Key result
Cathepsins B and H extracted from human kidneys activate human inactive renin and progressively decrease its molecular weight.
Human kidney cathepsins B and H activate inactive renin and reduce its molecular weight, suggesting a role in the physiological processing of renin.
May inform renin processing mechanisms; leaves open in vivo role and clinical relevance in hypertension.
Cathepsins B, H, and D, extracted from human kidneys, activate human inactive renin. Inactive renin, obtained from human kidneys, contains two components of Mr 53,000 and 50,000. Upon incubation with 0.5 microM cathepsin B, the Mr of the larger component decreased progressively to 45,000 (similar to the Mr of active renin) without appreciable loss of renin activity. Cathepsin H also activated and decreased the Mr of kidney inactive renin. Plasma inactive renin was activated by the thiol proteases, cathepsins B and H, with less reduction in Mr than that observed in kidney renin.
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Luetscher et al. (1982) studied this question. Cathepsins B and H was evaluated on Activation and molecular weight reduction of human inactive renin. Cathepsins B and H extracted from human kidneys activate human inactive renin and progressively decrease its molecular weight.
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