MEPRIINIT, Mitä ne ovat. kalvoon sitoutuneita astasiineja! / metalloproteinaasiryhmkää metsinkiinien suoerperheestä)

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2650038/
Tämä ihmisen TRIM37 jossa on  peptidihännäss MATH domeeni eli Mepriini ja TRAF-  homologidomeeni9 on peroxisomaalinen proteiini ja jos MATHdomeenissa on mutaatio, siitäseuraa että kokoTRUIM37  sijoittautuu muualle kuin peroxisomiin. 
Muita trimejä ei´n löytänyt joissa olisi tämä mepriini- tunnusmerkki.  olisko peroksisomit  tulleet  ihmiseen jostain sieltä ihan "korallien ajoista" ?
Täytyy katsoa mistäniitä tuli ihmiseen.

Tässä linkissä on hyviä kaavoja metsinkiineistä. 

ihmisen Meprin 1A alfa ja beta
https://www.ncbi.nlm.nih.gov/protein/Q16819 
https://www.ncbi.nlm.nih.gov/protein/XP_011524315.1 

 Biochem. J. (2013)450, 253–264 (Printed in Great Britain)doi:10.1042/BJ20121751253
 REVIEW ARTICLE The metalloproteases meprinα and meprinβ: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis 
Claudia BRODER and Christoph BECKER-PAULY

The  metalloproteases meprinα and meprinβ exhibit structural and functional features that are unique among all extracellular proteases. Although meprins were discovered more than 30 years ago, their precise substrates and physiological roles have been elusive. Both enzymes were originally found to be highly expressed in kidney and intestine, which focused research on these particular tissues and associated pathologies. Only recently it has become evident that meprins exhibit a much broader expression pattern, implicating functions in angiogenesis, cancer, inflammation, fibrosis and neurodegenerative diseases. Different animal models, as well as proteomics approaches for the identification of protease substrates, have helped to reveal more precise molecular signalling events mediated by meprin activity, such as activation and release of pro-inflammatory cytokines. APP (amyloid precursor protein) is cleaved by meprinβ in vivo, reminiscent of the β-secretase BACE1 (β-site APP-cleaving enzyme 1). The subsequent release of Aβ(amyloidβ)
peptides is thought to be the major cause of the neurodegenerative Alzheimer’s disease. On the other hand, ADAM10 (a disintegrin and metalloprotease domain 10), which is the constitutiveα-secretase, was shown to be activated by meprinβ, which is it self shed from the cell surface by ADAM10.
 In skin, both meprins are overexpressed in fibrotic tumours, characterized by massive accumulation of fibrillar collagens. Indeed, procollagen III is processed to its mature form by meprinα and meprinβ,an essential step in collagen fibril assembly. The recently solved crystal structure of meprinβ and the unique cleavage specificity of these proteases identified by proteomics will help to generate specific inhibitors that could be used as therapeutics to target meprins under certain pathological conditions .Key words: cancer, fibrosis, inflammation, meprin, metalloprotease, neurodegeneration, proteomics.

 Structure length function
Meprins are complex and highly glycosylated multi-domainenzymes that require post-translational modifications to reach fullactivity. They are expressed as proteolytically inactive zymogens that require the removal of their N-terminal propeptides by otherproteases. Several serine proteases have been identified as doingthis job [30–34], e.g. members of the tissue KLKs (kallikrein-related peptidases).Meprins belong to the astacin family of metalloproteases,comprising only six members in humans [35]. These enzymes are characterized by a conserved zinc-binding motif(HExxHxxGxxHxxxRxDR) and by a sequence in close proximity to the active-site cleft, the so called Met-turn, that includes a tyrosine residue as a fifth zinc ligand. Within the astacin family,meprins exhibit a unique domain composition. Human meprinα and β, encoded on chromosomes 6 and8 respectively, comprise an N-terminal signal peptide directing the polypeptide chain to the endoplasmic reticulum, an N-terminal propeptide, an astacin-like protease domain, a MAM(meprin A5 protein tyrosine phosphataseμ) domain and a TRAF(tumour-necrosis-factor-receptor-associated factor) domain, both of which are known to mediate protein–protein interactions, anEGF (epidermal growth factor)-like domain, a transmembranedomain, and a C-terminal cytosolic tail (Figure 1A)

 Mistä niit pre-peroxisomeja olisi tullut?
(Ehkä jokin niistä Cnidarioista hienolla injektiotekniikallaan on antanut "kykyjä"  monisoluisiin organismeihin, joisa kiertää veri ja on muutakin ravinnetta.  Siitä ajasta olisi peroxisomeihin jäänyt se  meoprin-MATH-pätkä TRIm37:ään kai.
 https://onlinelibrary.wiley.com/doi/full/10.1002/bies.201700050