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Igor P. Udovichenko - One of the best experts on this subject based on the ideXlab platform.

  • Immunosuppressant Peptide Abu-TGIRIS-Abu-NH2 and its Application for Treatment of Multiple Sclerosis.
    Journal of Bionanoscience, 2018
    Co-Authors: Valery I. Turobov, Viatcheslav N. Azev, Alexei B. Shevelev, Natalia V. Pozdniakova, Yulia K. Biryukova, Arkady N. Murashev, Valery M. Lipkin, Igor P. Udovichenko
    Abstract:

    : Immunosuppressant peptide immunocortin for the first time was described in 1993. It corresponds to residues 11-20 of human Ig heavy chain (conserved motif of VH domain). There are no data about production of immunocortin by proteolysis of Ig in vivo. Synthetic immunocortin in concentration ~ 10-9 M suppresses phagocytosis in peritoneal macrophages, ConA-dependent blast transformation of rat lymphocytes, exhibits ACTH-like neurotropic activity and was suggested as a potential drug for treatment of a multiple sclerosis (MS). Here, we report a sequence and method of synthesis of Abu-TGIRIS-Abu-NH2 (Abu, Alpha-Aminobutyric Acid), an artificial analogue of immunocortin. Biological trials of peritoneally injected Abu-TGIRIS-Abu-NH2 gave an evidence of its better efficacy versus immunocortin in a test for suppression of the experimental autoimmune encephalomyelitis (EAE) in Dark Agouti (DA) rats.

  • Immunosuppressant Peptide Abu-TGIRIS-Abu-NH_2 and its Application for Treatment of Multiple Sclerosis
    BioNanoScience, 2018
    Co-Authors: Valery I. Turobov, Viatcheslav N. Azev, Alexei B. Shevelev, Natalia V. Pozdniakova, Yulia K. Biryukova, Arkady N. Murashev, Valery M. Lipkin, Igor P. Udovichenko
    Abstract:

    Immunosuppressant peptide immunocortin for the first time was described in 1993. It corresponds to residues 11–20 of human Ig heavy chain (conserved motif of V_H domain). There are no data about production of immunocortin by proteolysis of Ig in vivo. Synthetic immunocortin in concentration ~ 10^−9 M suppresses phagocytosis in peritoneal macrophages, ConA-dependent blast transformation of rat lymphocytes, exhibits ACTH-like neurotropic activity and was suggested as a potential drug for treatment of a multiple sclerosis (MS). Here, we report a sequence and method of synthesis of Abu-TGIRIS-Abu-NH_2 (Abu, Alpha-Aminobutyric Acid), an artificial analogue of immunocortin. Biological trials of peritoneally injected Abu-TGIRIS-Abu-NH_2 gave an evidence of its better efficacy versus immunocortin in a test for suppression of the experimental autoimmune encephalomyelitis (EAE) in Dark Agouti (DA) rats.

Trond Riise - One of the best experts on this subject based on the ideXlab platform.

  • Cerebrospinal fluid proteins andfree aminoAcids in *patients withsolvent induced chronic toxic encephalopathy andhealthy controls
    1990
    Co-Authors: Benteelisabeth Moen, Kyvik Kr, B A Engelsen, Trond Riise
    Abstract:

    Theconcentrations ofprotein, albumin,IgG, andfreeaminoAcids inthecerebrospinal fluid of16patients withchronictoxicencephalopathyduetoorganic solvents weremeasured. Thepatient groupconsisted ofallpatients with thisdiagnosis inaneurological department in 1985. Thediagnosis wasbasedonneuraesthenic symptoms,pathological psychometric performance,andverified exposuretoneurotoxic organic solvents. A control groupof16patients withmyalgias orbackache, orboth,andno signs ofdisease wasusedforcomparison. The purposewastostudypossible changesinthe cerebrospinal fluidthatmightcontribute to understanding theaetiology ofsolvent induced chronictoxicencephalopathy. A risein protein, albumin,andIgGwasfoundinthe patient groupcomparedwiththecontrol group,aswellasreducedconcentrations of phosphoethanolamine, taurine, homocarnosine, ethanolamine, Alpha-Aminobutyric Acid, andleucine. Usingastepwise multiple regressionanalysis, taurinewas negatively correlated toexposure tosolvents. Thesefindings may indicate membranealterations inthe central nervoussystemrelated toexposure to organic solvents.

