Disease relevance of Mmp12

• Immunohistochemistry showed MMP-12 to be localized in activated monocytoid cells surrounding the hematoma [1].
• MMP-12 was detected in groups of macrophages Wistar rats lung exhibited a progressive morphological damage after 192 hours of recovery, after 8 daily doses of 1 mg/kg body weight on i.p. nicotine [2].

High impact information on Mmp12

• Similarly, in vivo minocycline treatment significantly reduced MMP-12 levels in brain [1].
• ICH increased brain MMP-2, -3, -7, and -9 mRNA levels relative to sham-injected (control) animals in the vicinity of the hematoma, but MMP-12 (macrophage metalloelastase) was the most highly induced MMP (>80-fold) [1].
• As expected, Western blot analyses also demonstrated increased production of MMP-12, MMP-14, and TIMP-2 (in the latter two cases as individual proteins and as complexes) [3].
• Although control cells were found to produce little or no MMP-9 (92-kD gelatinase B) or MMP-12 (metalloelastase), both enzymes were markedly upregulated upon stimulation [4].
• In addition to the expected transcript, a shorter one was identified and its sequence indicated that it corresponds to an alternatively spliced mRNA from which exons 5-18 of MME I are deleted [5].

Biological context of Mmp12

• It encodes a deduced 255 amino acid protein, MME II, instead of the 742 amino acid sequence of enkephalinase [5].
• Cigarette smoke can also promote MMP-12 gene expression and elevate the MMP-12/TIMP-1 ratio [6].

Anatomical context of Mmp12

• MME II mRNA is also expressed, together with MME I mRNA, in brain and thyroid in a tissue-specific manner [5].
• FGS lesions were defined by the presence of focal and segmental glomerular scarring and collapse of the glomerular tuft with increased mesangial cellularity (MC), mesangial matrix expansion (MME), and adhesions between the tuft and Bowman's capsule (Adh) [7].
• Within 3 days after axotomy in the peripheral nervous system, MMP-9, MMP-7 and MMP-12 are elevated [8].
• The ability of crude rat-brain microsome preparations to convert DME and MME to their corresponding phospholipid was explored [9].
• Morphometry was used to estimate the lung alveolar parenchyme and septal elastic fibers changes, and immunohistochemistry was performed to detect macrophage metalloelastase (MMP-12) and quantify vessels by immunolabelling with alpha-smooth muscle cells [2].

Associations of Mmp12 with chemical compounds

• This work suggests that MME and DME incorporated into the corresponding phospholipids function as effective substrates for phospholipid-N-methylation [10].
• The deduced structure of MME II is consistent with its being a membrane-bound, zinc-containing glycoprotein with a modified peptidase activity [5].
• Incubation of cells previously grown in presence of the bases MME and DME resulted in a marked increase of radioactivity in the corresponding phospholipids possessing one additional methyl group, PDME and PC respectively [10].
• Lung morphometry and MMP-12 expression in rats treated with intraperitoneal nicotine [2].
• Budesonide and N-acetylcysteine do not alter the MMP-12/TIMP-1 ratio in this study when given in the late phase of smoke exposure [6].

Other interactions of Mmp12

• The MMP-12/TIMP-1 ratio remained unchanged [6].
• Seven days after nerve crush, muscle MMP immunoreactivity, especially MMP-12 and MMP-14, became irregularly distributed [11].

Analytical, diagnostic and therapeutic context of Mmp12

• Amplification of rat intestine mRNAs was performed by the reverse transcriptase-polymerase chain reaction (RT-PCR) using various oligonucleotide primers mainly corresponding to the translated region of the enkephalinase (EC 3.4.24.11, membrane metalloendopeptidase, MME I) gene [5].
• Fetal rat brain aggregating cell cultures were exposed to varying concentrations of [3H]monomethylethanolamine (MME) and [3H] dimethylethanolamine (DME) [12].

References