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Journal articles on the topic 'Thimet'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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1

Dando, P. M., M. A. Brown, and A. J. Barrett. "Human thimet oligopeptidase." Biochemical Journal 294, no. 2 (September 1, 1993): 451–57. http://dx.doi.org/10.1042/bj2940451.

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We have purified human thimet oligopeptidase to homogeneity from erythrocytes, and compared it with the enzyme from rat testis and chicken liver. An antiserum raised against rat thimet oligopeptidase also recognized the human and chicken enzymes, suggesting that the structure of the enzyme has been strongly conserved in evolution. Consistent with this, the properties of the human enzyme were very similar to those for the other species. Thus human thimet oligopeptidase also is a thiol-dependent metallo-oligopeptidase with M(r) about 75,000. Specificity for cleavage of a number of peptides was indistinguishable from that of the rat enzyme, but Ki values for the four potent reversible inhibitors tested were lower. In discussing the results, we consider the determinants of the complex substrate specificity of thimet oligopeptidase. We question whether substrates containing more than 17 amino acid residues are cleaved, as has been suggested. We also point out that the favourable location of a proline residue and a free C-terminus in the substrate may be as important as the hydrophobic residues in the P2, P1 and P3′ positions that have been emphasized in the past.

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2

McKie, N., P. M. Dando, N. D. Rawlings, and A. J. Barrett. "Thimet oligopeptidase: similarity to ‘soluble angiotensin II-binding protein’ and some corrections to the published amino acid sequence of the rat testis enzyme." Biochemical Journal 295, no. 1 (October 1, 1993): 57–60. http://dx.doi.org/10.1042/bj2950057.

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The deduced amino acid sequence of pig liver soluble angiotensin II-binding protein [Sugiura, Hagiwara and Hirose (1992) J. Biol. Chem. 267, 18067-18072] is similar over most of its length to that reported for rat testis thimet oligopeptidase (EC 3.4.24.15) by Pierotti, Dong, Glucksman, Orlowski and Roberts [(1990) (Biochemistry 29, 10323-10329]. We have found that homogeneous rat testis thimet oligopeptidase binds angiotensin II with the same distinctive characteristics as the pig liver protein. Analysis of the nucleotide sequences reported for the two proteins pointed to the likelihood that sequencing errors had caused two segments of the amino acid sequence of the rat protein to be translated out of frame, and re-sequencing of selected parts of the clone (kindly provided by the previous authors) confirmed this. The revised deduced amino acid sequence of rat thimet oligopeptidase contains 687 residues, representing a protein of 78,308 Da, and is more closely related to those of the pig liver protein and other known homologues of thimet oligopeptidase than that described previously.

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3

Knight, C. G., P. M. Dando, and A. J. Barrett. "Thimet oligopeptidase specificity: evidence of preferential cleavage near the C-terminus and product inhibition from kinetic analysis of peptide hydrolysis." Biochemical Journal 308, no. 1 (May 15, 1995): 145–50. http://dx.doi.org/10.1042/bj3080145.

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The substrate-size specificity of human thimet oligopeptidase (EC 3.4.24.15) was investigated with oligomers of glycyl-prolyl-leucine (GPL)n where n = 2, 3, 4 and 5. These peptides were cleaved only at Leu-Gly bonds to give GPL as the single final product. Hydrolysis was most rapid with (GPL)3 and slowest with (GPL)5. The more water-soluble oligomers of Gly-Hyp-Leu showed the same trend. (Gly-Hyp-Leu)6 was not hydrolysed, consistent with the previous finding that substrates larger than 17 amino acids are not cleaved by thimet oligopeptidase. The cleavage of (GPL)3 to GPL fitted a sequential first-order model. First-order kinetics were unexpected as the initial substrate concentration was greater than Km. The anomaly was also seen during the cleavage of bradykinin and neurotensin, and in these cases first-order behaviour was due to potent competitive inhibition by the C-terminal product. The sequential mechanism for (GPL)3 breakdown by thimet oligopeptidase does not discriminate between initial cleavages towards the N- or C-terminus. As isoleucine is an unfavourable residue in P1, substrates were made in which selected leucine residues were replaced by isoleucine. GPL--GPI--GPL (where--represents the bond between the tripeptide units) was resistant to hydrolysis and GPI--GPL--GPL was cleaved only at the -Leu-Gly- bond. Experiments with isoleucine-containing analogues of (Gly-Hyp-Leu)4 showed that thimet oligopeptidase preferred to cleave these peptides near the C-terminus.

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4

Knight, C. G. "A quenched fluorescent substrate for thimet peptidase containing a new fluorescent amino acid, DL-2-amino-3-(7-methoxy-4-coumaryl)propionic acid." Biochemical Journal 274, no. 1 (February 15, 1991): 45–48. http://dx.doi.org/10.1042/bj2740045.

