those approved by the Committee for Medicinal Products for Human Use (CHMP) of the European Agency for Medicinal Products for Human Use, may have different properties, purity and, most importantly, different biological activity. When different manufacturers of erythropoietin were analyzed, 5 out of 12 products studied showed significant deviations in the strength of action between different series, in three samples - unacceptable levels of bacterial endotoxins.

Another study was a comparison of 11 EPO products (received from eight manufacturers) available on non-EU markets in terms of content, strength and isoform composition of the active ingredient (erythropoietin). In vitro bioactivity ranged from 71-226%, with 5 samples not meeting specifications. Among the deviations in the isoform composition are: the presence of one or more additional acidic and/or basic isoforms, as well as a changed quantitative ratio of different isoforms. Inter-series differences were also identified; some products did not meet their own specifications, i.e., manufacturers did not provide adequate control of production processes. The quantity of the active ingredient was also not always in line with the stated quantity. Such deviations from the declared parameters may have an important clinical significance, as they may lead to overdose or, conversely, to a lower dose. The data provided clearly indicate a threat of the use of recombinant erythropoietins without medical indication.

Medical applications

In medical practice, erythropoietin is used to treat anemia of various genesis, including cancer patients with chronic renal failure. Since, as noted above, endogenous erythropoietin is formed in the kidneys in the body, patients with chronic renal failure always suffer from anemia. In addition, a decrease in the concentration of EPO in human plasma and, consequently, the number of red blood cells, is observed in the following pathological conditions and diseases:

secondary polycythemia;
Inadequate stimulation of own EPO;
benign kidney disease (hydronephrosis);
general tissue hypoxia;
Kidney blood supply disorder
Reduced oxygen concentration in the environment;
Chronic obstructive pulmonary disease;
Cardiovascular diseases (from right to left);
anomalies in the structure of the hemoglobin molecule (sickle cell anemia);
Effects on the body of carbon monoxides, due to smoking;
Arteriosclerosis of the renal artery;
rejection of the graft;
renal aneurysms.

Before the appearance of recombinant erythropoietin, such patients were regularly subjected to hematransfusion of both whole blood and erythrocytic mass. However, since 1989, such procedures are no longer necessary, as they have been replaced by erythropoietin preparations. In some cases, anaemia of other origins is also successfully treated with recombinant EPO. The fact that the introduction of recombinant EPO induces additional erythropoiesis even at a fully intact endogenous level of EPO is used by autologous blood donors. As an alternative to erythrocytic mass transfusion, high-dose EPO therapy is an effective antianemic measure as an accompanying therapy in the treatment of chronic polyarthritis, AIDS, some tumors, as well as in a number of surgical interventions. The genesis of hypertension as a side effect of the therapeutic use of recombinant EPO is still unclear. When hemodialysis is performed on patients, erythropoietin medications are usually administered intravenously. In some cases, the same drug may be injected subcutaneously.

The increase in the number of red blood cells under the influence of erythropoietin, in turn, leads to an increase in oxygen content per unit of blood volume and, consequently, an increase in the oxygen capacity of the blood and the delivery of oxygen to the tissues. Ultimately, the body's endurance increases. Similar effects are achieved during training exercises in the middle mountains, when lack of oxygen in the air causes a state of hypoxia, which stimulates the production of endogenous EPO. Naturally, compared to the use of recombinant drug, hypoxic training is a physiological mechanism of erythropoiesis regulation and improvement of oxygen transport function of hemoglobin, which is the purpose of using EPO as a doping agent.

Due to the effect of erythropoietin on oxygen capacity and oxygen transport in tissues, this substance causes increased performance in sports with a predominant manifestation of aerobic endurance. These sports disciplines include all kinds of athletic running, starting from 800 m, as well as all kinds of skiing and cycling races. In addition, bodybuilding publications have recently begun to show that EPO can replace the mass use of anabolic steroids. Epo drugs are used in combination with stanazole, insulin and somatotropin hormone (HGH).

Erythropoietin preparations are well tolerated pharmacological agents that have almost no side effects. However, overdose of EPO and uncontrolled use can lead to an increase in blood viscosity and, consequently, to an increase in the risk of blood circulation disorders, up to peripheral vascular thrombosis and pulmonary embolism, which usually leads to death. The risk of these side effects of EPO increases with training in the middle mountains, as well as with dehydration.

However, there is evidence that long-term use of erythropoietin preparations can be dangerous to health and sometimes to life. In particular, the use of EPO is associated with constant headaches in athletes due to blood clotting and circulation disorders in the brain. In addition, iron metabolism may be impaired: the body's need for iron increases when there is a relatively small stockpile of iron in the liver. When exogenous iron is injected, it starts to be deposited in the liver, so that cirrhosis of the liver associated with iron excess is manifested after 20-25 years.

Erythropoietin in sports

The history of the use of recombinant erythropoietin in sport (commonly used in scientific literature as rHuEPO, r-HuEPO, rhu-EPO, rEPO) dates back to 1977, when erythropoietin was first isolated from human urine in its purified form. The introduction and control of erythropoietin in sport and competition as a prohibited drug was carried out in the following stages:

1985 - cloned the EPO gene;
1987 - recombinant erythropoietin became available for the first time in Europe;
1987-1990. - Several deaths among Dutch and Belgian cyclists are attributed to the use of EPO;
1988 - The International Ski Federation includes erythropoietin in its doping list;
1989 - FDA (Food and Drug Administration) - The government agency that controls the production and distribution of drugs in the country permits the production of recombinant EPO;
1990 - Use of erythropoietin is prohibited by the IOC;
1993-1994. - IAAF, with the active participation of Professor M. Donika, introduces blood collection procedures at eight World Cup competitions;
1997 - The International Cycling Union and the International Ski Federation approve a blood sampling procedure prior to the start of the competition, setting limits for haematocrit and haemoglobin. While exceeding these limits is not a basis for Ineligibility, it is intended to protect the Athlete's body from potential complications associated with elevated haemoglobin and haematocrit;
1998 - Disclosure of the use of erythropoietin in sport at the Tour de France cycling race received extensive media coverage;
1999 - Research on the development of a reliable method of EPO detection for the Olympics in Sydney was intensified.

