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Placental Leucine Aminopeptidase as a Potential Specific Urine Biomarker for Invasive Ovarian Cancer.

Journal of clinical medicine

Matsukawa T, Mizutani S, Matsumoto K, Kato Y, Yoshihara M, Kajiyama H, Shibata K.
PMID: 35011963
J Clin Med. 2021 Dec 31;11(1). doi: 10.3390/jcm11010222.

BACKGROUND: A non-invasive and sensitive biomarker for the detection of ovarian cancer (OvCa) is lacking. We aim to investigate if urinary placental leucine aminopeptidase (P-LAP) can serve as a reliable biomarker for OvCa.METHODS: P-LAP activity was measured using a...

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Matsukawa T, Mizutani S, Matsumoto K, et al. Placental Leucine Aminopeptidase as a Potential Specific Urine Biomarker for Invasive Ovarian Cancer. J Clin Med. 2021;11(1)doi: 10.3390/jcm11010222.
Matsukawa, T., Mizutani, S., Matsumoto, K., Kato, Y., Yoshihara, M., Kajiyama, H., & Shibata, K. (2021). Placental Leucine Aminopeptidase as a Potential Specific Urine Biomarker for Invasive Ovarian Cancer. Journal of clinical medicine, 11(1), . https://doi.org/10.3390/jcm11010222
Matsukawa, Tetsuya, et al. "Placental Leucine Aminopeptidase as a Potential Specific Urine Biomarker for Invasive Ovarian Cancer." Journal of clinical medicine vol. 11,1 (2021). doi: https://doi.org/10.3390/jcm11010222
Matsukawa T, Mizutani S, Matsumoto K, Kato Y, Yoshihara M, Kajiyama H, Shibata K. Placental Leucine Aminopeptidase as a Potential Specific Urine Biomarker for Invasive Ovarian Cancer. J Clin Med. 2021 Dec 31;11(1). doi: 10.3390/jcm11010222. PMID: 35011963.
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The Type of Fat in the Diet Influences Regulatory Aminopeptidases of the Renin-Angiotensin System and Stress in the Hypothalamic-Pituitary-Adrenal Axis in Adult Wistar Rats.

Nutrients

Domínguez-Vías G, Segarra AB, Ramírez-Sánchez M, Prieto I.
PMID: 34836194
Nutrients. 2021 Nov 04;13(11). doi: 10.3390/nu13113939.

(1) Background: Prolonged feeding with a high-fat diet (HFD) acts as a stressor by activating the functions of the hypothalamic-pituitary-adrenal gland (HPA) stress axis, accompanied of hypertension by inducing the renin-angiotensin-aldosterone system. Angiotensinases enzymes are regulatory aminopeptidases of angiotensin...

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Domínguez-Vías G, Segarra AB, Ramírez-Sánchez M, et al. The Type of Fat in the Diet Influences Regulatory Aminopeptidases of the Renin-Angiotensin System and Stress in the Hypothalamic-Pituitary-Adrenal Axis in Adult Wistar Rats. Nutrients. 2021;13(11)doi: 10.3390/nu13113939.
Domínguez-Vías, G., Segarra, A. B., Ramírez-Sánchez, M., & Prieto, I. (2021). The Type of Fat in the Diet Influences Regulatory Aminopeptidases of the Renin-Angiotensin System and Stress in the Hypothalamic-Pituitary-Adrenal Axis in Adult Wistar Rats. Nutrients, 13(11), . https://doi.org/10.3390/nu13113939
Domínguez-Vías, Germán, et al. "The Type of Fat in the Diet Influences Regulatory Aminopeptidases of the Renin-Angiotensin System and Stress in the Hypothalamic-Pituitary-Adrenal Axis in Adult Wistar Rats." Nutrients vol. 13,11 (2021). doi: https://doi.org/10.3390/nu13113939
Domínguez-Vías G, Segarra AB, Ramírez-Sánchez M, Prieto I. The Type of Fat in the Diet Influences Regulatory Aminopeptidases of the Renin-Angiotensin System and Stress in the Hypothalamic-Pituitary-Adrenal Axis in Adult Wistar Rats. Nutrients. 2021 Nov 04;13(11). doi: 10.3390/nu13113939. PMID: 34836194; PMCID: PMC8625891.
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The Long-Term Study of Urinary Biomarkers of Renal Injury in Spontaneously Hypertensive Rats.