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DL-2-Amino-3-(7-methoxy-4-coumaryl)propionic acid, a new fluorescent amino acid (abbreviated to Amp), has been synthesized to provide an alternative to tryptophan in quenched fluorescent peptide substrates for peptidases. The model compound Ac-DL-Amp-NH2 was intensely fluorescent with an excitation maximum at 328 nm and an emission maximum at 392 nm. Fmoc (fluoren-9-ylmethoxycarbonyl)-DL-Amp was made to allow the solid-phase synthesis of Amp-containing peptides by the Fmoc-polyamide method. The peptide derivative Dnp (2,4-dinitrophenyl)-Pro-Leu-Gly-Pro-DL-Amp-D-Lys was cleaved by thimet peptidase at the Leu-Gly bond, with a 20-fold enhancement of fluorescence. The value of kcat./Km for thimet peptidase was 6.7 x 10(5) M-1.s-1, compared with the value of 2.4 x 10(5) M-1.s-1 for the tryptophan-containing analogue, Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys.

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5

Hayashi, Mirian A. F., Marcelo D. Gomes, Nancy A. Rebouҫas, Beatriz L. Fernandes, Emer S. Ferro, and Antonio C. M. de Camargo. "Species Specificity of Thimet Oligopeptidase (EC 3.4.24.15)." Biological Chemistry Hoppe-Seyler 377, no. 5 (January 1996): 283–92. http://dx.doi.org/10.1515/bchm3.1996.377.5.283.

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6

Machado, Maurício F. M., Marcelo F. Marcondes, Vanessa Rioli, Emer S. Ferro, Maria A. Juliano, Luiz Juliano, and Vitor Oliveira. "Catalytic properties of thimet oligopeptidase H600A mutant." Biochemical and Biophysical Research Communications 394, no. 2 (April 2010): 429–33. http://dx.doi.org/10.1016/j.bbrc.2010.03.045.

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7

McCOOL, SUZAN, and ADRIAN R. PIEROTTI. "26 Promoter sequence of rat thimet oligopeptidase." Biochemical Society Transactions 26, no. 1 (February 1, 1998): S15. http://dx.doi.org/10.1042/bst026s015.

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8

Chen, Jinq-May, Alvin Changco, Molly A. Brown, and Alan J. Barrett. "Immunolocalization of Thimet Oligopeptidase in Chicken Embryonic Fibroblasts." Experimental Cell Research 216, no. 1 (January 1995): 80–85. http://dx.doi.org/10.1006/excr.1995.1010.

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9

Tisljar, Ursula, and Alan J. Barrett. "A distinct thimet peptidase from rat liver mitochondria." FEBS Letters 264, no. 1 (May 7, 1990): 84–86. http://dx.doi.org/10.1016/0014-5793(90)80771-a.

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10

Iannetta, Anthony A., Holden T. Rogers, Thualfeqar Al‐Mohanna, Juliana N. O’Brien, Andrew J. Wommack, Sorina C. Popescu, and Leslie M. Hicks. "Profiling thimet oligopeptidase‐mediated proteolysis in Arabidopsis thaliana." Plant Journal 106, no. 2 (February 17, 2021): 336–50. http://dx.doi.org/10.1111/tpj.15165.

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11

Molina, Hercilia M., Adriana K. Carmona, Maria Kouyoumdjian, and Durval R. Borges. "Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase." Life Sciences 67, no. 5 (June 2000): 509–20. http://dx.doi.org/10.1016/s0024-3205(00)00650-0.

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12

Icimoto, Marcelo Y., Juliana C. Ferreira, César H. Yokomizo, Larissa V. Bim, Alyne Marem, Joyce M. Gilio, Vitor Oliveira, and Iseli L. Nantes. "Redox modulation of thimet oligopeptidase activity by hydrogen peroxide." FEBS Open Bio 7, no. 7 (June 19, 2017): 1037–50. http://dx.doi.org/10.1002/2211-5463.12245.

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13

Barrett, A. J. "Thimet oligopeptidase (EC 3.4.24.15): the same by any name?" Biochemical Journal 277, no. 1 (July 1, 1991): 295–96. http://dx.doi.org/10.1042/bj2770295.

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14

CAMARGO, Antonio C. M., Marcelo D. GOMES, Antonia P. REICHL, Emer S. FERRO, Saul JACCHIERI, Isaura Y. HIRATA, and Luiz JULIANO. "Structural features that make oligopeptides susceptible substrates for hydrolysis by recombinant thimet oligopeptidase." Biochemical Journal 324, no. 2 (June 1, 1997): 517–22. http://dx.doi.org/10.1042/bj3240517.

