gelatinase

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gelatinase

[′jel·ə·tə‚nās]
(biochemistry)
An enzyme, found in some yeasts and molds, that liquefies gelatin.
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In situ zymography is commonly used as an index of net metalloproteinase activity resulting from the balance between gelatinases (principally MMP-9 and MMP-2) and the tissue inhibitors of MMPs (TIMPs) that are present in the tissue.
As matrix metalloproteases (MMPs) are known to mediate the conversion of memFasL into its inactive, soluble form (sFasL) [31, 32] and are coincidently regulated through EGFR/MAPK signaling, we next sought to analyze the two gelatinases MMP-2 and MMP-9 (Figures 2(b) and 2(c)).
Tetracyclines come under the family of antibiotics which inhibit the catalytic activity of human collagenases and gelatinases, especially MMPs.
Dynamic in vivo changes in the activities of gelatinases, matrix metalloproteinases (MMPs), and tissue inhibitor of metalloproteinases (TIMPs) in buffalo (Bubalus bubalis) uterine luminal fluid during estrous cycle and early pregnancy.
Second group comprises gelatinases: MMP-2 (gelatinase A) and MMP-9 (gelatinase B).
The intensity of the bands of individual gelatinases was plotted as a function of eluted volume ([v.sub.e]/[v.sub.o]) to determine their relative distribution between the LMMC species and the free state.
Gelatinases A and B (MMP-2 and MMP-9, resp.) digest the denatured collagens, gelatins, as well as some noncollagen matrix components of the joints.
Because gelatinases bind TIMPs to form a tightly bound 1: 1 molar stoichiometric complex [57], an increased expression of MMP-2 should be accompanied by enhanced production of TIMPs [50].
Gelatinases (MMP-2 and MMP-9) have a compact collagen binding domain called fibronectin-like domain within the catalytic domain.
Do matrix metalloproteinases MMP-2 and MMP-9 (gelatinases) play a role in renal development, physiology and glomerular diseases?
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].