Veterans’ Benefits: Pension Benefit Programs

[Excerpt] The Department of Veterans Affairs (VA) administers pension programs for certain low-income veterans and their surviving spouses and dependent children. This report discusses the Improved Disability Pension, which makes payments to certain low-income veterans, and the Improved Death Pension, which makes payments to certain low-income surviving spouses and dependent children of deceased veterans. To qualify for either program, individuals must have become eligible for payments on or after January 1, 1979. Both pension programs were created by P.L. 95-588, the Veterans and Survivors Pension Improvement Act of 1978. In addition, this report discusses a special pension program for Medal of Honor recipients. This report does not discuss several other pension programs that are administered by the VA, such as the Old Law Disability Pension and the Section 306 Disability Pension, which make payments to low-income veterans, and the Old Law Death Pension and the Section 306 Death Pension, which make payments to low-income surviving spouses and dependent children of veterans; these programs apply only to veterans and their survivors who became entitled to such benefits before 1979. This report also does not discuss pension programs for veterans of specific periods of war before World War I, such as the Civil War, the Indian Wars, and the Spanish-American War. Finally, this report does not address the military retirement system. For information on that system, see CRS Report RL34751, Military Retirement: Background and Recent Developments, by Kristy N. Kamarck

Veteran Benefits: An Overview

[Excerpt] The Department of Veterans Affairs (VA) offers a wide range of benefits and services to eligible veterans, members of their families, and survivors of deceased veterans. VA programs include disability compensation and pensions, readjustment benefits, and health care programs. The VA also provides life insurance, burial benefits, housing and other loan guaranty programs, and special counseling and outreach programs. While eligibility for specific benefits varies, veterans generally must meet requirements related to discharge type and length of active duty military service. This report provides an overview of major VA benefits and the VA budget. It will be updated as events warrant

The Glutathione S-Transferase GliG Mediates Gliotoxin Biosynthesis, not Self-Protection, in Aspergillus fumigatus: A Functional Genomic Investigation.

Gliotoxin is an epipolythiodioxopiperazine produced by the opportunistic fungal pathogen Aspergillus fumigatus. It contains an intact disulphide bridge, which mediates its toxic effects via redox cycling. Gliotoxin biosynthesis is directed by the gli gene cluster, and knowledge of the biosynthetic pathway which leads to gliotoxin formation is limited, although LPhe and L-Ser are known amino acid precursors and gliT is a gliotoxin oxidoreductase responsible for self-protection and disulphide bridge closure. Deletion of gliG, herein shown to be an epoxide-conjugating glutathione stransferase, from the gli cluster results in loss of gliG expression and the complete abrogation of gliotoxin biosynthesis. Instead, this deletion mutant, A. fumigatus !gliG, secretes a 6-benzyl-6-hydroxy-1-methoxy-3- methylenepiperazine-2,5-dione (262.1026 u), herein identified and structurally characterized for the first time, which is proposed to be a shunt metabolite formed in the absence of gliG. This putative shunt metabolite contains a hydroxyl group at C-6, consistent with a gliotoxin biosynthetic pathway involving thiolation, which is mediated by the addition of the glutathione thiol group to a reactive acyl imine intermediate. A new reduction and alkylation assay, which uses sodium borohydride and 5’-iodoacetamidofluorescein to label gliotoxin, yields a stable, labelled gliotoxin product, di-acetamidofluoresceingliotoxin (GT-(AF)2; 1103.47 Da). This species is readily detectable by RPHPLC and exhibits a 6.8-fold increase in molar absorptivity compared to gliotoxin, which results in a higher sensitivity of detection (50 ng; 125 pmol). Unlike gliotoxin, GT-(AF)2 is detectable by MALDI-ToF MS. 6-benzyl-6- hydroxy-1-methoxy-3-methylenepiperazine-2,5-dione cannot be alkylated and so is devoid of thiols or a disulphide bridge. Complementation of gliG restored gliG expression and gliotoxin production which coincided with the disappearance of 6-benzyl-6-hydroxy-1-methoxy-3-methylenepiperazine-2,5- dione. In addition, gliG was confirmed, unlike gliT, not to be involved in selfprotection against gliotoxin. It is over 75 years since gliotoxin was discovered. The work presented herein provides the first evidential support of the thiolation mechanism leading to gliotoxin biosynthesis, in addition to confirming a novel biosynthetic role for a glutathione s-transferase in fungi

The Glutathione S-Transferase GliG Mediates Gliotoxin Biosynthesis, not Self-Protection, in Aspergillus fumigatus: A Functional Genomic Investigation.

Gliotoxin is an epipolythiodioxopiperazine produced by the opportunistic fungal pathogen Aspergillus fumigatus. It contains an intact disulphide bridge, which mediates its toxic effects via redox cycling. Gliotoxin biosynthesis is directed by the gli gene cluster, and knowledge of the biosynthetic pathway which leads to gliotoxin formation is limited, although LPhe and L-Ser are known amino acid precursors and gliT is a gliotoxin oxidoreductase responsible for self-protection and disulphide bridge closure. Deletion of gliG, herein shown to be an epoxide-conjugating glutathione stransferase, from the gli cluster results in loss of gliG expression and the complete abrogation of gliotoxin biosynthesis. Instead, this deletion mutant, A. fumigatus !gliG, secretes a 6-benzyl-6-hydroxy-1-methoxy-3- methylenepiperazine-2,5-dione (262.1026 u), herein identified and structurally characterized for the first time, which is proposed to be a shunt metabolite formed in the absence of gliG. This putative shunt metabolite contains a hydroxyl group at C-6, consistent with a gliotoxin biosynthetic pathway involving thiolation, which is mediated by the addition of the glutathione thiol group to a reactive acyl imine intermediate. A new reduction and alkylation assay, which uses sodium borohydride and 5’-iodoacetamidofluorescein to label gliotoxin, yields a stable, labelled gliotoxin product, di-acetamidofluoresceingliotoxin (GT-(AF)2; 1103.47 Da). This species is readily detectable by RPHPLC and exhibits a 6.8-fold increase in molar absorptivity compared to gliotoxin, which results in a higher sensitivity of detection (50 ng; 125 pmol). Unlike gliotoxin, GT-(AF)2 is detectable by MALDI-ToF MS. 6-benzyl-6- hydroxy-1-methoxy-3-methylenepiperazine-2,5-dione cannot be alkylated and so is devoid of thiols or a disulphide bridge. Complementation of gliG restored gliG expression and gliotoxin production which coincided with the disappearance of 6-benzyl-6-hydroxy-1-methoxy-3-methylenepiperazine-2,5- dione. In addition, gliG was confirmed, unlike gliT, not to be involved in selfprotection against gliotoxin. It is over 75 years since gliotoxin was discovered. The work presented herein provides the first evidential support of the thiolation mechanism leading to gliotoxin biosynthesis, in addition to confirming a novel biosynthetic role for a glutathione s-transferase in fungi

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Can existing payment networks meet future needs? a conference summary

Payment systems

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