Skip to content
Back to outputs

Leishmania mexicana: LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein

Research output: Contribution to journalArticlepeer-review

Standard

Leishmania mexicana : LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein. / Gómez-Arreaza, Amaranta; Acosta, Héctor; Barros-Álvarez, Ximena; Concepción, Juan L; Albericio, Fernando; Avilan, Luisana.

In: Experimental Parasitology, Vol. 127, No. 4, 04.2011, p. 752-61.

Research output: Contribution to journalArticlepeer-review

Harvard

Gómez-Arreaza, A, Acosta, H, Barros-Álvarez, X, Concepción, JL, Albericio, F & Avilan, L 2011, 'Leishmania mexicana: LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein', Experimental Parasitology, vol. 127, no. 4, pp. 752-61. https://doi.org/10.1016/j.exppara.2011.01.008

APA

Gómez-Arreaza, A., Acosta, H., Barros-Álvarez, X., Concepción, J. L., Albericio, F., & Avilan, L. (2011). Leishmania mexicana: LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein. Experimental Parasitology, 127(4), 752-61. https://doi.org/10.1016/j.exppara.2011.01.008

Vancouver

Gómez-Arreaza A, Acosta H, Barros-Álvarez X, Concepción JL, Albericio F, Avilan L. Leishmania mexicana: LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein. Experimental Parasitology. 2011 Apr;127(4):752-61. https://doi.org/10.1016/j.exppara.2011.01.008

Author

Gómez-Arreaza, Amaranta ; Acosta, Héctor ; Barros-Álvarez, Ximena ; Concepción, Juan L ; Albericio, Fernando ; Avilan, Luisana. / Leishmania mexicana : LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein. In: Experimental Parasitology. 2011 ; Vol. 127, No. 4. pp. 752-61.

Bibtex

@article{251266a6c0d449f6b87831422147ac26,
title = "Leishmania mexicana: LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein",
abstract = "Leishmania mexicana is able to interact with the fibrinolytic system through its component plasminogen, the zymogenic form of the protease plasmin. In this study a new plasminogen binding protein of this parasite was identified: LACK, the Leishmania homolog of receptors for activated C-kinase. Plasminogen binds recombinant LACK with a K(d) value of 1.6±0.4 μM, and binding is lysine-dependent since it is inhibited by the lysine analog ε-aminocaproic acid. Inhibition studies with specific peptides and plasminogen binding activity of a mutated recombinant LACK have highlighted the internal motif (260)VYDLESKAV(268), similar to those found in several enolases, as involved in plasminogen binding. Recombinant LACK and secreted proteins, in medium conditioned by parasites, enhance plasminogen activation to plasmin by the tissue plasminogen activator (t-PA). In addition to its localization in the cytosol, in the microsomal fraction and as secreted protein in conditioned medium, LACK was also localized on the external surface of the membrane. The results presented here suggest that LACK might bind and enhance plasminogen activation in vivo promoting the formation of plasmin. Plasminogen binding of LACK represents a new function for this protein and might contribute to the invasiveness of the parasite.",
keywords = "Amino Acid Sequence, Animals, Antigens, Protozoan/chemistry, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Fluorescent Antibody Technique, Humans, Immune Sera/immunology, Leishmania mexicana/chemistry, Molecular Structure, Mutagenesis, Site-Directed, Plasminogen/metabolism, Protozoan Proteins/chemistry, Rabbits, Recombinant Proteins/genetics, Sequence Alignment",
author = "Amaranta G{\'o}mez-Arreaza and H{\'e}ctor Acosta and Ximena Barros-{\'A}lvarez and Concepci{\'o}n, {Juan L} and Fernando Albericio and Luisana Avilan",
note = "Copyright {\textcopyright} 2011 Elsevier Inc. All rights reserved.",
year = "2011",
month = apr,
doi = "10.1016/j.exppara.2011.01.008",
language = "English",
volume = "127",
pages = "752--61",
journal = "Experimental Parasitology",
issn = "0014-4894",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Leishmania mexicana

T2 - LACK (Leishmania homolog of receptors for activated C-kinase) is a plasminogen binding protein

AU - Gómez-Arreaza, Amaranta

AU - Acosta, Héctor

AU - Barros-Álvarez, Ximena

AU - Concepción, Juan L

AU - Albericio, Fernando

AU - Avilan, Luisana

N1 - Copyright © 2011 Elsevier Inc. All rights reserved.

PY - 2011/4

Y1 - 2011/4

N2 - Leishmania mexicana is able to interact with the fibrinolytic system through its component plasminogen, the zymogenic form of the protease plasmin. In this study a new plasminogen binding protein of this parasite was identified: LACK, the Leishmania homolog of receptors for activated C-kinase. Plasminogen binds recombinant LACK with a K(d) value of 1.6±0.4 μM, and binding is lysine-dependent since it is inhibited by the lysine analog ε-aminocaproic acid. Inhibition studies with specific peptides and plasminogen binding activity of a mutated recombinant LACK have highlighted the internal motif (260)VYDLESKAV(268), similar to those found in several enolases, as involved in plasminogen binding. Recombinant LACK and secreted proteins, in medium conditioned by parasites, enhance plasminogen activation to plasmin by the tissue plasminogen activator (t-PA). In addition to its localization in the cytosol, in the microsomal fraction and as secreted protein in conditioned medium, LACK was also localized on the external surface of the membrane. The results presented here suggest that LACK might bind and enhance plasminogen activation in vivo promoting the formation of plasmin. Plasminogen binding of LACK represents a new function for this protein and might contribute to the invasiveness of the parasite.

AB - Leishmania mexicana is able to interact with the fibrinolytic system through its component plasminogen, the zymogenic form of the protease plasmin. In this study a new plasminogen binding protein of this parasite was identified: LACK, the Leishmania homolog of receptors for activated C-kinase. Plasminogen binds recombinant LACK with a K(d) value of 1.6±0.4 μM, and binding is lysine-dependent since it is inhibited by the lysine analog ε-aminocaproic acid. Inhibition studies with specific peptides and plasminogen binding activity of a mutated recombinant LACK have highlighted the internal motif (260)VYDLESKAV(268), similar to those found in several enolases, as involved in plasminogen binding. Recombinant LACK and secreted proteins, in medium conditioned by parasites, enhance plasminogen activation to plasmin by the tissue plasminogen activator (t-PA). In addition to its localization in the cytosol, in the microsomal fraction and as secreted protein in conditioned medium, LACK was also localized on the external surface of the membrane. The results presented here suggest that LACK might bind and enhance plasminogen activation in vivo promoting the formation of plasmin. Plasminogen binding of LACK represents a new function for this protein and might contribute to the invasiveness of the parasite.

KW - Amino Acid Sequence

KW - Animals

KW - Antigens, Protozoan/chemistry

KW - Blotting, Western

KW - Electrophoresis, Gel, Two-Dimensional

KW - Fluorescent Antibody Technique

KW - Humans

KW - Immune Sera/immunology

KW - Leishmania mexicana/chemistry

KW - Molecular Structure

KW - Mutagenesis, Site-Directed

KW - Plasminogen/metabolism

KW - Protozoan Proteins/chemistry

KW - Rabbits

KW - Recombinant Proteins/genetics

KW - Sequence Alignment

U2 - 10.1016/j.exppara.2011.01.008

DO - 10.1016/j.exppara.2011.01.008

M3 - Article

C2 - 21272581

VL - 127

SP - 752

EP - 761

JO - Experimental Parasitology

JF - Experimental Parasitology

SN - 0014-4894

IS - 4

ER -

ID: 24736040