Since natural and recombinant erythropoietin have an almost identical amino acid structure, recombinant erythropoietin is extremely difficult to distinguish from its physiological analogue.

Inhalation of xenon inhalation is actively used for stimulation of erythropoietin secretion in Russia. At the Sochi 2014 Olympics, many Russian athletes received xenon inhalation before the start of the competition. This method has been banned by the Anti-Doping Agency since May 2014.

Doping control

The current arsenal of methods for the determination of erythropoietin includes direct and indirect approaches. The direct method is based on the identification of those insignificant differences found in the study of natural endogenous erythropoietin and EPO obtained by genetic engineering. In particular, some researchers have attempted to use the differences in the distribution of electrical charge that have been established for the two types of ELISA molecules. Based on these differences, attempts were made to separate the two types of molecules using the capillary electrophoresis method. Although this separation is possible in principle, it requires large amounts of urine (up to 1 litre, which is understandably unacceptable for practice).

Preference is given to indirect methods, which require only small amounts of blood or urine samples. Examples of indirect methods for detecting EPO are:

Deviations from normal levels in the bioenvironment of the sample. This fact means that the established excess of the EPO level should be different from physiological or pathological variations. However, the use of this criterion is possible only if the range of variation is narrow enough compared to the values that are detected after exogenous administration of the drug. The latter is only possible when using blood as a sample for a doping test;
Registration of biochemical parameters, the value of which depends on the concentration of erythropoietin. This approach may be based on measuring the serum content of the soluble transferrin receptor (sTfR), the level of which increases after the introduction of recombinant EPO. However, similar changes are occurring after training in the middle mountains;
determination of fibrin and fibrinogen decomposition products in urine after EPO administration.

At present, it is almost impossible to reliably identify cases of exogenous injection of erythropoietin into the body. Therefore, changes in the physiological parameters of blood, which are detected after the introduction of EPO, are used for control. Thus, the International Cycling Union uses the criterion of maximum hematocrit value (50% for men). The International Ski Federation has established the maximum allowable values of hemoglobin (165 g/l for women and 185 g/l for men) and reticulocyte levels of no more than 0.2%. If these limits are exceeded during the pre-competition control procedure, the athlete concerned will be suspended from the competition for health reasons. However, both haemoglobin and haematocrit are indicators that are affected by many factors. In particular, both of these indicators can change significantly even after one session of average volume endurance. In addition, these indicators are characterized by significant individual variability. Therefore, a single excess of more than 50% of the hematocrit value cannot prove the abuse of erythropoietin in sport.

To improve control over the use of erythropoietin as a doping agent, WADA has introduced an Athlete Blood Passport modus operandi. The Blood Passport is one of WADA's developments aimed primarily at detecting erythropoietin and its analogues. It generates a single computerized hematology profile for each athlete based on 30 different indicators, first in those sports where endurance is required. Ten countries, including Sweden, Norway, Canada and Germany, have already joined the introduction and improvement of the blood certification program. The Russian Anti-Doping Agency approves this initiative, but it is going to be implemented after all medical and legal aspects have been finalized.

WADA recommends the use of Sysmex (Japan) or an ERMA subsidiary to perform tests on the Athlete's blood sheet. This brand of the latest generation of fully automatic haematology analysers has won the highest index of confidence in the accuracy of the blood count.

During intensive training sessions and professional sports activities, it is necessary to constantly carry out hematological analysis to determine the number of erythrocytes and their parameters (volume, saturation with hemoglobin), hemoglobin and hematocrit levels. Hematocrit should not be allowed to rise above 50% - this leads to blood thickening, which, in turn, is fraught with deterioration of blood circulation in muscles and internal organs, increased risk of thrombosis (the propensity for thrombophilia can be assessed by the marker D-dimer). In addition, there is a need for complete control of iron metabolism (iron concentration in serum, total and unsaturated iron-binding capacity, iron saturation percentage, transferrine, ferritin, C-reactive protein) and determination of folic acid and vitamin B12 levels in the blood. All these compounds are necessary for proper erythropoiesis and should not be allowed to deficiency during sports activities. In addition to the above tests, it is necessary to control the level of erythropoietin itself.

Where to buy EPO?

On our website you can buy EPO with delivery all over the world. No matter what country you live in, you will receive the parcel without problems at customs and without risk of losing money. You do not need to see a doctor or have a prescription to place an order.

We always have EPOs of several types and generations in stock:

Epoetin Alfa(Binocrit, Eprex, Eralfon, Epocrin, Procrit)
Epoetin Beta(Vero epoetin, Epostim, Erythropoietin Binnopharm, Recormon)
NESP (Aranesp)
CERA (Mircera)

What a cost for an EPO?

Our EPO prices depend on the country of origin of the drug, the form of production (ampoules/vials/syringes), as well as the procurement price.

The lowest price starts from 30 USD for one 2000IU vial (suitable for trial order).

For wholesale buyers we can offer bulk prices on request.

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We deliver EPO to all countries of the world, including those with strict customs controls. We are able to guarantee the delivery of most of our EPO products without customs control. If you live in Australia, New Zealand, Germany, Switzerland, Austria, Italy or the United States and you are already desperate to get an EPO, we are your only option.
Upon your request, we can arrange direct or transit delivery from Europe (prices and available medicines are discussed individually).