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A systematic analysis of the peptide sequences and lengths of several homologues of bioactive peptides and of a number of quenched-fluorescence (qf) opioid- and bradykinin-related peptides was performed to determine the main features leading the oligopeptides to hydrolysis by the recombinant rat testis thimet oligopeptidase (EC 3.4.24.15). The results indicate that a minimum substrate length of six amino acids is required and that among the oligopeptides six to thirteen amino acid residues long, their susceptibility as substrates is highly variable. Thimet oligopeptidase was able to hydrolyse, with similar catalytic efficiency, peptide bonds having hydrophobic or hydrophilic amino acids as well as proline in the P1 position of peptides, ranging from a minimum of six to a maximum of approximately thirteen amino acid residues. An intriguing observation was the shift of the cleavage site, at a Leu-Arg bond in qf dynorphin-(2–8) [qf-Dyn2–8; Abz-GGFLRRV-EDDnp, where Abz stands for o-aminobenzoyl and EDDnp for N-(2,4-dinitrophenyl) ethylenediamine], to Arg-Arg in qf-Dyn2–8Q, in which Gln was substituted for Val at its C-terminus. Similarly, a cleavage site displacement was also observed with the hydrolysis of the internally quenched-fluorescence bradykinin analogues containing Gln at the C-terminal position, namely Abz-RPPGFSPFR-EDDnp and Abz-GFSPFR-EDDnp are cleaved at the Phe-Ser bond, but Abz-RPPGFSPFRQ-EDDnp and Abz-GFSPFRQ-EDDnp are cleaved at the Pro-Phe bond.

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15

MORRISON, Lesley S., and Adrian R. PIEROTTI. "Thimet oligopeptidase expression is differentially regulated in neuroendocrine and spermatid cell lines by transcription factor binding to SRY (sex-determining region Y), CAAT and CREB (cAMP-response-element-binding protein) promoter consensus sequences." Biochemical Journal 376, no. 1 (November 15, 2003): 189–97. http://dx.doi.org/10.1042/bj20030792.

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The zinc metalloprotease thimet oligopeptidase (EP24.15) is found predominantly in the neuroendocrine–gonadal axis where it is implicated in the processing of bioactive peptides, including GnRH (gonadotropin-releasing hormone), β-neoendorphin, α-neoendorphin and dynorphin(1–8), the progression of spermatogenesis and the normal clearance of β-amyloid in brain cells. Regulation of the enzyme's activity may occur in part by phosphorylation and redox disruption of intermolecular disulphide bridges. The elevated levels of both EP24.15 activity and mRNA within testicular and neuroendocrine tissues indicate that EP24.15 gene expression is differentially regulated. In the present paper, we present a detailed analysis of the rat EP24.15 promoter region previously isolated and partially characterized in this laboratory. Employing site-directed mutagenesis to create a series of promoter deletions and full-length promoter mutants, and measuring their activity in luciferase reporter gene and electrophoretic mobility-shift assays, we have shown that the transcription of the EP24.15 gene is differentially regulated in neuroendocrine and spermatid cell lines by transcription factor binding to SRY (sex-determining region Y), CAAT and CREB (cAMP-response-element-binding protein) promoter consensus sequences. The key to identifying the in vivo role of thimet oligopeptidase is likely to be found within the mechanisms by which it is regulated, and it is therefore of particular significance that EP24.15 expression is regulated by SRY and CREB/CREM (cAMP-response element modulator), the principle testes-determining protein and the major orchestrator of spermatogenesis respectively.

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16

JACCHIERI, S. G., M. D. GOMES, L. JULIANO, and A. C. M. CAMARGO. "A comparative conformational analysis of thimet oligopeptidase (EC 3.4.24.15) substrates." Journal of Peptide Research 51, no. 6 (January 12, 2009): 452–59. http://dx.doi.org/10.1111/j.1399-3011.1998.tb00644.x.

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17

Santos, Bruna A. C., Lucas A. F. da Rocha, Emer S. Ferro, and Alice C. Rodrigues. "Deletion Of Thimet Oligopeptidase Attenuates Nash Trough Microrna MIR-34a." Metabolism 116 (March 2021): 154621. http://dx.doi.org/10.1016/j.metabol.2020.154621.

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18

Morrison, Lesley, and Adrian R. Pierotti. "Regulation of expression of Thimet Oligopeptidase by steroids & other modulators." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A83. http://dx.doi.org/10.1042/bst028a083a.

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19

Lim, Eun Jeong, Sowmya Sampath, Jerry Coll-Rodriguez, Jack Schmidt, Kallol Ray, and David W. Rodgers. "Swapping the Substrate Specificities of the Neuropeptidases Neurolysin and Thimet Oligopeptidase." Journal of Biological Chemistry 282, no. 13 (January 24, 2007): 9722–32. http://dx.doi.org/10.1074/jbc.m609897200.

