المؤلفون: Kristof, Arnold S.

المصدر: Lymphatic Research and Biology ; volume 8, issue 1, page 33-42 ; ISSN 1539-6851 1557-8585

الإتاحة: https://doi.org/10.1089/lrb.2009.0019Test

المؤلفون: Kristof, Arnold S., You, Zhipeng, Han, Yin-Shan, Giaid, Adel

المصدر: Peptides ; volume 31, issue 8, page 1511-1516 ; ISSN 0196-9781

مصطلحات موضوعية: Cellular and Molecular Neuroscience, Endocrinology, Physiology, Biochemistry

الإتاحة: https://doi.org/10.1016/j.peptides.2010.04.017Test
https://api.elsevier.com/content/article/PII:S0196978110001713?httpAccept=text/xmlTest
https://api.elsevier.com/content/article/PII:S0196978110001713?httpAccept=text/plainTest

المؤلفون: Codère-Maruyama, Takumi, Schricker, Thomas, Shum-Tim, Dominique, Wykes, Linda, Nitschmann, Evan, Guichon, Céline, Kristof, Arnold S., Hatzakorzian, Roupen

المصدر: American Journal of Physiology: Regulatory, Integrative & Comparative Physiology; Dec2016, Vol. 311 Issue 6, pR1085-R1092, 8p

مصطلحات موضوعية: GLUCOSE clamp technique, PROTEINS in the body, CORONARY artery bypass, PATIENTS

مستخلص: Cardiac surgery triggers an inflammatory stress response, leading to protein catabolism, a process that even high-dose insulin therapy alone cannot reverse. To determine whether hyperinsulinemic-normoglycemic clamp and perioperative amino acid (AA) supplementation improves whole body protein balance, 20 patients scheduled for elective coronary artery bypass grafting surgery were randomly assigned to have intra- and postoperative hyperinsulinemic-normoglycemic clamp, with or without intravenous AA supplementation. Primed continuous infusions of [6,6-²H2]glucose and L-[1-¹³C]leucine were used to quantify whole body protein and glucose metabolism before and after surgery. Adipose tissue and serum cytokines were also analyzed to measure their responsiveness to the anabolic effect of AA administration. During hyperinsulinemic-normoglycemic clamp, AA supplementation successfully stimulated whole body protein synthesis, resulting in a positive whole body protein balance after surgery (insulin: -13.6 ± 4.5 vs. insulin + AA: 2.1 ± 5.4 µmol·kg^-1·h^-1, P < 0.001). Endogenous glucose production was equally suppressed in both groups (insulin: 0.0 ± 3.8 vs. insulin + AA 1.6 ± 1.6 µmol·kg^-1·min^-1, P = 0.230). AA supplementation led to significant changes in serum and tissue IL-6 (insulin: 246.6 ± 111.2 vs. insulin + AA: 124.5 ± 79.3 pg/ml, P = 0.011). In conclusion, hyperinsulinemic- normoglycemic clamp technique, together with AA supplementation, can induce an anabolic state after open-heart surgery, as quantified by a positive whole body protein balance. [ABSTRACT FROM AUTHOR]

: Copyright of American Journal of Physiology: Regulatory, Integrative & Comparative Physiology is the property of American Physiological Society and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Pacheco-Rodriguez, Gustavo, Kristof, Arnold S., Stevens, Linda A., Zhang, Yi, Crooks, Denise, Moss, Joel

المصدر: Chest ; volume 121, issue 3, page 56S-60S ; ISSN 0012-3692

مصطلحات موضوعية: Cardiology and Cardiovascular Medicine, Critical Care and Intensive Care Medicine, Pulmonary and Respiratory Medicine

الإتاحة: https://doi.org/10.1378/chest.121.3_suppl.56sTest
https://api.elsevier.com/content/article/PII:S0012369215354659?httpAccept=text/xmlTest
https://api.elsevier.com/content/article/PII:S0012369215354659?httpAccept=text/plainTest

المؤلفون: Kristof, Arnold S., Magder, Sheldon

المصدر: Critical Care Medicine ; volume 27, issue 6, page 1121-1127 ; ISSN 0090-3493

الإتاحة: https://doi.org/10.1097/00003246-199906000-00033Test
http://journals.lww.com/00003246-199906000-00033Test

المؤلفون: Kristof, Arnold S., Noorhosseini, Hamid, Hussain, Sabah N.A.

