Identification of artifactual cathepsin D activity in cardiac subcellular fractions related to formation of an iron-EDTA complex

1985 ◽  
Vol 17 (10) ◽  
pp. 997-1003 ◽  
Author(s):  
D NANDI ◽  
M LESCH ◽  
A SAMAREL
1972 ◽  
Vol 127 (4) ◽  
pp. 705-713 ◽  
Author(s):  
Janet N. Ryan ◽  
J. Frederick Woessner

1. The earlier observation (Woessner, 1969) of oestradiol inhibition of collagen breakdown is confirmed and extended. Administration of 100μg of oestradiol-17β/day to parturient rats strongly inhibits the loss of collagen from the involuting uterus. Three experiments show that this effect is due to an inhibition of collagen degradation rather than to a stimulation of collagen synthesis. 2. Uterine collagen was labelled with hydroxy[14C]-proline by the administration of [14C]proline near the end of pregnancy. By 3 days post partum, control uteri lost 83% of their collagen and 90% of their hydroxy[14C]proline. Uteri from oestradiol-treated rats lost only 50% of both total and labelled hydroxyproline, with no decrease in the specific radioactivity of the hydroxyproline. 3. Incorporation of [14C]proline into uterine collagen hydroxyproline in vivo was not affected by oestradiol treatment. 4. Urinary excretion of hydroxyproline was increased in post-partum control rats and decreased in oestradiol-treated rats. 5. An enzyme capable of cleaving 4-phenylazobenzyloxycarbonyl-l-prolyl-l-leucylglycyl- l-prolyl-d-arginine (a substrate for clostridial collagenase) increased in activity in the post-partum uterus and was unaffected by oestradiol treatment. 6. Uterine homogenates digested uterine collagen extensively at pH3.2. This digestion was unaffected by the oestradiol treatment. 7. Lysosomal fractions prepared by density-gradient centrifugation of uterine homogenates contained coincident peaks of cathepsin D activity and peptide-bound hydroxyproline. The cathepsin D and hydroxyproline contents of this peak were unaffected by oestradiol treatment.


2001 ◽  
Vol 1 (S3) ◽  
pp. 139-139
Author(s):  
Nektarios Tavernarakis ◽  
Keli Xu ◽  
Monica Driscoll

1984 ◽  
Vol 64 (2) ◽  
Author(s):  
Marian Orlowski ◽  
Robert Orlowski ◽  
JuiC. Chang ◽  
Elizabeth Wilk ◽  
Marvin Lesser

1994 ◽  
Vol 1 (2) ◽  
pp. 173-177 ◽  
Author(s):  
Dalibor I. Hradek ◽  
Bruce Kessel ◽  
Nader Husseinzadeh ◽  
Bruce C. Moulton

1981 ◽  
Vol 26 (1) ◽  
pp. 168-173 ◽  
Author(s):  
Rakesh Dixit ◽  
Rausan Husain ◽  
Hasan Mukhtar ◽  
Prahlad K. Seth

1983 ◽  
Vol 244 (5) ◽  
pp. E442-E446 ◽  
Author(s):  
B. C. Moulton ◽  
B. B. Koenig

Early in blastocyst implantation, cells of the uterine luminal epithelium deteriorate and die in response to the presence of the blastocyst. Destruction of the epithelial cells appears to depend on control of the autophagic activity and enzyme content of lysosomes in these cells. Concentrations of the lysosomal proteinase, cathepsin D, have been identified in luminal epithelial cells, and these studies examined changes in epithelial cathepsin D activity and their hormonal control during early pseudopregnancy in the rat. Cathepsin D activity in luminal epithelial cells increases during early pseudopregnancy to maximal levels at the time of sensitivity to deciduogenic stimuli. Rates of cathepsin D synthesis in luminal epithelial cells also increase during early pseudopregnancy, but neither enzyme activity nor rates of synthesis increase in stromal-myometrial tissues. In ovariectomized rats, progestins rather than estradiol increase cathepsin D activity and rates of synthesis in luminal epithelial cells. These studies suggest that cell death in the luminal epithelium during blastocyst implantation may depend in part on the accumulation of lysosomal cathepsin D in these cells in response to progesterone secretion during early pregnancy.


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