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Soluble Metalloendopeptidases and Neuroendocrine Signaling

Baker Medical Research Institute (C.N.S., A.I.S., R.A.L.), Melbourne, Australia 8008; and Thrombosis Research Section (C.N.S.), Department of Medicine, Baylor College of Medicine, Houston, Texas 77030

Correspondence: Address all correspondence and requests for reprints to: Rebecca A. Lew and Ian Smith, Baker Medical Research Institute, PO Box 6492, St. Kilda Road Central, Melbourne, Australia 8008. E-mail: rebecca.lew{at}baker.edu.au and ian.smith{at}baker.edu.au

Peptidases play a vital and often highly specific role in the physiological and pathological generation and termination of peptide hormone signals. The thermolysin-like family of metalloendopeptidases involved in the extracellular processing of neuroendocrine and cardiovascular peptides are of particular significance, reflecting both their specificity for particular peptide substrates and their utility as therapeutic targets. Although the functions of the membrane-bound members of this family, such as angiotensin-converting enzyme and neutral endopeptidase, are well established, a role for the predominantly soluble family members in peptide metabolism is only just emerging. This review will focus on the biochemistry, cell biology, and physiology of the soluble metalloendopeptidases EC 3.4.24.15 (thimet oligopeptidase) and EC 3.4.24.16 (neurolysin), as well as presenting evidence that both peptidases play an important role in such diverse functions as reproduction, nociception, and cardiovascular homeostasis.

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