Meprins are zinc metalloproteases of the
astacin family that are abundantly expressed in the brush border membranes (BBM) of kidney proximal tubules and small intestines [1,2].
A zinc proteinase member of the
astacin family was identified in P.
Bond, "Activation mechanism of meprins, members of the
astacin metalloendopeptidase family," The Journal of Biological Chemistry, vol.
[2.] Sterchi EE, Stocker W, Bond JS (2008) Meprins, membrane-bound and secreted
astacin metalloproteinase.
(1999) established that myosinases occurred in nonmuscle tissues, and they identified a new form (myosinase III) that had sequence homology to the
astacin group of zinc-dependent endopeptidases (Titani et al.
Identification and characterization of hydra metalloproteinase 2 (HMP2): a meprin-like
astacin metalloproteinase that functions in foot morphogenesis.
Interestingly, one of the VEB genes, SPAN, encodes a member of the
astacin protease family.
The matrix metalloproteinases or matrixins (MMPs) are members of the large metzincin superfamily such as the
astacins, serralysins, reprolysins, and adamalysins or disintegrin metalloproteinases (ADAMs).
Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'.