Disease relevance of Mmp8

• Marked up-regulation of trypsin and MMP-8 early during hyperoxic lung injury suggests that these enzymes play a role in the pathogenesis of acute lung injury and may therefore be potential targets for therapy of lung injury [1].
• Biliary decompression results in increased MMP-8 activity co-localized to areas of portal fibrosis and PMN accumulation [2].
• We conclude that secretion of MMP-8 by neutrophils may play a critical role in resolving the fibrotic scar generated during cholestasis [2].
• In the present time-course studies of pneumococcal meningitis in infant rats, MMP-8 and -9 were 100- to 1000-fold transcriptionally upregulated, both in CSF cells and in brain tissue [3].
• RESULTS: LPS injection significantly (P<0.001) increased alveolar bone loss and increased collagenase (MMP-8), gelatinase (MMP-9), and elastase activities [4].

High impact information on Mmp8

• Western blot data showed that all forms of MMP-8 and MMP-13 were clearly reduced in the CMT-8 treated group compared to OVX [5].
• Our results show for the first time that MMP-8 mRNA and protein are expressed in rat wound epithelium [5].
• Westerns were run on the MMPs known to cleave fibrillar collagen in the rat (MMP-8, -13, and -14) as well as TIMP-1, -2, and -4 [6].
• MMP-8 and MMP-14 protein levels increased later during heart failure progression [6].
• Up-Regulation of Trypsin and Mesenchymal MMP-8 During Development of Hyperoxic Lung Injury in the Rat [1].

Biological context of Mmp8

• Expression of MMP-8 and MMP-13 mRNAs in rat periodontium during tooth eruption [7].
• We used the in situ hybridization method and semi-quantitative reverse-transcription/polymerase chain-reaction analysis to elucidate the gene expression of MMP-8 and MMP-13 mRNA [8].
• Furthermore, the expression of MMP8 is much broader than that of MMP13, for which expression is confined to differentiated phenotypes of osteoblastic and chondrocytic lineage [9].
• Gene expression of MMP8 and MMP13 during embryonic development of bone and cartilage in the rat mandible and hind limb [9].

Anatomical context of Mmp8

• MMP-8 was mostly expressed in macrophages [1].
• Repair after cholestatic liver injury correlates with neutrophil infiltration and matrix metalloproteinase 8 activity [2].
• In situ hydridization demonstrated expression of MMP-8 in osteoblasts, osteocytes, periodontal ligament cells, cementoblasts, and cementocytes along with collagen types I and III [7].
• The results demonstrated that MMP8 is expressed by osteoblastic progenitors, differentiated osteoblasts, osteocytes, and chondrocytes in the growth plate for the first time [9].
• On the hypothesis that MMP8 is also involved in bone and cartilage development, the present study was designed to investigate gene expression of MMP8 in rat embryonic mandibles and hind limbs [9].

Associations of Mmp8 with chemical compounds

• However, the regulating action of estrogen on the expression of interstitial collagenases MMP-8 and MMP-13 in osteoblastic cells in vivo remains unclear [10].
• The MMP-1 and MMP-8 expression levels were higher in intact corneas in the diclofenac sodium groups than in the ketorolac and artificial tears groups [11].

Other interactions of Mmp8

• In situ zymography was performed by using fluorogenic substrates for MMP-8 and MMP-2 to spatially localize enzymatic activity [2].
• Because Mmp-8 and -13 expression overlapped with Col2a1 and Col10a1, chondrocytes could play a pivotal role in degradation as well as production of the cartilaginous matrix in MCC [12].
• In the DTH lesions, significant increases in the level of mRNA expression were observed for MMP-7, MMP-8, MMP-12, and TNFalpha [13].

Analytical, diagnostic and therapeutic context of Mmp8

• We found that MMP-8 and MMP-13 mRNA were expressed in wound epithelium of all samples examined as evidenced by in situ hybridization [5].
• Expression of MMP-8 and MMP-13 mRNA transiently increased on both the compression and tension sides during active tooth movement in vivo [8].
• RT-PCR for the decalcified paraffin sections indicated expression of MMP-8 and MMP-13 in the periodontal tissues [7].
• Proliferation (Ki67) and expression of a matrix metalloproteinase (MMP-8) were examined by immunohistochemistry [14].

References