  • Cerebrospinal fluid proteins and free amino Acids in patients with solvent induced chronic toxic encephalopathy and healthy controls.
    Occupational and Environmental Medicine, 1990
    Co-Authors: Bente E. Moen, Kyvik Kr, B A Engelsen, Trond Riise
    Abstract:

    The concentrations of protein, albumin, IgG, and free amino Acids in the cerebrospinal fluid of 16 patients with chronic toxic encephalopathy due to organic solvents were measured. The patient group consisted of all patients with this diagnosis in a neurological department in 1985. The diagnosis was based on neuraesthenic symptoms, pathological psychometric performance, and verified exposure to neurotoxic organic solvents. A control group of 16 patients with myalgias or backache, or both, and no signs of disease was used for comparison. The purpose was to study possible changes in the cerebrospinal fluid that might contribute to understanding the aetiology of solvent induced chronic toxic encephalopathy. A rise in protein, albumin, and IgG was found in the patient group compared with the control group, as well as reduced concentrations of phosphoethanolamine, taurine, homocarnosine, ethanolamine, Alpha-Aminobutyric Acid, and leucine. Using a stepwise multiple regression analysis, taurine was negatively correlated to exposure to solvents. These findings may indicate membrane alterations in the central nervous system related to exposure to organic solvents.

Valery I. Turobov - One of the best experts on this subject based on the ideXlab platform.

  • Immunosuppressant Peptide Abu-TGIRIS-Abu-NH2 and its Application for Treatment of Multiple Sclerosis.
    Journal of Bionanoscience, 2018
    Co-Authors: Valery I. Turobov, Viatcheslav N. Azev, Alexei B. Shevelev, Natalia V. Pozdniakova, Yulia K. Biryukova, Arkady N. Murashev, Valery M. Lipkin, Igor P. Udovichenko
    Abstract:

    : Immunosuppressant peptide immunocortin for the first time was described in 1993. It corresponds to residues 11-20 of human Ig heavy chain (conserved motif of VH domain). There are no data about production of immunocortin by proteolysis of Ig in vivo. Synthetic immunocortin in concentration ~ 10-9 M suppresses phagocytosis in peritoneal macrophages, ConA-dependent blast transformation of rat lymphocytes, exhibits ACTH-like neurotropic activity and was suggested as a potential drug for treatment of a multiple sclerosis (MS). Here, we report a sequence and method of synthesis of Abu-TGIRIS-Abu-NH2 (Abu, Alpha-Aminobutyric Acid), an artificial analogue of immunocortin. Biological trials of peritoneally injected Abu-TGIRIS-Abu-NH2 gave an evidence of its better efficacy versus immunocortin in a test for suppression of the experimental autoimmune encephalomyelitis (EAE) in Dark Agouti (DA) rats.

  • Immunosuppressant Peptide Abu-TGIRIS-Abu-NH_2 and its Application for Treatment of Multiple Sclerosis
    BioNanoScience, 2018
    Co-Authors: Valery I. Turobov, Viatcheslav N. Azev, Alexei B. Shevelev, Natalia V. Pozdniakova, Yulia K. Biryukova, Arkady N. Murashev, Valery M. Lipkin, Igor P. Udovichenko
    Abstract:

    Immunosuppressant peptide immunocortin for the first time was described in 1993. It corresponds to residues 11–20 of human Ig heavy chain (conserved motif of V_H domain). There are no data about production of immunocortin by proteolysis of Ig in vivo. Synthetic immunocortin in concentration ~ 10^−9 M suppresses phagocytosis in peritoneal macrophages, ConA-dependent blast transformation of rat lymphocytes, exhibits ACTH-like neurotropic activity and was suggested as a potential drug for treatment of a multiple sclerosis (MS). Here, we report a sequence and method of synthesis of Abu-TGIRIS-Abu-NH_2 (Abu, Alpha-Aminobutyric Acid), an artificial analogue of immunocortin. Biological trials of peritoneally injected Abu-TGIRIS-Abu-NH_2 gave an evidence of its better efficacy versus immunocortin in a test for suppression of the experimental autoimmune encephalomyelitis (EAE) in Dark Agouti (DA) rats.

R Fluhr - One of the best experts on this subject based on the ideXlab platform.