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20

Ferro, Emer S., Mayara C. F. Gewehr, and Ami Navon. "Thimet Oligopeptidase Biochemical and Biological Significances: Past, Present, and Future Directions." Biomolecules 10, no. 9 (August 24, 2020): 1229. http://dx.doi.org/10.3390/biom10091229.

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Thimet oligopeptidase (EC 3.4.24.15; EP24.15, THOP1) is a metallopeptidase ubiquitously distributed in mammalian tissues. Beyond its previously well characterized role in major histocompatibility class I (MHC-I) antigen presentation, the recent characterization of the THOP1 C57BL6/N null mice (THOP1−/−) phenotype suggests new key functions for THOP1 in hyperlipidic diet-induced obesity, insulin resistance and non-alcoholic liver steatosis. Distinctive levels of specific intracellular peptides (InPeps), genes and microRNAs were observed when comparing wild type C57BL6/N to THOP1−/− fed either standard or hyperlipidic diets. A possible novel mechanism of action was suggested for InPeps processed by THOP1, which could be modulating protein-protein interactions and microRNA processing, thus affecting the phenotype. Together, research into the biochemical and biomedical significance of THOP1 suggests that degradation by the proteasome is a step in the processing of various proteins, not merely for ending their existence. This allows many functional peptides to be generated by proteasomal degradation in order to, for example, control mRNA translation and the formation of protein complexes.

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21

Savković, N., J. Pečevski, D. Alavantić, Lj Vuksanović, I. Sunjevarić, and D. Radivojević. "Mutagenicity in mice induced by commercial mixture of thimet/phorate + lindane." Mutation Research/Environmental Mutagenesis and Related Subjects 147, no. 5 (October 1985): 318. http://dx.doi.org/10.1016/0165-1161(85)90203-1.

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22

Hoozemans, Jeroen J. M., Elise S. van Haastert, Thierry Hazes, Andrea Caricasole, Guiseppe Pollio, Georg C. Terstappen, and Annemieke J. M. Rozemuller. "P2-163: Thimet oligopeptidase expression is increased in Alzheimer's disease brain." Alzheimer's & Dementia 4 (July 2008): T418. http://dx.doi.org/10.1016/j.jalz.2008.05.1237.

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23

Pineau, C., S. McCool, M. J. Glucksman, B. Jegou, and A. R. Pierotti. "Distribution of thimet oligopeptidase (E.C. 3.4.24.15) in human and rat testes." Journal of Cell Science 112, no. 20 (October 15, 1999): 3455–62. http://dx.doi.org/10.1242/jcs.112.20.3455.

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Thimet oligopeptidase (TOP:E.C. 3.4.24.15) is a thiol sensitive metalloendopeptidase which is widely distributed and active in most tissues including testis, brain and pituitary. In the median eminence it is postulated to play a role in the degradation of GnRH released from the hypothalamus and thus to modulate LH levels. In the rat and human, the testis is the richest source of TOP activity with levels 3- to 5-fold higher than that of the brain. In order to define the exact localisation of this enzyme within the rat and human testis, the distribution of TOP in the developing and adult gonad was examined in situ and in isolated cells by immunohistochemistry, western blotting and northern blotting analysis. Ontogeny studies have demonstrated that TOP is detectable by western blotting from 9 days with levels of expression increasing with the age of the animal. Immunolocalisation of the protein in the interstitium was positive from 9 days onwards but was negative within the seminiferous tubules before 35 days of age, whereas TOP mRNA was not detected within the testis until 35 days of age with subsequent stable expression levels up to 90 days. In the adult rat testis, a strong TOP immunoreactivity was observed within seminiferous tubules, in elongating and elongated spermatids and residual bodies. In the interstitial compartment, immunoreactivity was also observed in Leydig cells and throughout the interstitial space. Western blot analyses confirmed the distribution of expression observed using immunochemistry, however Leydig cells display a lower signal than expected from the immunohistochemical data. Northern hybridization showed that the transcript is present in pachytene spermatocytes, early spermatids, and residual bodies, whereas its presence was not observed in Leydig cells probably due to very low levels of expression of the message. Analyses of various human tissue extracts showed that the testis displays the highest levels of TOP mRNA, with immunohistochemical experiments revealing that, as in the rat, the protein is principally expressed in elongated spermatids/residual bodies, and in Leydig cells. It is concluded that in the human and rat testes, TOP is highly expressed, in particular in post-meiotic germ cells and Leydig cells. The possible involvement of TOP in proteolytic events associated with the process of spermiogenesis and Leydig cell function is currently under investigation.

