scholarly journals Microarray Analysis of Tomato’s Early and Late Wound Response Reveals New Regulatory Targets for Leucine Aminopeptidase A

PLoS ONE ◽  
2013 ◽  
Vol 8 (10) ◽  
pp. e77889 ◽  
Author(s):  
Melissa A. Scranton ◽  
Jonathan H. Fowler ◽  
Thomas Girke ◽  
Linda L. Walling
Keyword(s):  
Microarray Analysis ◽  
Leucine Aminopeptidase ◽  
Wound Response ◽  
Aminopeptidase A

scholarly journals The Induction of Tomato Leucine Aminopeptidase Genes (LapA) After Pseudomonas syringae pv. tomato Infection Is Primarily a Wound Response Triggered by Coronatine

2001 ◽  
Vol 14 (2) ◽  
pp. 214-224 ◽  
Author(s):  
Véronique Pautot ◽  
Frances M. Holzer ◽  
Josette Chaufaux ◽  
Linda L. Walling
Keyword(s):  
Pseudomonas Syringae ◽  
Floral Development ◽  
Leucine Aminopeptidase ◽  
Wound Response ◽  
Global Changes ◽  
Pr Genes ◽  
Tomato Plants ◽  
Pathogenesis Related Protein ◽  
Pathogenesis Related ◽  
Antisense Construct

Tomato plants constitutively express a neutral leucine aminopeptidase (LAP-N) and an acidic LAP (LAP-A) during floral development and in leaves in response to insect infestation, wounding, and Pseudomonas syringae pv. tomato infection. To assess the physiological roles of LAP-A, a LapA-antisense construct (35S:asLapA1) was introduced into tomato. The 35S:asLapA1 plants had greatly reduced or showed undetectable levels of LAP-A and LAP-N proteins in healthy and wounded leaves and during floral development. Despite the loss of these aminopeptidases, no global changes in protein profiles were noted. The 35S:asLapA1 plants also exhibited no significant alteration in floral development and did not impact the growth and development of Manduca sexta and P. syringae pv. tomato growth rates during compatible or incompatible infections. To investigate the mechanism underlying the strong induction of LapA upon P. syringae pv. tomato infection, LapA expression was monitored after infection with coronatine-producing and -deficient P. syringae pv. tomato strains. LapA RNA and activity were detected only with the coronatine-producing P. syringae pv. tomato strain. Coronatine treatment of excised shoots caused increases in RNAs for jasmonic acid (JA)-regulated wound-response genes (LapA and pin2) but did not influence expression of a JA-regulated pathogenesis-related protein gene (PR-1). These results indicated that coronatine mimicked the wound response but was insufficient to activate JA-regulated PR genes.

Up-regulation of leucine aminopeptidase-A in cadmium-treated tomato roots

Planta ◽  
2011 ◽  
Vol 234 (4) ◽  
pp. 857-863 ◽  
Author(s):  
Latifa Boulila-Zoghlami ◽  
Philippe Gallusci ◽  
Frances M. Holzer ◽  
Gilles J. Basset ◽  
Whabi Djebali ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Tomato Roots ◽  
Aminopeptidase A

scholarly journals Distribution of Adipocyte-derived Leucine Aminopeptidase (A-LAP)/ER-aminopeptidase (ERAP)-1 in Human Uterine Endometrium

2004 ◽  
Vol 52 (9) ◽  
pp. 1169-1175 ◽  
Author(s):  
Daijiro Shibata ◽  
Hisao Ando ◽  
Akira Iwase ◽  
Tetsuro Nagasaka ◽  
Akira Hattori ◽  
...  
Keyword(s):  
Leucine Aminopeptidase ◽  
Uterine Endometrium ◽  
Aminopeptidase A ◽  
Human Uterine Endometrium

Characterization of a leucine aminopeptidase of Babesia gibsoni

Parasitology ◽  
2009 ◽  
Vol 136 (9) ◽  
pp. 945-952 ◽  
Author(s):  
H. JIA ◽  
M. A. TERKAWI ◽  
G. O. ABOGE ◽  
Y.-K. GOO ◽  
Y. LUO ◽  
...  
Keyword(s):  
Amino Acid ◽  
Free Amino Acid ◽  
Free Amino ◽  
Drug Targets ◽  
Leucine Aminopeptidase ◽  
Divalent Cations ◽  
Specific Inhibitor ◽  
Babesia Gibsoni ◽  
Aminopeptidase A

SUMMARYPeptidases of parasitic protozoa are currently under intense investigation in order to identify novel virulence factors, drug targets, and vaccine candidates, except in Babesia. Leucine aminopeptidases in protozoa, such as Plasmodium and Leishmania, have been identified to be involved in free amino acid regulation. We report here the molecular and enzymatic characterization, as well as the localization of a leucine aminopeptidase, a member of the M17 cytosolic aminopeptidase family, from B. gibsoni (BgLAP). A functional recombinant BgLAP (rBgLAP) expressed in Escherichia coli efficiently hydrolysed synthetic substrates for aminopeptidase, a leucine substrate. Enzyme activity of the rBgLAP was found to be optimum at pH 8·0 and at 37°C. The substrate profile was slightly different from its homologue in P. falciprum. The activity was also strongly dependent on metal divalent cations, and was inhibited by bestatin, which is a specific inhibitor for metalloprotease. These results indicated that BgLAP played an important role in free amino acid regulation.

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