Summary
The heart rate accelerating peptide neurohormone D is rapidly inactivated by intact Malpighian tubules of cockroaches and also by homogenates of them. The peptide is removed from a solution by an active uptake mechanism. Within the tubule cells one or a set of soluble proteinases with a molecular mass around 45000 Da hydrolyze the neuropeptide. The inhibition of the reaction by synthetic protease inhibitors and chelating agents characterizes the enzyme(s) as metalloendopeptidase with serine or cysteine at the active site. This seems to be the first evidence that a peptidase comparable to the neutral metalloendopeptidase of mammalian kidney microvilli exists in insect Malpighian tubules and could play an important role in the hydrolysis of neuropeptides.
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Abbreviations
- EDTA :
-
ethylenediamine tetraacetic acid
- AEBSF :
-
4-β-aminoethylbenzenesulfonylfluoride
- PMSF :
-
pnenylmethanesulfonyl fluoride
- TLCK :
-
tosyl-lysine chloromethyl ketone
- TPCK :
-
tosyl-phenylalanyl chloromethyl ketone
- CMB :
-
chloromercuribenzoic acid
- DNP-Ala :
-
N-dinitrophenyl-alanine
- TFA :
-
trifluoroacetic acid
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Baumann, E., Penzlin, H. Inactivation of neurohormone D by Malpighian tubules in an insect,Periplaneta americana . J Comp Physiol B 157, 511–517 (1987). https://doi.org/10.1007/BF00691836
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DOI: https://doi.org/10.1007/BF00691836