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24

Oliveira, Vitor, Marcelo Campos, Robson L. Melo, Emer S. Ferro, Antonio C. M. Camargo, Maria A. Juliano, and Luiz Juliano. "Substrate Specificity Characterization of Recombinant Metallo Oligo-Peptidases Thimet Oligopeptidase and Neurolysin†." Biochemistry 40, no. 14 (April 2001): 4417–25. http://dx.doi.org/10.1021/bi002715k.

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25

Sigman, J. A., M. L. Sharky, S. T. Walsh, A. Pabon, M. J. Glucksman, and A. J. Wolfson. "Involvement of surface cysteines in activity and multimer formation of thimet oligopeptidase." Protein Engineering Design and Selection 16, no. 8 (August 1, 2003): 623–28. http://dx.doi.org/10.1093/protein/gzg073.

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26

KNIGHT, C. GRAHAM, and ALAN J. BARRETT. "N-[1(RS)-Carboxy-3-phenylpropyl]peptides as inhibitors of thimet oligopeptidase." Biochemical Society Transactions 19, no. 3 (August 1, 1991): 290S. http://dx.doi.org/10.1042/bst019290s.

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27

dos Santos, Nilton, Roseane Franco, Rosana Camarini, Carolina Munhoz, Rosangela Eichler, Mayara Gewehr, Patricia Reckziegel, et al. "Thimet Oligopeptidase (EC 3.4.24.15) Key Functions Suggested by Knockout Mice Phenotype Characterization." Biomolecules 9, no. 8 (August 19, 2019): 382. http://dx.doi.org/10.3390/biom9080382.

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Thimet oligopeptidase (THOP1) is thought to be involved in neuropeptide metabolism, antigen presentation, neurodegeneration, and cancer. Herein, the generation of THOP1 C57BL/6 knockout mice (THOP1−/−) is described showing that they are viable, have estrus cycle, fertility, and a number of puppies per litter similar to C57BL/6 wild type mice (WT). In specific brain regions, THOP1-/- exhibit altered mRNA expression of proteasome beta5, serotonin 5HT2a receptor and dopamine D2 receptor, but not of neurolysin (NLN). Peptidomic analysis identifies differences in intracellular peptide ratios between THOP1-/- and WT mice, which may affect normal cellular functioning. In an experimental model of multiple sclerosis THOP1-/- mice present worse clinical behavior scores compared to WT mice, corroborating its possible involvement in neurodegenerative diseases. THOP1-/- mice also exhibit better survival and improved behavior in a sepsis model, but also a greater peripheral pain sensitivity measured in the hot plate test after bradykinin administration in the paw. THOP1-/- mice show depressive-like behavior, as well as attention and memory retention deficits. Altogether, these results reveal a role of THOP1 on specific behaviors, immune-stimulated neurodegeneration, and infection-induced inflammation.

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28

Kessler, Jan H., Selina Khan, Ulrike Seifert, Sylvie Le Gall, K. Martin Chow, Annette Paschen, Sandra A. Bres-Vloemans, et al. "Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes." Nature Immunology 12, no. 1 (December 12, 2010): 45–53. http://dx.doi.org/10.1038/ni.1974.

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29

SIGMAN, Jeffrey A., Tasneem H. PATWA, Ana V. TABLANTE, Calleen D. JOSEPH, Marc J. GLUCKSMAN, and Adele J. WOLFSON. "Flexibility in substrate recognition by thimet oligopeptidase as revealed by denaturation studies." Biochemical Journal 388, no. 1 (May 10, 2005): 255–61. http://dx.doi.org/10.1042/bj20041481.

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Thimet oligopeptidase (TOP) is a soluble metalloendopeptidase belonging to a family of enzymes including neurolysin and neprilysin that utilize the HEXXH metal-binding motif. TOP is widely distributed among cell types and is able to cleave a number of structurally unrelated peptides. A recent focus of interest has been on structure–function relationships in substrate selectivity by TOP. The enzyme's structural fold comprises two domains that are linked at the bottom of a deep substrate-binding cleft via several flexible loop structures. In the present study, fluorescence spectroscopy has been used to probe structural changes in TOP induced by the chemical denaturant urea. Fluorescence emission, anisotropy and collisional quenching data support a two-step unfolding process for the enzyme in which complete loss of the tertiary structure occurs in the second step. Complete loss of activity and loss of catalytic Zn(II) from the active site, monitored by absorption changes of the metal chelator 4-(2-pyridylazo)-resorcinol, are also connected with the second step. In contrast, the first unfolding event, which is linked to changes in the non-catalytic domain, leads to a sharp increase in kcat towards a 9-residue substrate and a sharp decrease in kcat for a 5-residue substrate. Thus a conformational change in TOP has been directly correlated with a change in substrate selectivity. These results provide insight into how the enzyme can process the range of structurally unrelated peptides necessary for its many physiological roles.

