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33. Shibata K, Mushiage M, Kondo T, Hayakawa T, Tsuge H. Effects of vitamin B6 deficiency on the conversion ratio of tryptophan to niacin. Biosci Biotechnol Biochem 1995; 59: 20603. Muschenheim C, McDermott W, McCune R, Deuschle K, Ormond L, Tompsett R. Pyrazinamide-isoniazid in tuberculosis: results in 58 patients with pulmonary lesions one year after the start of therapy. American Reviews of Tuberculosis 1954; 70: 7437. Jordahl C, Desprez R, Deuschle K, Muschenheim C, McDermott W. Further experience with single-drug isoniazid ; therapy in chronic pulmonary tuberculosis: initial therapy with high-dose isoniazid. Rev Tuberc Pulm 1958; 77: 53942. Badger TL. Tuberculosis. N Engl J Med 1959; 261: 306, Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC. Modification of the NADH of the isoniazid target InhA ; from Mycobacterium tuberculosis. Science 1998; 279: 98102. Somoskovi A, Parsons LM, Salfinger M. The molecular basis of resistance to isoniazid, rifampin, and pyrazinamide in Mycobacterium tuberculosis. Respir Res 2001; 2: 1648. Targeted tuberculin testing and treatment of latent tuberculosis infection. J Respir Crit Care Med 2000; 161: S22147. 40. Furlini G, Re MC, La Placa M. Increased poly ADP-ribose ; polymerase activity in cells infected by human immunodeficiency virus type-1. Microbiologica 1991; 14: 1418. Ha HC, Juluri K, Zhou Y, Leung S, Hermankova M, Snyder SH. Poly ADP-ribose ; polymerase1 is required for efficient HIV-1 integration. Proc Natl Acad Sci USA 2001; 98: 33648. Hussey GD, Klein M. Measles-induced vitamin A deficiency. Ann NY Acad Sci 1992; 669: 18896. Sharkey SJ, Sharkey KA, Sutherland LR, Church DL. Nutritional status and food intake in human immunodeficiency virus infection. GI HIV Study Group. J Acquir Immune Defic Syndr 1992; 5: 10918. Abrams B, Duncan D, Hertz-Picciotto I. A prospective study of dietary intake and acquired immune deficiency syndrome in HIVseropositive homosexual men. J Acquir Immune Defic Syndr 1993; 6: 94958. Tang AM, Graham NM, Saah AJ. Effects of micronutrient intake on survival in human immunodeficiency virus type 1 infection. J Epidemiol 1996; 143: 124456. Tabucchi A, Carlucci F, Consolmagno E, et al. Changes in purine nucleotide content in the.
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When magic ruled human belief, a cure for tuberculosis might have been regarded as a miracle. Today's scientific faithful view two drugs, isoniazid and pyrazinamide PZA ; , with almost equal wonder. This duo has helped demote the scourge 17th-century writer John Bunyan called "the captain of all these men of death" to a curable illness. Yet today, half a century after these drugs were introduced, no one can fully describe how they work. Driven by the emergence of resistant strains of TB, however, scientists have begun to entice the disease and its chemical assailants into yielding some of their elusive secrets. Two new reports offer insights into how the drugs work and what molecular mechanisms enable the TB bacterium, Mycobacterium tuberculosis, to resist them. An estimated one-third of the world's population is infected with latent TB. Each year, 8 million people develop active cases; nearly 3 million of them die. The Centers for Disease Control and Prevention in Atlanta has counted 6, 534 cases in the United States so far this year, many of them resistant to antibiotics. Resistance is fostered by the length of treatment--typically 6 months. Many patients begin to feel better much sooner than that and stop taking their medicine. The bacterium takes advantage of such gaps in therapy to develop resistance to the drugs. Although the authors of the reports worked separately, their research meshes well because isoniazid and PZA, while very different, have a common feature. Both drugs are harmless to the TB bacterium until they interact with its enzymes. Clifton E. Barry III, of the National Institute of Allergy and Infectious Diseases' Rocky Mountain Laboratories in Hamilton, Mont., calls this the "Trojan Horse paradigm" for eradicating the bacterium: "You feed it something that's nontoxic, and it becomes very toxic." The TB bacterium produces an enzyme called catalase, which activates isoniazid. When isoniazid is active, it interferes with the molecular mechanism that synthesizes mycolic acid, a fatty acid that is part of the bacterium's cell wall. This weakens the wall, leaving the cell vulnerable to corrosive, oxygen-containing molecules such as hydrogen peroxide. Scientists knew that a TB bacterium under threat from isoniazid switches off the KatG gene, which codes for catalase. Catalase, however, is central to the bacterium's survival because it breaks down the highly reactive oxygen-based molecules. If the bacterium doesn't make catalase, these molecules would most likely penetrate the bacterium and destroy it. Therefore, scientists couldn't understand how the isoniazid-resistant bacterium survives without catalase. Now, Barry and his colleagues report in the June 14 SCIENCE that TB has the makings of a back-up enzyme tucked in the inner workings of the cell. When the bacterium loses KatG, it compensates by turning on another gene, ahpC, which churns out alkyl hydroperoxidase, an enzyme that takes over where catalase leaves off. The research also demonstrates a key characteristic of isoniazid. Rather than targeting a single enzyme, as many other antibiotics do, it interacts with two separate aspects of the TB bacterium's life cycle--the protective enzymes and the mechanism that builds the cell wall. This makes it a provocative model for the development of new antibiotics. "We've thought of isoniazid as being somewhat old-fashioned. In fact, it is one of the most sophisticated drugs in use today, " Barry says. "We think it's a prototype for a new type of drug that attacks the regulatory mechanism in bacteria." In the June 6 NATURE MEDICINE, Ying Zhang and Angelo Scorpio of Johns Hopkins University School of Hygiene and Public Health in Baltimore report that they have identified a TB gene, pncA, that codes for an enzyme that converts the TB-fighting PZA into an acid lethal to the bacterium. They have also found mutations in the pncA gene that enable the bacterium to resist PZA.
