MMP25

MMP25

A gene on chromosome 16p13.3 that encodes membrane type matrix metalloproteinase 25. Unlike other matrix metalloproteinases, which are secreted as inactive proproteins and activated when cleaved by extracellular proteinases, MMP25 is a transmembrane protein, which may activate progelatinase A; it is expressed predominantly in the leukocytes, lung and spleen.
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Due to structural and substrate specificity, MMPs are currently divided into seven classes: collagenases (MMP1, MMP8, MMP13, and MMP18), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP10), stromelysin like (MMP11 and MMP12), matrilysins (MMP7 and MMP26), membrane type (MMP14, MMP15, MMP16, MMP17, MMP24, and MMP25), and others (MMP19, MMP20, MMP21, MMP22, MMP23, MMP27, and MMP28) [18, 27, 28].
Blanton y colaboradores (44) evidenciaron una asociacion entre los individuos con labio y paladar fisurado no sindromico y translocaciones en los genes de cromosomas ubicados en 10p13, 16p13,3 (MMP25).
Primers and probes were designed and validated by Applied Biosystems for 18SRNA (4308329), MMP1 (Hs00899658_m1), MMP2 (Hs00234422_m1), MMP3 (Hs00968308_m1), MMP8 (Hs01029057_m1), MMP9 (Hs00234579_m1), MMP13 (Hs00233992_m1), MMP14 (Hs00237119_m1), MMP16 (Hs00254755_m1) MMP24 (Hs00198580_m1), MMP25 (Hs01554789_m1), TIMP1 (Hs99999139_m1), and TIMP3 (Hs00165949_m1).
In general, levels of MMP25 were high for SG (19/22), except in 2/22 samples with low expression and 1/22 where no expression was detected; in GC, expression of this gene was moderate in 11/17 samples and high in only 6/17.
In addition, no correlations were detected between gene expression of MMP1, MMP2, MMP3, MMP8, MMP9, MMP13, MMP14, MMP16, MMP24, MMP25, TIMP1 and TIMP3 and the variables of age, gender, size and degree of differentiation (P > 0.05).
This study showed the existence of differences in the expression of MMP2, MMP24, and MMP25 between GC and SG, with expression significantly higher in GC compared to SG.
In addition, there is no correlation or association between the expression of the genes (MMP1, MMP2, MMP3, MMP8, MMP9, MMP13, MMP14, MMP16, MMP24, MMP25, TIMP1, and TIMP3) and proteins (MMP-2 zymogen, MMP-2 active form, the catalytic domain of MMP-2 [33], MMP-3, MMP9/lipocalin, MMP-9 zymogen, MMP-9 active form, TIMP1/MMP-1, TIMP-1 monomer, TIMP-3 dimer, and TIMP-3 monomer) and the variables of age, gender, size, and degree of differentiation.
In conclusion, this study represents the first partial pattern of gene expression of MMPs and TIMPs in GC and SG conducted in Mexican population and shows that the mRNA levels of MMP2 are significantly higher in advanced GC compared to SG; interestingly, levels of MMP24 and MMP25 are also elevated in GC compared to SG.
Sohail et al., "MMP25 (MT6-MMP) is highly expressed in human colon cancer, promotes tumor growth, and exhibits unique biochemical properties," Journal of Biological Chemistry, vol.
Membrane-anchored MMPs include MT1-MMP (MMP14), MT2-MMP (MMP15), MT3-MMP (MMP16), MT4-MMP (MMP17), MT5-MMP (MMP24), MT6-MMP (MMP25), and MMP23.