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30

Pandita, T. K. "Evaluation of Thimet 10-G for mutagenicity by 4 different genetic systems." Mutation Research/Genetic Toxicology 171, no. 2-3 (August 1986): 131–38. http://dx.doi.org/10.1016/0165-1218(86)90045-5.

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31

Knight, C. Graham, and Alan J. Barrett. "Structure/function relationships in the inhibition of thimet oligopeptidase by carboxyphenylpropyl-peptides." FEBS Letters 294, no. 3 (December 9, 1991): 183–86. http://dx.doi.org/10.1016/0014-5793(91)80664-o.

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32

Dalio, Fernanda M., Bruna Visniauskas, Eliane S. Bicocchi, Juliana C. Perry, Rodrigo Freua, Tarsis F. Gesteira, Helena B. Nader, et al. "Acute cocaine treatment increases thimet oligopeptidase in the striatum of rat brain." Biochemical and Biophysical Research Communications 419, no. 4 (March 2012): 724–27. http://dx.doi.org/10.1016/j.bbrc.2012.02.088.

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33

Visniauskas, Bruna, Priscila S. R. Simões, Fernanda M. Dalio, Maria D. G. Naffah-Mazzacoratti, Vitor Oliveira, Sergio Tufik, and Jair R. Chagas. "Sleep deprivation changes thimet oligopeptidase (THOP1) expression and activity in rat brain." Heliyon 5, no. 11 (November 2019): e02896. http://dx.doi.org/10.1016/j.heliyon.2019.e02896.

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34

Wang, Ruiying, Krithika Rajagopalan, Kianoush Sadre-Bazzaz, Magali Moreau, Daniel F. Klessig, and Liang Tong. "Structure of theArabidopsis thalianaTOP2 oligopeptidase." Acta Crystallographica Section F Structural Biology Communications 70, no. 5 (April 15, 2014): 555–59. http://dx.doi.org/10.1107/s2053230x14006128.

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Thimet oligopeptidase (TOP) is a zinc-dependent metallopeptidase. Recent studies suggest thatArabidopsis thalianaTOP1 and TOP2 are targets for salicylic acid (SA) binding and participate in SA-mediated plant innate immunity. The crystal structure ofA. thalianaTOP2 has been determined at 3.0 Å resolution. Comparisons to the structure of human TOP revealed good overall structural conservation, especially in the active-site region, despite their weak sequence conservation. The protein sample was incubated with the photo-activated SA analog 4-azido-SA and exposed to UV irradiation before crystallization. However, there was no conclusive evidence for the binding of SA based on the X-ray diffraction data. Further studies are needed to elucidate the molecular mechanism of how SA regulates the activity ofA. thalianaTOP1 and TOP2.

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35

McKie, N., P. M. Dando, M. A. Brown, and A. J. Barrett. "Rat thimet oligopeptidase: large-scale expression in Escherichia coli and characterization of the recombinant enzyme." Biochemical Journal 309, no. 1 (July 1, 1995): 203–7. http://dx.doi.org/10.1042/bj3090203.

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The coding sequence for rat testis thimet oligopeptidase (TOP) (EC 3.4.24.15) was placed under the control of the T7 polymerase/promoter system. Cultures of Escherichia coli transfected with the resulting plasmid expressed the enzyme as a soluble cytoplasmic protein. Medium-scale cultures allowed isolation of the enzyme in quantities of tens of milligrams. The availability of the recombinant enzyme permitted the determination of such chemical properties as epsilon 280 (48,960), zinc content (2 atom/molecule) and available thiol content (8-10/molecule) for TOP. The recombinant enzyme showed the catalytic activities previously reported for the naturally occurring enzyme, so that we can now conclude with confidence that these are all due to TOP and there is no need to postulate the existence of separate ‘Pz-peptidase’ or ‘endo-oligopeptidase A’ enzymes.

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36

Russo, Lilian C., Camila N. Goñi, Leandro M. Castro, Amanda F. Asega, Antonio C. M. Camargo, Cleber A. Trujillo, Henning Ulrich, Marc J. Glucksman, Cristoforo Scavone, and Emer S. Ferro. "Interaction with calmodulin is important for the secretion of thimet oligopeptidase following stimulation." FEBS Journal 276, no. 16 (August 2009): 4358–71. http://dx.doi.org/10.1111/j.1742-4658.2009.07144.x.

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37

Portaro, Fernanda C. V., Marcelo D. Gomes, Adriana Cabrera, Beatriz L. Fernandes, Celio L. Silva, Emer S. Ferro, Luis Juliano, and Antonio C. M. de Camargo. "Thimet Oligopeptidase and the Stability of MHC Class I Epitopes in Macrophage Cytosol." Biochemical and Biophysical Research Communications 255, no. 3 (February 1999): 596–601. http://dx.doi.org/10.1006/bbrc.1999.0251.

