Meprin zinc metalloproteases, which are abundantly expressed in the brush border membranes (BBM) of renal proximal tubules, have also emerged as susceptibility markers for DKD [10].
In the article titled "
Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes" [1], the
meprins in Figure 1(b) were mistakenly duplicated due to a production error.
Meyer et al., "Fetuin-A and cystatin C are endogenous inhibitors of human
meprin metalloproteases," Biochemistry, vol.
Walker et al., "The alpha and beta subunits of the metalloprotease
meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation," The Journal of Investigative Dermatology, vol.
B-type natriuretic peptide 8-32, which is produced from mature BNP 1-32 by the metalloprotease
meprin A, has reduced bioactivity.
The domain abbreviations used in the text are for laminin G or laminin G/neurexin/sex hormone binding globulin or LNS domains (L); epidermal growth factor repeat (EGF); coagulation factor 5/8 type C (F58C); fibrinogen-like (FBG); extracellular cadherin (EC); alpha/beta ([alpha]/[beta]); immunoglobulin (Ig); Toll/Il-1 receptor homology (TIR);
meprin, A-5 protein, receptor protein tyrosine phosphatase mu (MAM); fibronectin type 3 (FN), protein tyrosine phosphatase (PTP); leucine rich repeat (LRR), N-terminal leucine rich repeat (LRRNT); C-terminal leucine rich repeat (LRRCT); galactose binding lectin domain (LEC); olfactomedin-like domain (OLF); hormone binding domain (HBD); GPCR- autoproteolysis inducing (GAIN); thrombospondin (TSP).
Bellac et al., "The substrate degradome of
meprin metalloproteases reveals an unexpected proteolytic link between
meprin and ADAM10," Cellular and Molecular Life Sciences, vol.
Several other types of functional domains, including zinc finger (ZF), Kelch, BTB and C-terminal Kelch (BACK),
meprin and TRAF homology (MATH), ankyrin repeats (ANK), PHR, and Ras homology (Rho) domains, are also found in some BTB proteins.
The enzyme, coded for by the MEP1A gene, is a zinc-containing metalloprotease called
meprin, and is abundant in the intestine.
A role for
meprin [beta] in the progression of diabetic nephropathy (DN) and fibrosis-associated kidney disease has been demonstrated by several studies in both rodents and humans [14-16].
Another protease, peptidyl arginine aldehyde protease, can also degrade BNP, and
meprin was shown to lyse BNP in animal models but not in humans (26).
Studies with a yeast two-hybrid system showed that OS-9 interacts with the carboxyl-terminal tail of
meprin [beta] [15].
