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A decreasing function describes a relationship where the output consistently declines as the input increases. This means that for any two input values, if one is greater than the other, the corresponding output is smaller. Mathematically, a function f is decreasing on an interval I if for every x1 < x2​ in I, f (x1) > f (x2). This type of behavior is visually identified on a graph that slopes downward from left to right.The nature of a function can be analyzed by calculating...
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ortho&ndash;para-Directing Activators: &ndash;CH3, &ndash;OH, &ndash;&NoBreak;NH2, &ndash;OCH301:11

ortho–para-Directing Activators: –CH3, –OH, –⁠NH2, –OCH3

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All ortho–para directors, excluding halogens, are activating groups. These groups donate electrons to the ring, making the ring carbons electron-rich. Consequently, the reactivity of the aromatic ring towards electrophilic substitution increases. For instance, the nitration of anisole is about 10,000 times faster than the nitration of benzene. The electron-donating effect of the methoxy group in anisole activates the ortho and para positions on the ring and stabilizes the corresponding...
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Bradycardia is a medical condition in which the heart rate is slower than normal. It occurs when the heart's natural pacemaker, the sinus node, generates slower electrical impulses than the standard rhythm. In adults, bradycardia is diagnosed when the pulse rate falls below 60 beats per minute, indicating a deviation from the normal heart rate range.
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Propeptide glycosylation and galectin-3 binding decrease proteolytic activation of human proMMP-9/progelatinase B.

Lise Boon1, Estefania Ugarte-Berzal1, Erik Martens1

  • 1Laboratory of Immunobiology, Rega Institute for Medical Research, KU Leuven, Belgium.

The FEBS Journal
|November 14, 2018
PubMed
Summary
This summary is machine-generated.

Glycosylation of matrix metalloproteinase-9 (MMP-9) propeptide enhances its resistance to proteolysis and modulates activation. This post-translational modification fine-tunes MMP-9 activity in both normal physiology and disease states.

Keywords:
N-linked glycosylationgalectin-3matrix metalloproteinase-9propeptideproteolytic activation

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Area of Science:

  • Biochemistry
  • Enzymology
  • Glycobiology

Background:

  • Matrix metalloproteinases (MMPs) are crucial enzymes involved in extracellular matrix remodeling.
  • MMP-9 propeptide undergoes unique N-linked glycosylation, influencing its activation.
  • ProMMP-9 activation is a stepwise process involving cleavage by other proteases.

Purpose of the Study:

  • To investigate the role of MMP-9 propeptide glycosylation in its proteolytic activation.
  • To identify new cleavage sites within the MMP-9 propeptide.
  • To assess the impact of glycosylation on proMMP-9 resistance to various proteases and its activation rate.

Main Methods:

  • Chemical synthesis of aglycosyl propeptides and purification of recombinant glycosylated propeptides.
  • Western blot analysis to assess proteolysis resistance.
  • Zymography and dye-quenched gelatin cleavage assays to evaluate proteolytic activation.
  • Analysis of proMMP-9 from Congenital Disorder of Glycosylation patients.

Main Results:

  • New cleavage sites in the MMP-9 propeptide by MMP-3 and neutrophil elastase were identified.
  • Glycosylated pro-AT exhibited higher resistance to proteolysis compared to aglycosyl forms.
  • Larger oligosaccharides on human neutrophil proMMP-9 increased resistance to activation.
  • ProMMP-9 from CDG patients showed a higher activation rate by MMP-3.
  • Glycan-galectin-3 interactions were found to reduce proMMP-9 activation.

Conclusions:

  • MMP-9 propeptide glycosylation is a critical regulatory mechanism for its activation.
  • Glycosylation influences proMMP-9 stability and susceptibility to proteolysis.
  • This modification plays a significant role in modulating MMP-9 activity in physiological and pathological contexts.