Asset Details
Do you wish to reserve the book?
Secreted cystatins decrease proliferation and enhance apoptosis of human leukemic cells
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Secreted cystatins decrease proliferation and enhance apoptosis of human leukemic cells
Do you wish to request the book?
Secreted cystatins decrease proliferation and enhance apoptosis of human leukemic cells
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Secreted cystatins decrease proliferation and enhance apoptosis of human leukemic cells
2020
Overview
The secreted cysteine protease inhibitors, cystatin C and cystatin D, were added externally to leukemic U937, Jurkat, and HL‐60 cell cultures. The cystatins were internalized into endo‐lysosomal vesicles resulting in augmented hydrogen peroxide‐induced apoptosis, as well as decreased proliferation, both in apoptotic and nonapoptotic cells. Cysteine proteases are implicated in proteolysis events favoring cancer cell growth, spread, and death by apoptosis. Herein, we have studied whether the net growth and survival of the leukemic cell lines Jurkat, U937, and HL‐60 are affected by external addition of five proteins acting as natural cysteine protease inhibitors. None of the cystatins examined (A, C, D, and E/M) or chagasin showed consistent effects on Fas‐induced apoptosis when evaluated at 1 µm. In contrast, when the intrinsic apoptosis pathway was activated by hydrogen peroxide, addition of cystatin D augmented caspase‐3‐like activity within all three cell lines. Flow cytometric analysis of U937 cells also showed increased numbers of annexin V‐positive cells when hydrogen peroxide was used to initiate apoptosis and cells were cultured in the presence of cystatin D or C. Moreover, stimulation of hydrogen peroxide‐induced apoptotic U937 cells with either cystatin C or D resulted in a dose‐dependent decrease in the number of cells. Cell viability was also decreased when U937 cells were cultured in the presence of cystatin C or D (1–9 µm) only, demonstrating that these cystatins can reduce cell proliferation by themselves in addition to enhancing apoptosis induced by oxidative stress. These effects on U937 cells were paralleled by internalization of cystatins C and D, indicating these effects are caused by downregulation of intracellular proteolysis. External addition of cystatins C and D to HL‐60 and Jurkat cells demonstrated similar degrees of cystatin D uptake and decreased viability as for U937 cells, indicating that these effects are general for leukemic cells.
