TY - JOUR

T1 - Regulation of urokinase receptors in monocytelike U937 cells by phorbol ester phorbol myristate acetate

AU - Picone, R

AU - Kajtaniak, E L

AU - Nielsen, L S

AU - Behrendt, N

AU - Mastronicola, M.R.

AU - Cubellis, M.V.

AU - Stoppelli, M P

AU - Pedersen, S

AU - Danø, K

AU - Blasi, F.

PY - 1989/2

Y1 - 1989/2

N2 - A specific surface receptor for urokinase plasminogen activator (uPA) recognizes the amino-terminal growth factor-like sequence of uPA, a region independent from and not required for the catalytic activity of this enzyme. The properties of the uPA receptor (uPAR) and the localization and distribution of uPA in tumor cells and tissues suggest that the uPA/uPAR interaction may be important in regulating extracellular proteolysis-dependent processes (e.g., invasion, tissue destruction). Phorbol myristate acetate (PMA), an inducer of U937 cell differentiation to macrophage-like cells, elicits a time- and concentration-dependent increase in the number of uPAR molecules as shown by binding, cross-linking, and immunoprecipitation studies. The effect of PMA is blocked by cycloheximide. Overall, the data indicate that PMA increases the synthesis of uPA. PMA treatment also causes a decrease in the affinity of the uPAR for uPA, thus uncovering another way of regulating the interaction between uPA and uPAR. In addition, the PMA treatment causes a modification of migration of the cross-linked receptor in mono- and bidimensional gel electrophoresis.

AB - A specific surface receptor for urokinase plasminogen activator (uPA) recognizes the amino-terminal growth factor-like sequence of uPA, a region independent from and not required for the catalytic activity of this enzyme. The properties of the uPA receptor (uPAR) and the localization and distribution of uPA in tumor cells and tissues suggest that the uPA/uPAR interaction may be important in regulating extracellular proteolysis-dependent processes (e.g., invasion, tissue destruction). Phorbol myristate acetate (PMA), an inducer of U937 cell differentiation to macrophage-like cells, elicits a time- and concentration-dependent increase in the number of uPAR molecules as shown by binding, cross-linking, and immunoprecipitation studies. The effect of PMA is blocked by cycloheximide. Overall, the data indicate that PMA increases the synthesis of uPA. PMA treatment also causes a decrease in the affinity of the uPAR for uPA, thus uncovering another way of regulating the interaction between uPA and uPAR. In addition, the PMA treatment causes a modification of migration of the cross-linked receptor in mono- and bidimensional gel electrophoresis.

KW - Cell Count

KW - Cell Line

KW - Cross-Linking Reagents

KW - Electrophoresis, Polyacrylamide Gel

KW - Enzyme Precursors

KW - Humans

KW - Immunosorbent Techniques

KW - Molecular Weight

KW - Monocytes

KW - Peptide Fragments

KW - Plasminogen Activators

KW - Receptors, Cell Surface

KW - Receptors, Urokinase Plasminogen Activator

KW - Tetradecanoylphorbol Acetate

KW - Urokinase-Type Plasminogen Activator

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - Journal article

C2 - 2537321

VL - 108

SP - 693

EP - 702

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 2

ER -