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38

Shrimpton, Corie N., Adele J. Wolfson, A. Ian Smith, and Rebecca A. Lew. "Regulators of the neuropeptide-degrading enzyme, EC 3.4.24.15 (thimet oligopeptidase), in cerebrospinal fluid." Journal of Neuroscience Research 74, no. 3 (October 28, 2003): 474–78. http://dx.doi.org/10.1002/jnr.10698.

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39

Serizawa, Atsushi, Pamela M. Dando, and Alan J. Barrett. "Characterization of a Mitochondrial Metallopeptidase Reveals Neurolysin as a Homologue of Thimet Oligopeptidase." Journal of Biological Chemistry 270, no. 5 (February 3, 1995): 2092–98. http://dx.doi.org/10.1074/jbc.270.5.2092.

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40

Smith, A. I., C. N. Shrimpton, U. M. Norman, I. J. Clarke, A. J. Wolfson, and R. A. Lew. "Neuropeptidases regulating gonadal function." Biochemical Society Transactions 28, no. 4 (August 1, 2000): 430–34. http://dx.doi.org/10.1042/bst0280430.

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The generation and metabolism of bioactive peptides involves a series of highly ordered proteolytic events. This post-translational processing can occur either within the cell, at the cell surface or after secretion. In the central nervous system a number of extracellular peptidases have been implicated in the regulated processing of peptides, particularly in the regulation of neuroendocrine function. The aim of this study has been to identify the peptidases involved in the metabolism of gonadotropin-releasing hormone (GnRH) and to characterize the factors and the mechanisms by which the activity of these peptidases are regulated. We have shown that both prolylendo-peptidase and the thimet oligopeptidase EC 3.4.24.15 are involved in GnRH metabolism and that both oestrogen and thiol-based reductants could be involved in the physiological regulation of their activities.

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41

Ray, Kallol, Christina S. Hines, Jerry Coll-Rodriguez, and David W. Rodgers. "Crystal Structure of Human Thimet Oligopeptidase Provides Insight into Substrate Recognition, Regulation, and Localization." Journal of Biological Chemistry 279, no. 19 (March 3, 2004): 20480–89. http://dx.doi.org/10.1074/jbc.m400795200.

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Thimet oligopeptidase (TOP) is a zinc metallopeptidase that metabolizes a number of bioactive peptides and degrades peptides released by the proteasome, limiting antigenic presentation by MHC class I molecules. We present the crystal structure of human TOP at 2.0-Å resolution. The active site is located at the base of a deep channel that runs the length of the elongated molecule, an overall fold first seen in the closely related metallopeptidase neurolysin. Comparison of the two related structures indicates hinge-like flexibility and identifies elements near one end of the channel that adopt different conformations. Relatively few of the sequence differences between TOP and neurolysin map to the proposed substrate-binding site, and four of these variable residues may account for differences in substrate specificity. In addition, a loop segment (residues 599-611) in TOP differs in conformation and degree of order from the corresponding neurolysin loop, suggesting it may also play a role in activity differences. Cysteines thought to mediate covalent oligomerization of rat TOP, which can inactivate the enzyme, are found to be surface-accessible in the human enzyme, and additional cysteines (residues 321,350, and 644) may also mediate multimerization in the human homolog. Disorder in the N terminus of TOP indicates it may be involved in subcellular localization, but a potential nuclear import element is found to be part of a helix and, therefore, unlikely to be involved in transport. A large acidic patch on the surface could potentially mediate a protein-protein interaction, possibly through formation of a covalent linkage.

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42

McCool, Suzan, and Adrian R. Pierotti. "Expression of the Thimet Oligopeptidase Gene is Regulated by Positively and Negatively Acting Elements." DNA and Cell Biology 19, no. 12 (December 2000): 729–38. http://dx.doi.org/10.1089/104454900750058099.

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43

Ray, Kallol, Christina S. Hines, and David W. Rodgers. "Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition." Protein Science 11, no. 9 (January 1, 2009): 2237–46. http://dx.doi.org/10.1110/ps.0216302.

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44

Dubois, V., M. Nieder, F. Collot, A. Negrouk, T. T. Nguyen, S. Gangwar, B. Reitz, R. Wattiez, L. Dasnois, and A. Trouet. "Thimet oligopeptidase (EC 3.4.24.15) activates CPI-0004Na, an extracellularly tumour-activated prodrug of doxorubicin." European Journal of Cancer 42, no. 17 (November 2006): 3049–56. http://dx.doi.org/10.1016/j.ejca.2005.10.030.

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45

Speese, John. "Use of Soil and Foliar Insecticides to Control Thrips and Leafhoppers in Snapbeans, 1995." Arthropod Management Tests 21, no. 1 (January 1, 1996): 86–87. http://dx.doi.org/10.1093/amt/21.1.86.

