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Strickman, Daniel,Miller, Mary-E.,Lee, Kwan-Woo,Kim, Heung-Chul,Wirtz, Robert-A.,Perich, Michael,Novakoski, William-L.,Feighner, Brian-H.,Roh, Cheon-Seop 한국곤충학회 2001 Entomological Research Vol.31 No.3
The Republic of Korea (ROK) has been experiencing an expanding epidemic of Plasmodium vivax malaria since 1993, with most cases occurring near the Demilitarized Zone in the northwestern part of the country. During 1996 and 1997, U.S. Army preventive medicine assets undertook a program of surveillance and vector control to reduce transmission to U.S. Forces Korea (USFK). In 1996, the total number of cases was low and only routine vector control (ULV applications of malathion in early evening, availability of repellent for soldiers without command emphasis) was undertaken. Surveillance in 1996 indicated that Anopheles sinensis Wiedemann was the vector and that the risk to unprotected troops was high (1 of 361 mosquitoes infected in one area with 30 bites/person per night, 1 of 1,559 mosquitoes infected in another area with biting rate of 130/person/night). All night collections showed that most biting was occurring late at night, between 2300 and 0300 hrs. Expecting more transmission in 1997, a coordinated program (which did not include chemoprophylaxis) was initiated in which physicians, military commanders, and entomology assets all played a role. The following entomological interventions were concentrated at the site of highest risk, Camp Bonifas: 1) application of residual insecticide to tents, barracks, and bed nets, 2) ULV application of resmethrin late at night, 3) replacement and repair of screens, 4) use of permethrin treated bednets in unscreened billets, and 5) command emphasis on use of repellents and proper wear of the permethrin-treated uniform. Camp Bonifas experienced a 40% decrease in malaria cases (from 5 cases in 1996 to 3 cases in 1997) compared to a 243% increase in other American troops (from 7 to 24 cases) and a 306% increase (from 285 to 1,156 cases) in ROK Army troops. Although more effective use of ULV and application of larvicides would probably have improved the result, we conclude that entomological interventions without chemoprophylaxis reduced malaria transmission at Camp Bonifas by 82% in 1997.
Expression of the Ammonia Transporter, Rh C Glycoprotein, in Normal and Neoplastic Human Kidney
Han, Ki-Hwan,Croker, Byron P.,Clapp, William L.,Werner, Dietrich,Sahni, Manisha,Kim, Jin,Kim, Hye-Young,Handlogten, Mary E.,Weiner, I. David American Society of Nephrology 2006 Journal of the American Society of Nephrology Vol.17 No.10
<P>Recent studies have identified the presence of a novel Mep/Amt/Rh glycoprotein family of proteins that may play an important role in transmembrane ammonia transport. One of the mammalian members of this family, Rh C glycoprotein (RhCG), transports ammonia, is expressed in distal nephron sites that are critically important for ammonia secretion, exhibits increased expression in response to chronic metabolic acidosis, and originally was cloned as a tumor-related protein. The purpose of our studies was to determine the localization of RhCG in the normal and neoplastic human kidney. Immunoblot analysis of human renal cortical protein lysates demonstrated RhCG protein expression with a molecular weight of approximately 52 kD. Immunohistochemistry revealed both apical and basolateral Rhcg expression in the distal convoluted tubule, connecting segment, and initial collecting tubule and throughout the collecting duct. Co-localization with calbindin-D28k, H(+)-ATPase, aquaporin-2, and pendrin showed that distal convoluted tubule and connecting segment cells, A-type intercalated cells, and non-A, non-B cells express RhCG and that B-type intercalated cells, principal cells, and inner medullary collecting duct cells do not. In renal neoplasms, RhCG was expressed by chromophobe renal cell carcinoma and renal oncocytoma but not by clear cell renal cell carcinoma or by papillary renal cell carcinomas. These studies suggest that RhCG contributes to both apical and basolateral membrane ammonia transport in the human kidney. Furthermore, renal chromophobe renal cell carcinoma and renal oncocytoma seem to originate from the A-type intercalated cell.</P>
Expression of the ammonia transporter family member, Rh B Glycoprotein, in the human kidney
Han, Ki-Hwan,Lee, Hyun-Wook,Handlogten, Mary E.,Whitehill, Florence,Osis, Gunars,Croker, Byron P.,Clapp, William L.,Verlander, Jill W.,Weiner, I. David American Physiological Society 2013 American journal of physiology. Renal physiology Vol.304 No.7
<P>The ammonia transporter family member, Rh B Glycoprotein (RhBG/Rhbg), is essential for ammonia transport by the rodent kidney, but in the human kidney mRNA but not protein expression has been reported. Because ammonia transport is fundamental for acid-base homeostasis, the current study addressed RhBG expression in the human kidney. Two distinct RhBG mRNA sequences have been reported, with different numbers of consecutive cytosines at nt1265 and thus encoding different carboxy-tails. Sequencing the region of difference in both human kidney and liver mRNA showed eight sequential cytosines, not seven as in some reports. Knowing the correct mRNA sequence for RhBG, we then assessed RhBG protein expression using antibodies against the correct amino acid sequence. Immunoblot analysis demonstrated RhBG protein expression in human kidney and immunohistochemistry identified basolateral RhBG in connecting segment (CNT) and the cortical and outer medullary collecting ducts. Colocalization of RhBG with multiple cell-specific markers demonstrated that that CNT cells and collecting duct type A intercalated cells express high levels of RhBG, and type B intercalated cells and principal cells do not express detectable RhBG. Thus, these studies identify the correct mRNA and thus protein sequence for human RhBG and show that the human kidney expresses basolateral RhBG protein in CNT, type A intercalated cells, and non-A, non-B cells. We conclude that RhBG can mediate an important role in human renal ammonia transport.</P>
Spezia, Riccardo,Cimas, Alvaro,Gaigeot, Marie-Pierre,Salpin, Jean-Yves,Song, Kihyung,Hase, William L. The Royal Society of Chemistry 2012 Physical chemistry chemical physics Vol.14 No.33
<P>In this paper we report different theoretical approaches to study the gas-phase unimolecular dissociation of the doubly-charged cation [Ca(urea)]<SUP>2+</SUP>, in order to rationalize recent experimental findings. Quantum mechanical plus molecular mechanical (QM/MM) direct chemical dynamics simulations were used to investigate collision induced dissociation (CID) and rotational–vibrational energy transfer for Ar + [Ca(urea)]<SUP>2+</SUP> collisions. For the picosecond time-domain of the simulations, both neutral loss and Coulomb explosion reactions were found and the differences in their mechanisms elucidated. The loss of neutral urea subsequent to collision with Ar occurs <I>via</I> a shattering mechanism, while the formation of two singly-charged cations follows statistical (or almost statistical) dynamics. Vibrational–rotational energy transfer efficiencies obtained for trajectories that do not dissociate during the trajectory integration were used in conjunction with RRKM rate constants to approximate dissociation pathways assuming complete intramolecular vibrational energy redistribution (IVR) and statistical dynamics. This statistical limit predicts, as expected, that at long time the most stable species on the potential energy surface (PES) dominate. These results, coupled with experimental CID from which both neutral loss and Coulomb explosion products were obtained, show that the gas phase dissociation of this ion occurs by multiple mechanisms leading to different products and that reactivity on the complicated PES is dynamically complex.</P> <P>Graphic Abstract</P><P>Chemical dynamics and statistical analysis differentiate reaction pathway kinetics between neutral loss and Coulomb explosion in unimolecular [Ca(urea)]<SUP>2+</SUP> dissociation. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2cp41379e'> </P>