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Jacketing Jacketing is the key feature that allows VAX and Alpha AXP interoperability, i.e., gives a processor the appearance of being able to execute both VAX and Alpha AXP instructions. Although the details of jacketing are intricate, the result is simple and elegant. Calls can be made freely back and forth between VAX compiled code and Alpha AXP compiled code, without any special compilation modes on either side. The AUD support is fully recursive and reentrant. Static calls from VAX to Alpha AXP code are directed to dummy entry points in the object module produced by the ALA compiler. Each entry point is simply an instruction that loads a pointer to the jacketing description table for the target Alpha AXP procedure, followed by a transfer into common jacket interpretation code. Calls from Alpha AXP code to VAX code use the fact that the Callable Mannequin component stops and returns control to the AUD environment when it detects an instruction that transfers control out of the Alpha AXP image. In this case, the apparent address is an encoded integer created by the ALA ; , whose high four bits make it look like an illegal address in the VAX reserved S1 space ; and whose remaining bits are a two-level index i.e., 12 bits of facility code and 16 bits of offset ; into the jacket description table for the target VAX procedure. This two-level scheme was chosen to allow jacket descriptions for different shared library facilities to be prepared and compiled independently. The facility code is a number normally already associated with that facility by software convention for other purposes. When a routine is called using a dynamically determined address, such as an address given in a function variable, a property of the VAX and Alpha AXP architectures is exploited to determine dynamically whether the target routine is a VAX routine or an Alpha AXP routine. According to the VAX architecture, the first 16 bits of a routine comprise a mask that encodes the registers to be preserved as part of the call. Bits 12 and 13 of this mask are unused and required to be 0; if one of these bits is set at the time of a call, then a hardware exception results. According to the OpenVMS AXP software architecture, an Alpha AXP procedure address is actually the address of a procedure descriptor, which is a data structure and not the actual Alpha AXP code. By design, bits 12 and 13 of this data structure must be set to 1. VAX execution of a VAX CALL instruction that attempts to transfer to an Alpha AXP procedure results in an exception. A special AUD exception handler intercepts the exception, determines if the illegal entry mask is caused by a reference into an Alpha AXP image, and if so, calls into the AUD jacketing routines to reformat the call frame. This mechanism also, for example, rifampicin isoniazid pyrazinamide.
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Substantial weight loss may occur after either VBG 9 ; or GBP 10 ; , the two most common surgical techniques currently in use for the treatment of severe obesity 3 ; . VBG involves the creation of a proximal vertical pouch about 15 cc in capacity ; along the lesser curvature of the stomach by placing four lines of staples from the esophagogastric angle parallel with the lesser curvature, and reinforcing the outlet of the pouch by a band or collar made of Marlex mesh or similar material ; . VBG is, therefore, designed to limit the capacity for a meal and to delay the emptying of solid foods from the pouch 118 ; . GBP involves the creation of a small proximal pouch about 40 cc in capacity ; partitioned by four horizontal lines of staples from the rest of the stomach, and connection of the pouch through a 10- to 15-mm surgical anastomosis to a Roux-en-Y jejunal limb usually 40 cm but may be longer ; . GBP, therefore, combines gastric restriction with the bypass of the distal stomach, duodenum, and proximal jejunum 17 ; . The superiority of GBP over VBG in achieving weight loss has been demonstrated by several controlled studies 11-14 ; : At 2 years after surgery, 60% of excess weight may be lost after GBP and 40% after VBG 15 ; . The benefit in terms of improvement in quality of life, as well as decrease in severity of comorbid disorders, has been amply demonstrated 16, 17 ; . However, the overall results mask important individual differences in outcome 7, 12, 14, ; . For instance, in the Adelaide study 12 ; in which GBP was compared with VBG and gastrogastrostomy, 15% of the 99 patients who underwent GBP the most effective of the three procedures studied ; had not lost any weight at 3 years after the procedure. Sugerman et al. 19 ; found an overall weight regain of 5% among 18 GBP patients from 12- to 36-months follow-up. In the longest follow-up study published thus far, Pories et al. 20 ; reported a 13.2-lb regain among GBP patients between the 1-year and 5-year-follow-up, with little additional regain thereafter. However, because the patient population at each point of follow-up are quite different among a total of 608 subjects, 506 were followed at 1 year, 317 at 5 years, 158 at 10 years, and 10 at 14 years ; , the cross-sectional outcome data may yield misleading information. Therefore, despite the favorable overall weight loss after bariatric surgery, it remains unclear why there is variability in outcome and why the body weight of many subjects does not fully normalize. Our own speculations that eating disturbances and abnormal energy metabolism may be responsible will be discussed below. In addition to weight loss, bariatric surgery leads to significant improvement in health status: blood pressure 21 ; , cardiac chamber size, wall thickness and left ventricular function 22 ; , hyperlipidemia 23 ; , respiratory insufficiency 24 ; , and diabetes 20 ; all improved after weight loss. There is, therefore, unanimous agreement that bariatric surgery, by virtue of its efficacy for weight loss, improves health status. However, it is unclear from these studies whether weight loss is the only factor responsible for the improvement in the.
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