UI  - 0
PMID- 12456375
DA  - 20021128
IS  - 1093-4715
VI  - 8
DP  - 2003 Jan 1
TI  - NITRIC OXIDE (NO) - BIOGENERATION, REGULATION, AND RELEVENCE TO HUMAN
      DISEASES.
PG  - D264-D278
AB  - On October 12, 1998, the Nobel Assembly awarded the Nobel Prize in
      Medicine and Physiology to scientists Robert Furchgott, Louis Ignarro, and
      Ferid Murad for their discoveries concerning nitric oxide as a signalling
      molecule in the cardiovascular system. In contrast with the short research
      history of the enzymatic synthesis of NO, the introduction of
      nitrate-containing compounds for medicinal purposes marked its 150th
      anniversary in 1997. Glyceryl trinitrate (nitroglycerin; GTN) is the first
      compound of this category. Alfred Nobel (the founder of Nobel Prize)
      himself had suffered from angina pectoris and was prescribed nitroglycerin
      for his chest pain. Almost a century later, research in the NO field has
      dramatically extended and the role of NO in physiology and pathology has
      been extensively studied. The steady-state concentration and the
      biological effects of NO are critically determined not only by its rate of
      formation, but also by its rate of decomposition. Biotransformation of NO
      and its related N-oxides occurs via different metabolic routes within the
      body and presents another attractive field for our research as well as for
      the venture of drug discovery.
AD  - Department of Integrative Biology and Pharmacology, The Institute of
      Molecular Medicine, The University of Texas-Houston Medical School, 6431
      Fannin, Houston, TX 77030.
AU  - Bian K
AU  - Murad F
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Front Biosci
JID - 9709506
EDAT- 2002/11/29 04:00
MHDA- 2002/11/29 04:00
PST - ppublish
SO  - Front Biosci 2003 Jan 1;8:D264-D278.



UI  - 22317358
PMID- 12429871
DA  - 20021113
IS  - 0031-6997
VI  - 54
IP  - 4
DP  - 2002 Dec
TI  - Protein nitration in cardiovascular diseases.
PG  - 619-34
AB  - There is growing evidence that cardiovascular disease is associated with
      progressive changes in the production of free radicals and radical-derived
      reactive species. These intermediates react with all major cellular
      constituents and may serve several physiological and pathophysiological
      functions. The nitration of protein tyrosine residues has been used as a
      footprint for in vivo production of radical and nonradical reactive
      species. Tyrosine nitration may alter protein function and metabolism and
      therefore, provides for further dysfunctional changes. This review focuses
      on an appearance of tyrosine nitrated proteins in cardiovascular tissues
      under different settings of cardiovascular disease. Sources of reactive
      species, putative mechanisms of protein nitration in vivo, as well as
      protein nitration under normal physiological conditions, are also
      described. The goal of this review is to attract more attention to
      identification of specific proteins, which undergo tyrosine nitration and
      to study a correlation between their altered function and pathology.
      Understanding how protein nitration affects disease progression may offer
      a unique option for design of antioxidant therapy for the treatment of
      cardiovascular complications. At the same time, protein nitration can be a
      biological marker of efficiency of antioxidant therapy.
AD  - Department of Integrative Biology and Pharmacology and Institute of
      Molecular Medicine, University of Texas Medical School, Houston, Texas.
FAU - Turko, Illarion V
AU  - Turko IV
FAU - Murad, Ferid
AU  - Murad F
LA  - eng
PT  - Journal Article
CY  - United States
TA  - Pharmacol Rev
JID - 0421737
SB  - IM
EDAT- 2002/11/14 04:00
MHDA- 2002/11/14 04:00
PST - ppublish
SO  - Pharmacol Rev 2002 Dec;54(4):619-34.



UI  - 21565630
PMID- 11709394
DA  - 20011115
DCOM- 20020107
IS  - 0363-6135
VI  - 281
IP  - 6
DP  - 2001 Dec
TI  - Diabetes-associated nitration of tyrosine and inactivation of
      succinyl-CoA:3-oxoacid CoA-transferase.
PG  - H2289-94
AB  - High levels of reactive species of nitrogen and oxygen in diabetes may
      cause modifications of proteins. Recently, an increase in protein tyrosine
      nitration was found in several diabetic tissues. To understand whether
      protein tyrosine nitration is the cause or the result of the associated
      diabetic complications, it is essential to identify specific proteins
      vulnerable to nitration with in vivo models of diabetes. In the present
      study, we have demonstrated that succinyl-CoA:3-oxoacid CoA-transferase
      (SCOT; EC 2.8.3.5) is susceptible to tyrosine nitration in hearts from
      streptozotocin-treated rats. After 4 and 8 wk of streptozotocin
      administration and diabetes progression, SCOT from rat hearts had a 24%
      and 39% decrease in catalytic activity, respectively. The decrease in SCOT
      catalytic activity is accompanied by an accumulation of nitrotyrosine in
      SCOT protein. SCOT is a mitochondrial matrix protein responsible for
      ketone body utilization. Ketone bodies provide an alternative source of
      energy during periods of glucose deficiency. Because diabetes results in
      profound derangements in myocardial substrate utilization, we suggest that
      SCOT tyrosine nitration is a contributing factor to this impairment in the
      diabetic heart.
AD  - Department of Integrative Biology and Pharmacology, University of Texas
      Houston Medical School, Houston, Texas 77030, USA.
FAU - Turko, I V
AU  - Turko IV
FAU - Marcondes, S
AU  - Marcondes S
FAU - Murad, F
AU  - Murad F
LA  - eng
ID  - HL-64221/HL/NHLBI
PT  - Journal Article
CY  - United States
TA  - Am J Physiol Heart Circ Physiol
JID - 100901228
RN  - 0 (Reactive Nitrogen Species)
RN  - 10102-43-9 (Nitric Oxide)
RN  - 3604-79-3 (3-nitrotyrosine)
RN  - 55520-40-6 (Tyrosine)
RN  - EC 2.8.3 (Coenzyme A-Transferases)
RN  - EC 2.8.3.5 (3-ketoacid CoA-transferase)
SB  - IM
MH  - Animal
MH  - Catalysis
MH  - Coenzyme A-Transferases/*metabolism
MH  - Diabetes Mellitus, Experimental/*metabolism
MH  - Energy Metabolism/*physiology
MH  - Enzyme Activation/physiology
MH  - Kidney/metabolism
MH  - Lipid Peroxidation/physiology
MH  - Male
MH  - Mitochondria/metabolism
MH  - Myocardium/metabolism
MH  - Nitric Oxide/metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Reactive Nitrogen Species/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, Non-P.H.S.
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tyrosine/*analogs & derivatives/*metabolism
EDAT- 2001/11/16 10:00
MHDA- 2002/01/10 10:01
PST - ppublish
SO  - Am J Physiol Heart Circ Physiol 2001 Dec;281(6):H2289-94.



