Biological and Pathobiological Functions of Gelatinase Dimers and Complexes

Malla, Nabin; Sjøli, Stian; Winberg, Jan‐Olof; Hadler‐Olsen, Elin; Uhlin‐Hansen, Lars

doi:10.1080/03008200802151755

Cited by 52 publications

(52 citation statements)

References 28 publications

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“…Gelatin-degrading enzymes are known to be associated with cell surface molecules and extracellular matrix components (Fridman et al 2003;Van den Steen et al 2006;Piccard et al 2007;Malla et al 2008b). Because these interactions involve hydrophobic, hydrogen, and ionic bonds, the use of different agents may be necessary to extract these enzymes from the tissue.…”

Section: Discussionmentioning

confidence: 99%

“…Pro-MMP-9 and pro-MMP-2 normally have an M r of 92 kDa and 72 kDa, respectively. In addition, it is known that MMP-9 can form complexes with a higher M r that are not dissolved in SDS (Winberg et al 2000;Malla et al 2008b). Western blots on non-reduced extracted material were therefore performed to determine which of the zymographic bands in gelatin zymography are produced by MMP-9 and MMP-2.…”

Section: Identification Of Extracted Enzymesmentioning

confidence: 99%

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Gelatin In Situ Zymography on Fixed, Paraffin-embedded Tissue: Zinc and Ethanol Fixation Preserve Enzyme Activity

Hadler‐Olsen

Kanapathippillai

Berg

et al. 2009

J Histochem Cytochem.

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In situ zymography is a method for the detection and localization of enzymatic activity in tissue sections. This method is used with frozen sections because routine fixation of tissue in neutral-buffered formalin inhibits enzyme activity. However, frozen sections present with poor tissue morphology, making precise localization of enzymatic activity difficult to determine. Ethanol- and zinc-buffered fixative (ZBF) are known to preserve both morphological and functional properties of the tissue well, but it has not previously been shown that these fixatives preserve enzyme activity. In the present study, we show that in situ zymography can be performed on ethanol- and ZBF-fixed paraffin-embedded tissue. Compared with snap-frozen tissue, ethanol- and ZBF-fixed tissue showed stronger signals and superior morphology, allowing for a much more precise detection of gelatinolytic activity. Gelatinolytic enzymes could also be extracted from both ethanol- and ZBF-fixed tissue. The yield, as analyzed by SDS-PAGE gelatin zymography and Western blotting, was influenced by the composition of the extraction buffer, but was generally lower than that obtained from unfixed tissue.

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Section: Discussionmentioning

confidence: 99%

Section: Identification Of Extracted Enzymesmentioning

confidence: 99%

Gelatin In Situ Zymography on Fixed, Paraffin-embedded Tissue: Zinc and Ethanol Fixation Preserve Enzyme Activity

Hadler‐Olsen

Kanapathippillai

Berg

et al. 2009

J Histochem Cytochem.

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“…Immunodetection of two high molecular weight protein bands (~140 and ~120 kDa, respectively) was greater in the ID than the MD extract and was absent in the OD (Figure 2). These bands may indicate MMP-2 complex formation with other proteins such as a TIMP, proteoglycan or bone sialoprotein (BSP) that could not be dissociated under the conditions used [23][24][25][26]. A greater amount of high molecular weight MMP-2 complex formation in the ID may explain the lower level of immunodetection of the pro-MMP-2 and MMP-2 as compared with MD.…”

Section: Discussionmentioning

confidence: 78%

Distribution and relative activity of matrix metalloproteinase‐2 in human coronal dentin

et al. 2011

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The presence of matrix metalloproteinase-2 (MMP-2) in dentin has been reported, but its distribution and activity level in mature human coronal dentin are not well understood. The purpose of this study was to determine the MMP-2 distribution and relative activity in demineralized dentin. Crowns of twenty eight human molars were sectioned into inner (ID), middle (MD), and outer dentin ( The concentration of MMP-2 in human coronal dentin was highest in the region of dentin that contains the dentinoenamel junction and least in the middle region of dentin. However, levels of Western blot immunodetection and gelatinolytic activity did not correlate with the estimated regional concentrations of MMP-2, potentially indicating region specific protein interactions.

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“…It is also important for localizing the enzyme at the cell periphery through interaction with low density lipoprotein-receptor related protein (LRP), CD-91 or different isomer forms of CD-44, protein Ku, and is involved in the formation of covalent complexes with proteoglycans (Malla et al, 2008;Monferran et al, 2004). …”

Section: Biological Properties Of Gelatinasesmentioning

confidence: 99%

Pharmacomodulation of Broad Spectrum Matrix Metalloproteinase Inhibitors Towards Regulation of Gelatinases

Bourguet¹,

Hornebeck²,

Sápi³

et al. 2012

Enzyme Inhibition and Bioapplications

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Biological and Pathobiological Functions of Gelatinase Dimers and Complexes

Abstract: The two matrix metalloproteinases, MMP-2 and MMP-9, are known to form various dimer complexes. In the present review, some of these complexes are described along with their biological and pathobiological functions.

Cited by 52 publications

References 28 publications

Gelatin In Situ Zymography on Fixed, Paraffin-embedded Tissue: Zinc and Ethanol Fixation Preserve Enzyme Activity

Gelatin In Situ Zymography on Fixed, Paraffin-embedded Tissue: Zinc and Ethanol Fixation Preserve Enzyme Activity

Distribution and relative activity of matrix metalloproteinase‐2 in human coronal dentin

Pharmacomodulation of Broad Spectrum Matrix Metalloproteinase Inhibitors Towards Regulation of Gelatinases

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