Figure 4.
Figure 4. Differential expression on matriptase by THP-1 and U937 cells. (A) RNA was isolated from THP-1 and U937 cells, reverse transcribed, and subjected to qRT-PCR. Values are corrected for RNA content by comparison with 18S ribosomal RNA and shown as mean ± SD (n = 3). (B) Cell lysates (lys, 10 μg protein) and concentrated conditioned medium (CM, 10 μL) were isolated from THP-1 and U937 cells in the presence of protease inhibitor cocktail, subject to 10% SDS-PAGE, and probed with an antibody to matriptase (M32). The mobility of matriptase is consistent with the molecular weight of the form proteolytically processed at Gly149,25 but this does not lead to shedding of the protease as it is not detectable in the cell-conditioned medium.

Differential expression on matriptase by THP-1 and U937 cells. (A) RNA was isolated from THP-1 and U937 cells, reverse transcribed, and subjected to qRT-PCR. Values are corrected for RNA content by comparison with 18S ribosomal RNA and shown as mean ± SD (n = 3). (B) Cell lysates (lys, 10 μg protein) and concentrated conditioned medium (CM, 10 μL) were isolated from THP-1 and U937 cells in the presence of protease inhibitor cocktail, subject to 10% SDS-PAGE, and probed with an antibody to matriptase (M32). The mobility of matriptase is consistent with the molecular weight of the form proteolytically processed at Gly149,25  but this does not lead to shedding of the protease as it is not detectable in the cell-conditioned medium.

Close Modal

or Create an Account

Close Modal
Close Modal