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Polyamines and enzymes of polyamines metabolism in the cartilage during embryonic development.

1. In chicken embryo cartilage putrescine levels, maximal at day 8, fall by day 16 to a four-fold lower value, which remains unchanged through hatching and in the 12-day-old chick. 2. Spermine and spermidine, initially higher than putrescine, are almost halved between days 8 and 11, and remain constant afterwards. 3. Ornithine decarboxylase is down to 20% of the day 8 value by day 16, and is further reduced in the newly hatched chick. 4. S-Adenosyl-methionine decarboxylase activity shows a 50% reduction between days 8 and 11, and no further changes. 5. Spermidine acetyltransferase activity at day 11 is 30% lower than at day 8, goes back up to the initial level by day 16, and progressively decreases through hatching and the first 12 days of life.

Acetyltransferases↗

Polyamine FTX-3.3 and polyamine amide sFTX-3.3 inhibit presynaptic calcium currents and acetylcholine release at mouse motor nerve terminals.

FTX-3.3 is the proposed structure of a calcium-channel blocking toxin that has been isolated from the funnel web spider (Agelenopsis aperta). The effects of FTX-3.3 and one of its analogues, sFTX-3.3, on acetylcholine release, on presynaptic currents at mouse motor nerve terminals and on whole-cell sodium currents in SK.N.SH cells (a human neuroblastoma cell line) have been studied. FTX-3.3 (10-30 microM) and sFTX-3.3 (100-300 microM) reversibly reduced release of acetylcholine by approximately 70-90% and 40-60%, respectively. FTX-3.3 (10 microM) blocked the fast component of presynaptic calcium currents by approximately 60%. sFTX-3.3 (100 microM) reduced the duration of the slow component of presynaptic calcium currents by about 50% of the control and also reduced presynaptic sodium current by approximately 20% of the control. sFTX-3.3 (100 microM) reduced whole-cell sodium current recorded from SK.N.SH cells by approximately 15%, whereas FTX-3.3, even at 200 microM, did not affect this current. Since the only difference in chemical structures of these toxins is that sFTX-3.3 has an amide function which is absent in FTX-3.3, the amide function may be responsible for the reduced potency and selectivity of sFTX-3.3. This study also provides further support for the existence of P-type calcium channels at mouse motor nerve terminals.

Acetylcholine↗