zinc metalloproteases, which are abundantly expressed in the brush border membranes (BBM) of renal proximal tubules, have also emerged as susceptibility markers for DKD .
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" , 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