Fig. 2.
Fig. 2. Multimer pattern of vWF released in response to ATP. Confluent HUVECs were metabolically labeled with [35S]-cysteine and [35S]-methionine for 24 hours. vWF was immunoprecipitated from the labeling medium (medium) and from the supernatant of cells incubated for 30 minutes with ATP (100 μmol/L), ATP/IBMX (100 μmol/L), thrombin (1 U/mL), or KRBH-BSA 0.1% alone (control). vWF multimers were resolved on a horizontal nonreducing 2% SDS-agarose gel. Top arrowhead, the origin of the gel; bottom arrowhead, position of vWF dimers. vWF released constitutively into the labeling medium consists predominantly of dimers and small multimers, whereas vWF released in response to ATP and thrombin consists of high–molecular weight multimers.

Multimer pattern of vWF released in response to ATP. Confluent HUVECs were metabolically labeled with [35S]-cysteine and [35S]-methionine for 24 hours. vWF was immunoprecipitated from the labeling medium (medium) and from the supernatant of cells incubated for 30 minutes with ATP (100 μmol/L), ATP/IBMX (100 μmol/L), thrombin (1 U/mL), or KRBH-BSA 0.1% alone (control). vWF multimers were resolved on a horizontal nonreducing 2% SDS-agarose gel. Top arrowhead, the origin of the gel; bottom arrowhead, position of vWF dimers. vWF released constitutively into the labeling medium consists predominantly of dimers and small multimers, whereas vWF released in response to ATP and thrombin consists of high–molecular weight multimers.

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