المصدر: European Journal of Pharmacology ; volume 328, issue 1, page 69-73 ; ISSN 0014-2999

مصطلحات موضوعية: Pharmacology

الإتاحة: https://doi.org/10.1016/s0014-2999Test(97)83030-0
https://api.elsevier.com/content/article/PII:S0014299997830300?httpAccept=text/xmlTest
https://api.elsevier.com/content/article/PII:S0014299997830300?httpAccept=text/plainTest

المؤلفون: Delarosa, Sierra, Guillemette, Julie, Papillon, Joan, Ying-Shan Han, Kristof, Arnold S., Cybulsky, Andrey V.

المصدر: American Journal of Physiology: Renal Physiology; Sep2011, Vol. 301 Issue 3, pF554-F564, 11p

مصطلحات موضوعية: GENE expression, GENETIC transcription, GENETIC regulation, GENETIC translation, APOPTOSIS, PROTEIN kinases, GEL permeation chromatography

مستخلص: The expression and activation of the Ste20-like kinase, SLK, is increased during renal development and recovery from ischemic acute renal failure. SLK promotes apoptosis, and during renal injury and repair, transcriptional induction or posttranscriptional control of SLK may, therefore, regulate cell survival. SLK contains protein interaction (coiled-coil) domains, suggesting that posttranslational homodimerization may also modulate SLK activity. We therefore expressed coiled-coil regions in the C-terminal domain of SLK as fusion proteins and demonstrated their homodimerization. By gel-filtration chromatography, endogenous and heterologously expressed SLK were detected in a macromolecular protein complex. To test the role of homodimerization in kinase activation, we constructed a fusion protein consisting of the SLK catalytic domain (amino acids 1-373) and a modified FK506 binding protein, Fv (Fv-SLK 1-373). Addition of AP20187 (an analog of FK506) enhanced the homodimerization of Fv-SLK 1-373. In an in vitro kinase assay, the dimeric Fv-SLK 1-373 displayed greater kinase activity than the monomeric form. In cells expressing Fv-SLK 1-373, homodimerization increased activation-specific phosphorylation of the proapoptotic kinases, c-Jun N-terminal kinase and p38 kinase. Compared with the monomer, dimeric Fv-SLK 1-373 enhanced the activation of a Bax promoter-luciferase reporter. Finally, expression of Fv-SLK 1-373 induced apoptosis, and the effect was increased by homodimerization. Thus the activity, downstream signaling, and functional effects of SLK are enhanced by dimerization of the kinase domain. [ABSTRACT FROM AUTHOR]

: Copyright of American Journal of Physiology: Renal Physiology is the property of American Physiological Society and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Taveira-DaSilva AM, Stylianou MP, Hedin CJ, Kristof AS, Avila NA, Rabel A, Tavis WD, Moss J, Taveira-DaSilva, Angelo M, Stylianou, Mario P, Hedin, Carolyn J, Kristof, Arnold S, Avila, Nilo A, Rabel, Antoinette, Travis, William D, Moss, Joel

المصدر: American Journal of Respiratory & Critical Care Medicine; 2003, Vol. 168 Issue 12, p1427-1431, 5p

مستخلص: Lymphangioleiomyomatosis (LAM), a disease that occurs primarily in women, is characterized by cystic lung lesions causing respiratory failure, which may require lung transplantation. Lung diffusion (DLCO) and/or FEV1 are decreased, but frequently not in parallel with each other. Because cardiopulmonary exercise testing (CPET) provides information that is not obtainable from resting cardiopulmonary tests, we performed CPET in 217 LAM patients and correlated exercise data with clinical markers of severity, computed tomography scans, lung function, and histology. VO2max was decreased in 162 patients, of whom 28 did not reach anaerobic threshold; 29 had low oxygen uptake at anaerobic threshold, and 54 developed hypoxemia. Hypoxemia occurred even in patients with near normal DLCO and FEV1. VO2max decreased with an increasing score of histologic LAM severity and was correlated with computed tomography scans, the use of oxygen, and resting PaO2. DLCO and FEV1, however, were the only significant predictors of VO2max. We conclude that CPET uncovers the presence of exercise-induced hypoxemia and assists in grading the severity of disease and determining supplemental oxygen requirements in patients with LAM. [ABSTRACT FROM AUTHOR]

