scholarly journals Study of Oostatic Peptide Uptake and Metabolism in Developing Ovaries of the Flesh Fly,Neobellieria bullata

2010 ◽  
Vol 10 (48) ◽  
pp. 1-10 ◽  
Author(s):  
Blanka Bennettová ◽  
Jiřina Slaninová ◽  
Věra Vlasáková ◽  
Jan Hlaváček ◽  
Josef Holík ◽  
...  
Keyword(s):  
Flesh Fly ◽  
Peptide Uptake ◽  
Uptake And Metabolism ◽  
Neobellieria Bullata

Peptides with antimicrobial activity isolated from larvae of the flesh fly Neobellieria bullata

2009 ◽  
Author(s):  
Tereza Neubauerová ◽  
Martina Macková ◽  
Tomáš Macek ◽  
Miloslav Šanda ◽  
Zdeněk Voburka
Keyword(s):  
Antimicrobial Activity ◽  
Flesh Fly ◽  
Neobellieria Bullata

20-Hydroxyecdysone and juvenile hormone regulate the laminarin-induced nodulation reaction in larvae of the flesh fly, Neobellieria bullata

2006 ◽  
Vol 30 (9) ◽  
pp. 735-740 ◽  
Author(s):  
Vanessa Franssens ◽  
Guy Smagghe ◽  
Gert Simonet ◽  
Ilse Claeys ◽  
Bert Breugelmans ◽  
...  
Keyword(s):  
Juvenile Hormone ◽  
Flesh Fly ◽  
Neobellieria Bullata

Larvae of flesh fly Neobellieria bullata as a source for novel antimicrobial peptides

2011 ◽  
Author(s):  
Tereza Neubauerová ◽  
Martina Macková ◽  
Tomáš Macek ◽  
Miloslav Šanda ◽  
Zdeněk Voburka
Keyword(s):  
Antimicrobial Peptides ◽  
Flesh Fly ◽  
Neobellieria Bullata

Preparation of tritiated oostatic peptides for study of radioactivity incorporation in flesh fly Neobellieria bullata

Amino Acids ◽  
2006 ◽  
Vol 33 (3) ◽  
pp. 489-497 ◽  
Author(s):  
J. Hlaváček ◽  
B. Černý ◽  
B. Bennettová ◽  
J. Holík ◽  
R. Tykva
Keyword(s):  
Flesh Fly ◽  
Neobellieria Bullata

Distribution and degradation of oostatic peptides in the flesh fly Neobellieria bullata

2007 ◽  
Author(s):  
Jan Hlaváček ◽  
Blanka Bennettová ◽  
Jiřina Slaninová ◽  
Bohuslav Černý ◽  
Věra Vlasáková ◽  
...  
Keyword(s):  
Flesh Fly ◽  
Neobellieria Bullata

Effects of lysine infusion on the renal metabolism of aprotinin (Trasylol) in man

1992 ◽  
Vol 83 (3) ◽  
pp. 295-299 ◽  
Author(s):  
R. Rustom ◽  
P. Maltby ◽  
J. S. Grime ◽  
H. R. Stockdale ◽  
M. Critchley ◽  
...  
Keyword(s):  
Renal Function ◽  
Urinary Excretion ◽  
Proteolytic Enzymes ◽  
Renal Metabolism ◽  
Biphasic Effect ◽  
The Mean ◽  
Renal Tubular ◽  
Peptide Uptake ◽  
Uptake And Metabolism ◽  
Low Dosage

1. Aprotinin (Trasylol) is a cationic 6500 Da polypeptide that inhibits proteolytic enzymes, and when labelled with 99mTc it is a reproducible marker for the renal tubular turnover of small filtered proteins in man. Lysine potently inhibits tubular peptide uptake, and may thus depress the uptake and metabolism of aprotinin. This was investigated in 14 glomerulonephritic patients with normal renal function and variable proteinuria and in one healthy subject. 2. 99mTc-labelled aprotinin was given intravenously alone, and again 3 days later, immediately after the intravenous administration of 3–6 g of lysine, followed by an infusion over 1 h of 0.3–1.9 g of lysine/kg in individual patients. Activity over kidneys and in urine was measured over 24 h and chromatography was used to separate the undegraded peptide from free isotope. 3. At the low dosage of lysine (< 0.8 g/kg) given to six patients, kidney activity (representing tubular uptake) was unchanged, but early urine samples contained some undegraded aprotinin. Urinary excretion of free isotope, representing tubular metabolism, fell from 1.6 ± 0.2% of dose/h with no lysine to 0.9 ± 0.1% of dose/h in the 24 h after lysine, suggesting suppression of tubular aprotinin degradation. Corrected fractional degradation was calculated from the mean urinary excretion of free isotope over a given interval, determined by chromatography, divided by the mean cumulative kidney counts over this same interval, and this also fell after lysine from 0.06 ± 0.006 to 0.03 ± 0.006 h−1 (P<0.005) between 3.75 and 24 h. 4. By contrast, in nine subjects given more lysine (> 0.8 g/kg) tubular uptake fell and urine contained more undegraded aprotinin at all times. However, the corrected urinary excretion of free isotope (determined by chromatography) was unchanged and, paradoxically, fractional degradation rose from 0.06 + 0.01 to 0.10 ± 0.01% of dose/h (P<0.025) between 3.75 and 24 h. 5. Thus, lysine seemed to have a biphasic effect, inhibiting tubular peptide degradation at the low dosage, but depressing uptake into the tubular cell at the high dosage. This, in turn, might relieve intra cellular proteolytic enzymes from autoinhibition by aprotinin and result in a paradoxical restoration of tubular metabolism.

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