Kidney & blood pressure research

Montoro-Molina S, Quesada A, O'Valle F, Morales NM, de Gracia MDC, Rodríguez-Gómez I, Osuna A, Wangensteen R, Vargas F.
PMID: 34237745
Kidney Blood Press Res. 2021;46(4):502-513. doi: 10.1159/000516843. Epub 2021 Jul 08.

BACKGROUND: The age-related increase in blood pressure in spontaneously hypertensive rats (SHRs) is associated to cardiac hypertrophy, heart failure, and renal injury. Here, we investigated for the first time the urinary enzymatic activities of glutamil aminopeptidase (GluAp), alanyl aminopeptidase...

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Montoro-Molina S, Quesada A, O'Valle F, et al. The Long-Term Study of Urinary Biomarkers of Renal Injury in Spontaneously Hypertensive Rats. Kidney Blood Press Res. 2021;46(4):502-513doi: 10.1159/000516843.
Montoro-Molina, S., Quesada, A., O'Valle, F., Morales, N. M., de Gracia, M. D. C., Rodríguez-Gómez, I., Osuna, A., Wangensteen, R., & Vargas, F. (2021). The Long-Term Study of Urinary Biomarkers of Renal Injury in Spontaneously Hypertensive Rats. Kidney & blood pressure research, 46(4), 502-513. https://doi.org/10.1159/000516843
Montoro-Molina, Sebastián, et al. "The Long-Term Study of Urinary Biomarkers of Renal Injury in Spontaneously Hypertensive Rats." Kidney & blood pressure research vol. 46,4 (2021): 502-513. doi: https://doi.org/10.1159/000516843
Montoro-Molina S, Quesada A, O'Valle F, Morales NM, de Gracia MDC, Rodríguez-Gómez I, Osuna A, Wangensteen R, Vargas F. The Long-Term Study of Urinary Biomarkers of Renal Injury in Spontaneously Hypertensive Rats. Kidney Blood Press Res. 2021;46(4):502-513. doi: 10.1159/000516843. Epub 2021 Jul 08. PMID: 34237745.
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Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.

Proceedings of the National Academy of Sciences of the United States of America

Chen SJ, Kim L, Song HK, Varshavsky A.
PMID: 34663735
Proc Natl Acad Sci U S A. 2021 Oct 26;118(43). doi: 10.1073/pnas.2115430118.

N-degron pathways are proteolytic systems that recognize proteins bearing N-terminal (Nt) degradation signals (degrons) called N-degrons. Our previous work identified Gid4 as a recognition component (N-recognin) of the

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Chen SJ, Kim L, Song HK, et al. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 2021;118(43)doi: 10.1073/pnas.2115430118.
Chen, S. J., Kim, L., Song, H. K., & Varshavsky, A. (2021). Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proceedings of the National Academy of Sciences of the United States of America, 118(43), . https://doi.org/10.1073/pnas.2115430118
Chen, Shun-Jia, et al. "Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway." Proceedings of the National Academy of Sciences of the United States of America vol. 118,43 (2021). doi: https://doi.org/10.1073/pnas.2115430118
Chen SJ, Kim L, Song HK, Varshavsky A. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 2021 Oct 26;118(43). doi: 10.1073/pnas.2115430118. PMID: 34663735.
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Recent Advances in the Endogenous Brain Renin-Angiotensin System and Drugs Acting on It.

Journal of the renin-angiotensin-aldosterone system : JRAAS

Urmila A, Rashmi P, Nilam G, Subhash B.
PMID: 34925551
J Renin Angiotensin Aldosterone Syst. 2021 Nov 30;2021:9293553. doi: 10.1155/2021/9293553. eCollection 2021.

The RAS (renin-angiotensin system) is the part of the endocrine system that plays a prime role in the control of essential hypertension. Since the discovery of brain RAS in the seventies, continuous efforts have been put by the scientific...

