(Fruste 2002) Even less well understood are the proliferative effects it has on other tissues such as the bone marrow (stroma parenchyma) and tumors. (Polenakovic 1996, Ratajczak 2001, Schwartz 1992) Less well understood are the roles erythropoietin may play either directly or indirectly in angiogenesis (blood vessel formation), e.g., wounds and the female productive tract (Haroon 2003, Yasuda 1998, Zwezdaryk 2007) and the increase in thrombogenic properties of vascular endothelium. (Ingley 2004) It also decreases erythrocyte apoptosis (cell death). Erythropoietin regulates erythrocyte production by stimulating progenitor cell proliferation and differentiation in the bone marrow. (Bahlmann 2004, Rossert 2005) Its classic actions are well understood. (Van Dyke 1961) Serum levels of the hormone may transiently increase by a thousand-fold.Įrythropoietin has multiple actions. Basal physiologic levels range from approximately 6 to 32 U/L. Via intermediate signaling, perhaps with hydrogen peroxide (H 2O 2) and hypoxia inducible factors (HIF), cells increase transcription of the erythropoietin gene and subsequent production of the processed protein hormone. (Bauer 1898, Erslev 1980) Anemia and/or hypoxia result in decreased oxygen tension at the tissue level. (Faults 1989)Īs indicated above, production of this hormone is controlled via a feedback loop. The major side chains, sialated tetra-antennary saccharides, contribute to in vivo stability. The mature protein consists of a 165 amino acid backbone with 2 disulfide bonds, three N-linked carbohydrate chains, and one O-linked carbohydrate chain. An arginyl residue at the carboxyl terminus also appears to be cleaved during post-translation processing. (Miyake 1977) The native protein is a 193 amino acid peptide sequence from which a 27 amino acid peptide leader sequence is removed from the N-terminus. We caution the reader that the term “inulin” refers to a polysaccharide used to measure kidney function and should not be misread as the term “insulin.”Įrythropoietin is a 34-kDa glycoprotein hormone produced primarily, but not exclusively, in the kidney and to a lesser extent in the liver. Though we have tried to simplify the discussion for the lay reader, the topic is scientifically complex and we believe that an overly simplistic treatment would ultimately be detrimental to the understanding of our review. For purposes of this discussion, therapy for a medical condition includes treatment for the signs and symptoms of the underlying condition. Finally we describe how anemia management has changed over time. This is followed by a description of the types of anemia found in renal disease.
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We then describe the physiologic role of the kidneys, pathology of renal disease, and the demographics of renal disease. In this section, we describe the technological developments that gave rise to recombinant erythropoietin and related erythrocyte stimulating agents (ESAs). We will respond to public comments in a final decision memorandum, consistent with the spirit of §1862(l)(3). In order to maintain an open and transparent process, we are seeking comments on our proposal that no national coverage determination is appropriate at this time. Given the totality of the currently available evidence, we propose that CMS not issue a national coverage determination at this time for Erythropoiesis Stimulating Agents (ESAs) for Treatment of Anemia in Adults with CKD Including Patients on Dialysis and Patients not on Dialysis (CAG-00413N). Subject: Proposed Decision Memorandum for CAG # 00413N
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Including Patients on Dialysis and Patients not on Dialysisĭeputy Director, Coverage and Analysis Group
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Erythropoiesis Stimulating Agents (ESAs) for Treatment of Anemia in Adults with CKD