![Fig. 4. A high concentration of collagen induces PLCγ2-independent aggregation. / PLCγ2-deficient (PLCγ2−/−) and wild-type (WT) platelets were stimulated with a high level (50 μg/mL) of collagen. PLCγ2-deficient platelets aggregated in response to a high level of collagen, but the extent of aggregation was diminished in comparison to wild-type platelets (A). Aggregation of PLCγ2-deficient platelets preincubated with inhibitors (apyrase [10 U/mL], A3P5P [2 mM], AR-C69931MX [2 μM], and indomethacin [25μM]) and stimulated with 50 μg/mL collagen was inhibited by 10μg/mL hamster antimouse αIIbβ3 monoclonal antibody 1B5, but not by 10μg/mL hamster control IgG (B). PLCγ2-deficient platelets with and without inhibitors (apyrase [10 U/mL], A3P5P [2 mM], AR-C69931MX [2 μM], and indomethacin [25μM]) aggregated in response to a high level of collagen; the extents of aggregation were similar (C). PLCγ2-deficient platelets in the absence of inhibitors and wild-type platelets plus inhibitors (apyrase [10 U/mL], A3P5P [2 mM], AR-C69931MX [2 μM], and indomethacin [25μM]) aggregated to similar extents in response to a high level of collagen (D). Wild-type platelets treated with 4 inhibitors and PLCγ2-deficient platelets with and without inhibitors did not secrete TxA2 (E) even in response to a high concentration of collagen. Data were obtained from 6 tests. Bars represent means ± SEM.](https://ash.silverchair-cdn.com/ash/content_public/journal/blood/101/7/10.1182_blood-2002-05-1363/3/h80734073004.jpeg?Expires=1735849781&Signature=rP6qfPHHM4ssADA-prsMq1OzVa5jUxLEUbYJlwm-FUhPxH8nY46kZMcQfFcyY8ZOfo4zPvIzwlBf45BSLhEX4kIxtutc2eBpJEznn16wIBuX0IpqiylWpGUHLcGxHR1m6HVr45UsJpQIb92hClmj2KsXRYzDefqevU7JXNzSmoN-G4rgfXLHTz~Dw3oG3gyNAktrMdTgrHqUk0bLGNynsd~zMIt38fkYypUfUdt5tLSZ2aXjFWxaSu9oROXVEF3OndBwNDJm2fzcBbxb7fp4VgvQaHuBuX7TDXDoMo6nG3QihkYO~jfoI36sHmqwsc069IvmackhaCbb5OS596o10Q__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA)
A high concentration of collagen induces PLCγ2-independent aggregation.
PLCγ2-deficient (PLCγ2−/−) and wild-type (WT) platelets were stimulated with a high level (50 μg/mL) of collagen. PLCγ2-deficient platelets aggregated in response to a high level of collagen, but the extent of aggregation was diminished in comparison to wild-type platelets (A). Aggregation of PLCγ2-deficient platelets preincubated with inhibitors (apyrase [10 U/mL], A3P5P [2 mM], AR-C69931MX [2 μM], and indomethacin [25μM]) and stimulated with 50 μg/mL collagen was inhibited by 10μg/mL hamster antimouse αIIbβ3 monoclonal antibody 1B5, but not by 10μg/mL hamster control IgG (B). PLCγ2-deficient platelets with and without inhibitors (apyrase [10 U/mL], A3P5P [2 mM], AR-C69931MX [2 μM], and indomethacin [25μM]) aggregated in response to a high level of collagen; the extents of aggregation were similar (C). PLCγ2-deficient platelets in the absence of inhibitors and wild-type platelets plus inhibitors (apyrase [10 U/mL], A3P5P [2 mM], AR-C69931MX [2 μM], and indomethacin [25μM]) aggregated to similar extents in response to a high level of collagen (D). Wild-type platelets treated with 4 inhibitors and PLCγ2-deficient platelets with and without inhibitors did not secrete TxA2 (E) even in response to a high concentration of collagen. Data were obtained from 6 tests. Bars represent means ± SEM.