: Copyright of American Journal of Respiratory & Critical Care Medicine is the property of American Thoracic Society and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Delarosa, Sierra, Guillemette, Julie, Papillon, Joan, Han, Ying-Shan, Kristof, Arnold S., Cybulsky, Andrey V.

المصدر: American Journal of Physiology - Renal Physiology; September 2011, Vol. 301 Issue: 3 pF554-F564, 11p

مستخلص: The expression and activation of the Ste20-like kinase, SLK, is increased during renal development and recovery from ischemic acute renal failure. SLK promotes apoptosis, and during renal injury and repair, transcriptional induction or posttranscriptional control of SLK may, therefore, regulate cell survival. SLK contains protein interaction (coiled-coil) domains, suggesting that posttranslational homodimerization may also modulate SLK activity. We therefore expressed coiled-coil regions in the C-terminal domain of SLK as fusion proteins and demonstrated their homodimerization. By gel-filtration chromatography, endogenous and heterologously expressed SLK were detected in a macromolecular protein complex. To test the role of homodimerization in kinase activation, we constructed a fusion protein consisting of the SLK catalytic domain (amino acids 1–373) and a modified FK506 binding protein, Fv (Fv-SLK 1–373). Addition of AP20187 (an analog of FK506) enhanced the homodimerization of Fv-SLK 1–373. In an in vitro kinase assay, the dimeric Fv-SLK 1–373 displayed greater kinase activity than the monomeric form. In cells expressing Fv-SLK 1–373, homodimerization increased activation-specific phosphorylation of the proapoptotic kinases, c-Jun N-terminal kinase and p38 kinase. Compared with the monomer, dimeric Fv-SLK 1–373 enhanced the activation of a Bax promoter-luciferase reporter. Finally, expression of Fv-SLK 1–373 induced apoptosis, and the effect was increased by homodimerization. Thus the activity, downstream signaling, and functional effects of SLK are enhanced by dimerization of the kinase domain.

المؤلفون: Abdel-Malak, Nelly A., Srikant, Coimbatore B., Kristof, Arnold S., Magder, Sheldon A., Di Battista, John A., Hussain, Sabah N. A.

المصدر: Blood; April 2008, Vol. 111 Issue: 8 p4145-4154, 10p

مستخلص: Angiopoietin-1 (Ang-1), ligand for the endothelial cell–specific Tie-2 receptors, promotes migration and proliferation of endothelial cells, however, whether these effects are promoted through the release of a secondary mediator remains unclear. In this study, we assessed whether Ang-1 promotes endothelial cell migration and proliferation through the release of interleukin-8 (IL-8). Ang-1 elicited in human umbilical vein endothelial cells (HUVECs) a dose- and time-dependent increase in IL-8 production as a result of induction of mRNA and enhanced mRNA stability of IL-8 transcripts. IL-8 production is also elevated in HUVECs transduced with retroviruses expressing Ang-1. Neutralization of IL-8 in these cells with a specific antibody significantly attenuated proliferation and migration and induced caspase-3 activation. Exposure to Ang-1 triggered a significant increase in DNA binding of activator protein-1 (AP-1) to a relatively short fragment of IL-8 promoter. Upstream from the AP-1 complex, up-regulation of IL-8 transcription by Ang-1 was mediated through the Erk1/2, SAPK/JNK, and PI-3 kinase pathways, which triggered c-Jun phosphorylation on Ser63 and Ser73. These results suggest that promotion of endothelial migration and proliferation by Ang-1 is mediated, in part, through the production of IL-8, which acts in an autocrine fashion to suppress apoptosis and facilitate cell proliferation and migration.