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Urmila A, Rashmi P, Nilam G, et al. Recent Advances in the Endogenous Brain Renin-Angiotensin System and Drugs Acting on It. J Renin Angiotensin Aldosterone Syst. 2021;2021:9293553doi: 10.1155/2021/9293553.
Urmila, A., Rashmi, P., Nilam, G., & Subhash, B. (2021). Recent Advances in the Endogenous Brain Renin-Angiotensin System and Drugs Acting on It. Journal of the renin-angiotensin-aldosterone system : JRAAS, 20219293553. https://doi.org/10.1155/2021/9293553
Urmila, Aswar, et al. "Recent Advances in the Endogenous Brain Renin-Angiotensin System and Drugs Acting on It." Journal of the renin-angiotensin-aldosterone system : JRAAS vol. 2021 (2021): 9293553. doi: https://doi.org/10.1155/2021/9293553
Urmila A, Rashmi P, Nilam G, Subhash B. Recent Advances in the Endogenous Brain Renin-Angiotensin System and Drugs Acting on It. J Renin Angiotensin Aldosterone Syst. 2021 Nov 30;2021:9293553. doi: 10.1155/2021/9293553. eCollection 2021. PMID: 34925551; PMCID: PMC8651430.
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Melflufen: A Peptide-Drug Conjugate for the Treatment of Multiple Myeloma.

Journal of clinical medicine

Mateos MV, Bladé J, Bringhen S, Ocio EM, Efebera Y, Pour L, Gay F, Sonneveld P, Gullbo J, Richardson PG.
PMID: 32992506
J Clin Med. 2020 Sep 27;9(10). doi: 10.3390/jcm9103120.

Despite the availability of new therapies that have led to improved outcomes for patients with multiple myeloma, most patients will eventually relapse. With triplet and even quadruplet combination therapies becoming standard in the first and second line, many patients...

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Mateos MV, Bladé J, Bringhen S, et al. Melflufen: A Peptide-Drug Conjugate for the Treatment of Multiple Myeloma. J Clin Med. 2020;9(10)doi: 10.3390/jcm9103120.
Mateos, M. V., Bladé, J., Bringhen, S., Ocio, E. M., Efebera, Y., Pour, L., Gay, F., Sonneveld, P., Gullbo, J., & Richardson, P. G. (2020). Melflufen: A Peptide-Drug Conjugate for the Treatment of Multiple Myeloma. Journal of clinical medicine, 9(10), . https://doi.org/10.3390/jcm9103120
Mateos, María-Victoria, et al. "Melflufen: A Peptide-Drug Conjugate for the Treatment of Multiple Myeloma." Journal of clinical medicine vol. 9,10 (2020). doi: https://doi.org/10.3390/jcm9103120
Mateos MV, Bladé J, Bringhen S, Ocio EM, Efebera Y, Pour L, Gay F, Sonneveld P, Gullbo J, Richardson PG. Melflufen: A Peptide-Drug Conjugate for the Treatment of Multiple Myeloma. J Clin Med. 2020 Sep 27;9(10). doi: 10.3390/jcm9103120. PMID: 32992506; PMCID: PMC7601491.
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Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.

Proceedings of the National Academy of Sciences of the United States of America

Chen SJ, Kim L, Song HK, Varshavsky A.
PMID: 34663735
Proc Natl Acad Sci U S A. 2021 Oct 26;118(43). doi: 10.1073/pnas.2115430118.

N-degron pathways are proteolytic systems that recognize proteins bearing N-terminal (Nt) degradation signals (degrons) called N-degrons. Our previous work identified Gid4 as a recognition component (N-recognin) of the

Cite
Chen SJ, Kim L, Song HK, et al. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 2021;118(43)doi: 10.1073/pnas.2115430118.
Chen, S. J., Kim, L., Song, H. K., & Varshavsky, A. (2021). Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proceedings of the National Academy of Sciences of the United States of America, 118(43), . https://doi.org/10.1073/pnas.2115430118
Chen, Shun-Jia, et al. "Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway." Proceedings of the National Academy of Sciences of the United States of America vol. 118,43 (2021). doi: https://doi.org/10.1073/pnas.2115430118
Chen SJ, Kim L, Song HK, Varshavsky A. Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway. Proc Natl Acad Sci U S A. 2021 Oct 26;118(43). doi: 10.1073/pnas.2115430118. PMID: 34663735; PMCID: PMC8639330.
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Structures and reactivity of synthetic zinc(II) complexes resembling the active sites and reaction intermediates of aminopeptidases.

Chemical communications (Cambridge, England)

Rivas JC, Salvagni E, Parsons S.
PMID: 14765258
Chem Commun (Camb). 2004 Feb 21;(4):460-1. doi: 10.1039/b314089j. Epub 2004 Jan 22.

Herein we report the first crystallographic characterization and hydrolysis of a synthetic zinc(II) complex that resembles the active site and reaction intermediates proposed for aminopeptidases.