  • beta aminobutyric Acid induces the accumulation of pathogenesis related proteins in tomato lycopersicon esculentum l plants and resistance to late blight infection caused by phytophthora infestans
    Plant Physiology, 1994
    Co-Authors: Yigal Cohen, T Niderman, Egon Mosinger, R Fluhr
    Abstract:

    Tomato (Lycopersicon esculentum L.) plants were sprayed with aqueous solutions of isomers of aminobutyric Acid and were either analyzed for the accumulation of pathogenesis-related (PR) proteins or challenged with the late blight fungal agent Phytophthora infestans. The [beta] isomer of aminobutyric Acid induced the accumulation of high levels of three proteins: P14a, [beta]-1,3 glucanase, and chitinase. These proteins either did not accumulate or accumulated to a much lower level in [alpha]- or [gamma]-aminobutyric Acid-treated plants. Plants pretreated with [alpha]-, [beta]-, and [gamma]-aminobutyric Acid were protected up to 11 d to an extent of 35, 92, and 6%, respectively, against a challenge infection with P. infestans. Protection by [beta]-aminobutyric Acid was afforded against the blight even when the chemical was applied 1 d postinoculation. Examination of ethylene evolution showed that [alpha]-aminobutyric Acid induced the production of 3-fold higher levels of ethylene compared with [beta]-aminobutyric Acid, whereas [gamma]-aminobutyric Acid induced no ethylene production. In addition, silver thiosulfate, a potent inhibitor of ethylene action, did not abolish the resistance induced by [beta]-aminobutyric Acid. The results are consistent with the possibility that [beta]-aminobutyric Acid protects tomato foliage against the late blight disease by a mechanism that is not mediated by ethylene and that PR proteins can be involved in induced resistance.

James Travis - One of the best experts on this subject based on the ideXlab platform.

  • Structural and functional characterization of elastases from horse neutrophils.
    Biochemical Journal, 1994
    Co-Authors: Adam Dubin, Jan Potempa, James Travis
    Abstract:

    In order better to understand the pathophysiology of the equine form of emphysema, two elastinolytic enzymes from horse neutrophils, referred to as proteinases 2A and 2B, have been extensively characterized and compared with the human neutrophil proteinases, proteinase-3 and elastase. Specificity studies using both the oxidized insulin B-chain and synthetic peptides revealed that cleavage of peptide bonds with P1 alanine or valine residues was preferred. Further characterization of the two horse elastases by N-terminal sequence and reactive-site analyses indicated that proteinases 2A and 2B have considerable sequence similarity to each other, to proteinase-3 from human neutrophils (proteinase 2A), to human neutrophil elastase (proteinase 2B) and to a lesser extent to pig pancreatic elastase. Horse and human elastases differed somewhat in their interaction with some natural protein proteinase inhibitors. For example, in contrast with its action on human neutrophil elastase, aprotinin did not inhibit either of the horse proteinases. However, the Val15, Alpha-Aminobutyric Acid-15 (Abu15), alpha-aminovaleric Acid-15 (Nva15) and Ala15 reactive-site variants of aprotinin were good inhibitors of proteinase 2B (Ki 10(-7) M). In summary, despite these differences, the horse neutrophil elastases were found to resemble closely their human counterparts, thus implicating them in the pathological degradation of connective tissue in chronic lung diseases in the equine species.

  • Structural and functional characterization of elastases from horse neutrophils.
    The Biochemical journal, 1994
    Co-Authors: Adam Dubin, Jan Potempa, James Travis
    Abstract:

    In order better to understand the pathophysiology of the equine form of emphysema, two elastinolytic enzymes from horse neutrophils, referred to as proteinases 2A and 2B, have been extensively characterized and compared with the human neutrophil proteinases, proteinase-3 and elastase. Specificity studies using both the oxidized insulin B-chain and synthetic peptides revealed that cleavage of peptide bonds with P1 alanine or valine residues was preferred. Further characterization of the two horse elastases by N-terminal sequence and reactive-site analyses indicated that proteinases 2A and 2B have considerable sequence similarity to each other, to proteinase-3 from human neutrophils (proteinase 2A), to human neutrophil elastase (proteinase 2B) and to a lesser extent to pig pancreatic elastase. Horse and human elastases differed somewhat in their interaction with some natural protein proteinase inhibitors. For example, in contrast with its action on human neutrophil elastase, aprotinin did not inhibit either of the horse proteinases. However, the Val15, Alpha-Aminobutyric Acid-15 (Abu15), alpha-aminovaleric Acid-15 (Nva15) and Ala15 reactive-site variants of aprotinin were good inhibitors of proteinase 2B (Ki < 10(-9) M) but only weak inhibitors of proteinase 2A (Ki > 10(-7) M). In summary, despite these differences, the horse neutrophil elastases were found to resemble closely their human counterparts, thus implicating them in the pathological degradation of connective tissue in chronic lung diseases in the equine species.