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Abstract Snapbeans were planted on 18 May at the Eastern Shore Agricultural Research and Extension Center, Painter, VA. Each plot consisted of 2 rows 25 ft long and planted on 3 ft row spacing. Plots were bordered on each side by an untreated guard row. Each treatment was replicated 4 times in a RCBD. Granular treatments were applied in furrow prior to planting using a hand-held shaker. DiSyston and Thimet granules were manually incorporated to avoid direct contact with the seeds and phytotoxicity. The Orthene foliar spray was applied on 9 June, after the formation of the first trifoliate leaves, with a three-nozzle boom backpack sprayer delivering 60 gal water/acre at 40 psi. To evaluate efficacy, 10 trifoliate leaves/plot were randomly picked on the dates indicated in the table, washed in soapy water, and filtered through a Buchner funnel. Thrips and PLH nymphs were then counted under a stereoscopic microscope.

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Chen, Jinq-May, Richard A. E. Stevens, Paul W. Wray, Neil D. Rawlings, and Alan J. Barrett. "Thimet oligopeptidase: site-directed mutagenesis disproves previous assumptions about the nature of the catalytic site." FEBS Letters 435, no. 1 (September 11, 1998): 16–20. http://dx.doi.org/10.1016/s0014-5793(98)01032-1.

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47

Morowati, Mohssen. "Inhalation toxicity studies of thimet (phorate) in male Swiss albino mouse, Mus musculus: I. Hepatotoxicity." Environmental Pollution 96, no. 3 (1997): 283–88. http://dx.doi.org/10.1016/s0269-7491(97)00052-3.

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48

Sigman, Jeffrey A., Sarah R. Edwards, Amanda Pabon, Marc J. Glucksman, and Adele J. Wolfson. "pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15)." FEBS Letters 545, no. 2-3 (May 24, 2003): 224–28. http://dx.doi.org/10.1016/s0014-5793(03)00548-9.

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49

Gewehr, Mayara C. F., Alexandre A. S. Teixeira, Bruna A. C. Santos, Luana A. Biondo, Fábio C. Gozzo, Amanda M. Cordibello, Rosangela A. S. Eichler, et al. "The Relevance of Thimet Oligopeptidase in the Regulation of Energy Metabolism and Diet-Induced Obesity." Biomolecules 10, no. 2 (February 17, 2020): 321. http://dx.doi.org/10.3390/biom10020321.

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Thimet oligopeptidase (EC 3.4.24.15; EP24.15; THOP1) is a potential therapeutic target, as it plays key biological functions in processing biologically functional peptides. The structural conformation of THOP1 provides a unique restriction regarding substrate size, in that it only hydrolyzes peptides (optimally, those ranging from eight to 12 amino acids) and not proteins. The proteasome activity of hydrolyzing proteins releases a large number of intracellular peptides, providing THOP1 substrates within cells. The present study aimed to investigate the possible function of THOP1 in the development of diet-induced obesity (DIO) and insulin resistance by utilizing a murine model of hyperlipidic DIO with both C57BL6 wild-type (WT) and THOP1 null (THOP1−/−) mice. After 24 weeks of being fed a hyperlipidic diet (HD), THOP1−/− and WT mice ingested similar chow and calories; however, the THOP1−/− mice gained 75% less body weight and showed neither insulin resistance nor non-alcoholic fatty liver steatosis when compared to WT mice. THOP1−/− mice had increased adrenergic-stimulated adipose tissue lipolysis as well as a balanced level of expression of genes and microRNAs associated with energy metabolism, adipogenesis, or inflammation. Altogether, these differences converge to a healthy phenotype of THOP1−/− fed a HD. The molecular mechanism that links THOP1 to energy metabolism is suggested herein to involve intracellular peptides, of which the relative levels were identified to change in the adipose tissue of WT and THOP1−/− mice. Intracellular peptides were observed by molecular modeling to interact with both pre-miR-143 and pre-miR-222, suggesting a possible novel regulatory mechanism for gene expression. Therefore, we successfully demonstrated the previously anticipated relevance of THOP1 in energy metabolism regulation. It was suggested that intracellular peptides were responsible for mediating the phenotypic differences that are described herein by a yet unknown mechanism of action.

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Ferreira, Juliana C., Marcelo Y. Icimoto, Marcelo F. Marcondes, Vitor Oliveira, Otaciro R. Nascimento, and Iseli L. Nantes. "Recycling of the High Valence States of Heme Proteins by Cysteine Residues of Thimet-Oligopeptidase." PLoS ONE 8, no. 11 (November 1, 2013): e79102. http://dx.doi.org/10.1371/journal.pone.0079102.

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