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Rivas JC, Salvagni E, Parsons S. Structures and reactivity of synthetic zinc(II) complexes resembling the active sites and reaction intermediates of aminopeptidases. Chem Commun (Camb). 2004;(4):460-1doi: 10.1039/b314089j.
Rivas, J. C., Salvagni, E., & Parsons, S. (2004). Structures and reactivity of synthetic zinc(II) complexes resembling the active sites and reaction intermediates of aminopeptidases. Chemical communications (Cambridge, England), (4), 460-1. https://doi.org/10.1039/b314089j
Rivas, Juan C Mareque, et al. "Structures and reactivity of synthetic zinc(II) complexes resembling the active sites and reaction intermediates of aminopeptidases." Chemical communications (Cambridge, England) vol. ,4 (2004): 460-1. doi: https://doi.org/10.1039/b314089j
Rivas JC, Salvagni E, Parsons S. Structures and reactivity of synthetic zinc(II) complexes resembling the active sites and reaction intermediates of aminopeptidases. Chem Commun (Camb). 2004 Feb 21;(4):460-1. doi: 10.1039/b314089j. Epub 2004 Jan 22. PMID: 14765258.
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The Role of Conformational Dynamics in Antigen Trimming by Intracellular Aminopeptidases.

Frontiers in immunology

Papakyriakou A, Stratikos E.
PMID: 28824657
Front Immunol. 2017 Aug 07;8:946. doi: 10.3389/fimmu.2017.00946. eCollection 2017.

Antigenic peptides presented by the major histocompatibility complex class I (MHC-I) molecules for recognition by cytotoxic T-lymphocytes are processed by members of the oxytocinase sub-family of M1 aminopeptidases ERAP1, ERAP2, and IRAP. These three homologous zinc metallopeptidases trim N-terminally...

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Papakyriakou A, Stratikos E. The Role of Conformational Dynamics in Antigen Trimming by Intracellular Aminopeptidases. Front Immunol. 2017;8:946doi: 10.3389/fimmu.2017.00946.
Papakyriakou, A., & Stratikos, E. (2017). The Role of Conformational Dynamics in Antigen Trimming by Intracellular Aminopeptidases. Frontiers in immunology, 8946. https://doi.org/10.3389/fimmu.2017.00946
Papakyriakou, Athanasios, and Stratikos, Efstratios. "The Role of Conformational Dynamics in Antigen Trimming by Intracellular Aminopeptidases." Frontiers in immunology vol. 8 (2017): 946. doi: https://doi.org/10.3389/fimmu.2017.00946
Papakyriakou A, Stratikos E. The Role of Conformational Dynamics in Antigen Trimming by Intracellular Aminopeptidases. Front Immunol. 2017 Aug 07;8:946. doi: 10.3389/fimmu.2017.00946. eCollection 2017. PMID: 28824657; PMCID: PMC5545687.
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Potential Activities of Freshwater Exo- and Endo-Acting Extracellular Peptidases in East Tennessee and the Pocono Mountains.

Frontiers in microbiology

Mullen L, Boerrigter K, Ferriero N, Rosalsky J, Barrett AVB, Murray PJ, Steen AD.
PMID: 29559961
Front Microbiol. 2018 Mar 06;9:368. doi: 10.3389/fmicb.2018.00368. eCollection 2018.

Proteins constitute a particularly bioavailable subset of organic carbon and nitrogen in aquatic environments but must be hydrolyzed by extracellular enzymes prior to being metabolized by microorganisms. Activities of extracellular peptidases (protein-degrading enzymes) have frequently been assayed in freshwater...

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Mullen L, Boerrigter K, et al. Potential Activities of Freshwater Exo- and Endo-Acting Extracellular Peptidases in East Tennessee and the Pocono Mountains. Front Microbiol. 2018;9:368doi: 10.3389/fmicb.2018.00368.
Mullen, L., Boerrigter, K., Ferriero, N., Rosalsky, J., Barrett, A. V. B., Murray, P. J., & Steen, A. D. (2018). Potential Activities of Freshwater Exo- and Endo-Acting Extracellular Peptidases in East Tennessee and the Pocono Mountains. Frontiers in microbiology, 9368. https://doi.org/10.3389/fmicb.2018.00368
Mullen, Lauren. "Potential Activities of Freshwater Exo- and Endo-Acting Extracellular Peptidases in East Tennessee and the Pocono Mountains." Frontiers in microbiology vol. 9 (2018): 368. doi: https://doi.org/10.3389/fmicb.2018.00368
Mullen L, Boerrigter K, Ferriero N, Rosalsky J, Barrett AVB, Murray PJ, Steen AD. Potential Activities of Freshwater Exo- and Endo-Acting Extracellular Peptidases in East Tennessee and the Pocono Mountains. Front Microbiol. 2018 Mar 06;9:368. doi: 10.3389/fmicb.2018.00368. eCollection 2018. PMID: 29559961; PMCID: PMC5845674.
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Role of aminopeptidases in the neuroendocrine control of blood pressure in experimental animals.

