Peter Agre Did Not Deserve The Nobel Prize In Medicine
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Subject: Gheorghe Benga - discoverer of the first water channel protein From: Ad Astra X-PMX-Version: 4.1.0.80455 X-PerlMx-Spam: Gauge=IIIIIIII, Probability=8%, Report='__HAS_MSGID, __SANE_MSGID' In 1986, Gheorghe Benga and his coworkers discovered the presence and location of the first water channel protein in the human red blood cell membrane, several years before Peter Agre. In October 2003, Peter Agre was awarded the Nobel Prize in Chemistry, "for the discovery of water channels", jointly with Roderick MacKinnon. The Nobel Committee has neglected the important scientific contribution of Prof. Benga, without even mentioning it in the historical description of the discovery of aquaporins that joined the prize announcement. You may find pointers to documents that prove Prof. Benga's discovery at http://www.ad-astra.ro/benga/ . Please support the recognition of Gheorghe Benga as a discoverer of the first water channel protein in the human red blood cell membrane by doing the following: - add your signature to support a petition available at http://www.ad-astra.ro/benga/petition/ ; - forward this email to your colleagues and friends. A list of people that have already expressed their support for the petition is available at http://www.ad-astra.ro/benga/support/ . You may find the original text of this message, without quoting characters (e.g., '>'), at http://www.ad-astra.ro/benga/mail/ . Quick facts: - In 1986, Benga and coworkers clearly demonstrated the presence and location in the human red blood cell membrane of a protein involved in water transport and indicated the way to further studies, by purification of protein and reconstitution in lipid vesicles: "The binding pattern of PCMBS we have observed in correlation with the inhibition of water diffusion suggests that either or both band 3 and 4.5 proteins could be associated with water channels. Polypeptides migrating in these regions have already been
identified in other transport functions, notably anion exchange and the transport of glucose and nucleosides [...]. To date, however, there is no evidence that a specific inhibitor of one of these processes will inhibit water transport. It remains possible that a minor membrane protein that binds PCMBS is involved in water transport [...]. We believe that the best way to clarify the role of bands 3 and 4.5 in water transport will ultimately be through studies on the reconstitution of purified protein in liposomes" (Benga et al., Biochemistry 25 (7), 1986, pp. 1535-1538). - In 1988, Agre and coworkers isolated a new 28 kDa membrane protein, CHIP28, from both red cells and renal tubules. They suggested that "this new protein may play a role in linkage of the membrane skeleton to the lipid bilayer" (Denker et al., Journal of Biological Chemistry, 263 (30), 1988, pp. 15634-15642). It is now known that, in addition to the 28 kDa component, this protein has a 35-60 kDa glycosylated component, the one detected in 1986 by the Benga group. - Only in 1992, the Agre group suggested that "it is likely that CHIP28 is a functional unit of membrane water channels" (Preston et al., Science 256, 1992, pp. 385-387). In this paper, they cited a paper of Benga et al. from 1983, without mentioning their landmark 1986 paper. - An invited review of the history of the discovery of water channels proteins was published in September 2003, one month before the Nobel Prize for Chemistry was awarded (Benga, Cell Biology International, 27 (9), 2003, pp. 701-709). The contributions of the Benga group, also mentioned in this review, were overlooked by the Nobel Committee. No mention of the results of Benga and coworkers appeared in the historical description of the discovery of aquaporins that joined the prize announcement.
identified in other transport functions, notably anion exchange and the transport of glucose and nucleosides [...]. To date, however, there is no evidence that a specific inhibitor of one of these processes will inhibit water transport. It remains possible that a minor membrane protein that binds PCMBS is involved in water transport [...]. We believe that the best way to clarify the role of bands 3 and 4.5 in water transport will ultimately be through studies on the reconstitution of purified protein in liposomes" (Benga et al., Biochemistry 25 (7), 1986, pp. 1535-1538). - In 1988, Agre and coworkers isolated a new 28 kDa membrane protein, CHIP28, from both red cells and renal tubules. They suggested that "this new protein may play a role in linkage of the membrane skeleton to the lipid bilayer" (Denker et al., Journal of Biological Chemistry, 263 (30), 1988, pp. 15634-15642). It is now known that, in addition to the 28 kDa component, this protein has a 35-60 kDa glycosylated component, the one detected in 1986 by the Benga group. - Only in 1992, the Agre group suggested that "it is likely that CHIP28 is a functional unit of membrane water channels" (Preston et al., Science 256, 1992, pp. 385-387). In this paper, they cited a paper of Benga et al. from 1983, without mentioning their landmark 1986 paper. - An invited review of the history of the discovery of water channels proteins was published in September 2003, one month before the Nobel Prize for Chemistry was awarded (Benga, Cell Biology International, 27 (9), 2003, pp. 701-709). The contributions of the Benga group, also mentioned in this review, were overlooked by the Nobel Committee. No mention of the results of Benga and coworkers appeared in the historical description of the discovery of aquaporins that joined the prize announcement.
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