Endocrinologia y nutricion : organo de la Sociedad Espanola de Endocrinologia y Nutricion

Banegas I, Ramírez M, Alba F, Vives F, de Gasparo M, Belén Segarra A, Hermoso F, Durán R, Prieto I.
PMID: 22974453
Endocrinol Nutr. 2008 Oct;55(9):402-8. doi: 10.1016/S1575-0922(08)75077-0. Epub 2009 Jan 07.

Control of blood pressure is partially accomplished by several proteolytic enzymes included in the renin-angiotensin system. These enzymes produce several peptides that form the active components of the system. Study of these enzymes is essential for a deep understanding...

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Banegas I, Ramírez M, Alba F, et al. Role of aminopeptidases in the neuroendocrine control of blood pressure in experimental animals. Endocrinol Nutr. 2009;55(9):402-8doi: 10.1016/S1575-0922(08)75077-0.
Banegas, I., Ramírez, M., Alba, F., Vives, F., de Gasparo, M., Belén Segarra, A., Hermoso, F., Durán, R., & Prieto, I. (2008). Role of aminopeptidases in the neuroendocrine control of blood pressure in experimental animals. Endocrinologia y nutricion : organo de la Sociedad Espanola de Endocrinologia y Nutricion, 55(9), 402-8. https://doi.org/10.1016/S1575-0922(08)75077-0
Banegas, Inmaculada, et al. "Role of aminopeptidases in the neuroendocrine control of blood pressure in experimental animals." Endocrinologia y nutricion : organo de la Sociedad Espanola de Endocrinologia y Nutricion vol. 55,9 (2008): 402-8. doi: https://doi.org/10.1016/S1575-0922(08)75077-0
Banegas I, Ramírez M, Alba F, Vives F, de Gasparo M, Belén Segarra A, Hermoso F, Durán R, Prieto I. Role of aminopeptidases in the neuroendocrine control of blood pressure in experimental animals. Endocrinol Nutr. 2008 Oct;55(9):402-8. doi: 10.1016/S1575-0922(08)75077-0. Epub 2009 Jan 07. Spanish. PMID: 22974453.
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Focus on Brain Angiotensin III and Aminopeptidase A in the Control of Hypertension.

International journal of hypertension

Wright JW, Mizutani S, Harding JW.
PMID: 22792446
Int J Hypertens. 2012;2012:124758. doi: 10.1155/2012/124758. Epub 2012 Jun 26.

The classic renin-angiotensin system (RAS) was initially described as a hormone system designed to mediate cardiovascular and body water regulation. The discovery of a brain RAS composed of the necessary functional components (angiotensinogen, peptidases, angiotensins, and specific receptor proteins)...

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Wright JW, Mizutani S, Harding JW. Focus on Brain Angiotensin III and Aminopeptidase A in the Control of Hypertension. Int J Hypertens. 2012;2012:124758doi: 10.1155/2012/124758.
Wright, J. W., Mizutani, S., & Harding, J. W. (2012). Focus on Brain Angiotensin III and Aminopeptidase A in the Control of Hypertension. International journal of hypertension, 2012124758. https://doi.org/10.1155/2012/124758
Wright, John W, et al. "Focus on Brain Angiotensin III and Aminopeptidase A in the Control of Hypertension." International journal of hypertension vol. 2012 (2012): 124758. doi: https://doi.org/10.1155/2012/124758
Wright JW, Mizutani S, Harding JW. Focus on Brain Angiotensin III and Aminopeptidase A in the Control of Hypertension. Int J Hypertens. 2012;2012:124758. doi: 10.1155/2012/124758. Epub 2012 Jun 26. PMID: 22792446; PMCID: PMC3389720.
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Showing 25 to 36 of 100 entries