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PubMed2001

Activation of matrix-metalloproteinase-2 and membrane-type-1-matrix-metalloproteinase in endothelial cells and induction of vascular permeability in vivo by human immunodeficiency virus-1 Tat protein and basic fibroblast growth factor.

Previous studies indicated that the Tat protein of human immunodeficiency virus type-1 (HIV-1) is a progression factor for Kaposi's sarcoma (KS). Specifically, extracellular Tat cooperates with basic fibroblast growth factor (bFGF) in promoting KS and endothelial cell growth and locomotion and in inducing KS-like lesions in vivo. Here we show that Tat and bFGF combined increase matrix-metalloproteinase-2 (MMP-2) secretion and activation in endothelial cells in an additive/synergistic manner. These effects are due to the activation of the membrane-type-1-matrix-metalloproteinase and to the induction of the membrane-bound tissue inhibitor of metalloproteinase-2 (TIMP-2) by Tat and bFGF combined, but also to Tat-mediated inhibition of both basal or bFGF-induced TIMP-1 and -2 secretion. Consistent with this, Tat and bFGF promote vascular permeability and edema in vivo that are blocked by a synthetic MMP inhibitor. Finally, high MMP-2 expression is detected in acquired immunodeficiency virus syndrome (AIDS)-KS lesions, and increased levels of MMP-2 are found in plasma from patients with AIDS-KS compared with HIV-uninfected individuals with classic KS, indicating that these mechanisms are operative in AIDS-KS. This suggests a novel pathway by which Tat can increase KS aggressiveness or induce vasculopathy in the setting of HIV-1 infection.

Acquired Immunodeficiency Syndrome↗

PubMed1999

Cyclic mechanical stress induces extracellular matrix degradation in cultured chondrocytes via gene expression of matrix metalloproteinases and interleukin-1.

To clarify the mechanism of cartilage degradation induced by mechanical stress, we investigated the influence of cyclic tension force (CTF) on the metabolism of cultured chondrocytes. The chondrocytes were exposed to CTF using a Flexercell strain unit. Five or 15 kPa of high frequency CTF significantly inhibited the syntheses of DNA, proteoglycan, collagen, and protein. Fifteen kPa of high frequency CTF induced the expression of interleukin-1 (IL-1), matrix metalloproteinase (MMP)-2 and -9 mRNA, and increased the production of pro- and active-MMP-9. The degradation of proteoglycan was inhibited by and MMP inhibitor, indicating that MMPs are involved in the degradation of proteoglycans induced by high frequency CTF. Moreover, reducing the frequency of CTF from high to low decreased the inhibition of proteoglycan synthesis. These findings suggest that the CTF frequency is one of the key determinants of chondrocyte metabolism. Low magnitude CTF, whether high or low frequency, did not cause the gene expression of cartilage degradation factors, suggesting that this CTF magnitude causes only minor changes in the cartilage matrix. High magnitude and frequency CTF caused the gene expression of IL-1 and MMP-9, followed by increases in the production of MMP-2 and -9 proteins, suggesting that excessive and continuous cyclic mechanical stress induces the production of IL-1 and MMP-9, resulting in cartilage degradation.

Animals↗

PubMed2000

Expression of matrix metalloproteinase-2, -9, and -14, tissue inhibitors of metalloproteinase-1, and matrix proteins in human placenta during the first trimester.

Matrix metalloproteinases (MMPs) are implicated in the degradation of extracellular matrix; they play important roles in the invasion of the trophoblast cell into the maternal endometrium during placentation. Previous studies have concentrated on comparison of MMP expression in trophoblast cells between the first and third trimester. But the dynamic expression of MMPs during the first trimester has not been reported. In the present study, the expression of MMP-2, -9, and -14 (membrane-type MMP-1) and the production of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) by cultured human cytotrophoblast cells from 6 to 11 wk of gestation were investigated. The cells were cultured under serum-free conditions. There was no MMP-9 secretion by the cells at Week 6, but from Week 7 to 11 the MMP-9 secretion increased gradually. Week 11 cells secreted more than 10-fold as much MMP-9 (167.7 +/- 18.8 ng/ml) as Week 7 (14.7 +/- 3.9 ng/ml) cultures. However, MMP-2 production declined from Week 6 to Week 11, and the production at Week 11 (32.3 +/- 8.1 ng/ml) was about one sixth that at Week 6 (205.7 +/- 27.2 ng/ml). The expression of mRNA transcripts for MMP-2 and MMP-9 correlated with enzyme secretion; we did not detect any MMP-9 mRNA signal in 20 microg total RNA extracted from cultured cells at Weeks 6, 7, and 8 of pregnancy, but a signal was apparent in Weeks 9 and 11. MMP-2 mRNA was expressed throughout the 6- to 11-wk period and exhibited a remarkable decline during this period. MMP-14 mRNA transcripts remained relatively stable from 6 to 11 wk. Significantly more TIMP-1 (P < 0.01) was detected in Week 9 (87.5 +/- 15.0 ng/ml) and Week 11 (169.1 +/- 30.2 ng/ml) media compared to Week 6 media (23.5 +/- 4.8 ng/ml), but we did not detect any TIMP-2 in the media of the tested cells. This study demonstrated that first-trimester human cytotrophoblast cells were able to produce abundant laminin, fibronectin, and vitronectin. However, we did not observe detectable secretion of collagen I and collagen IV. These data indicated that human trophoblast-derived MMPs and their inhibitors are intrinsically and developmentally regulated. The same cytotrophoblast cells that produced MMPs could also secrete various substrates for these enzymes.

Adult↗

PubMed2001

Matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-3 are key regulators of extracellular matrix degradation by mouse embryos.

Embryo implantation in humans and rodents is a highly invasive yet tightly controlled process involving extracellular matrix (ECM) degradation. Matrix metalloproteinase 9 (MMP-9) has been implicated as the major facilitator of this ECM degradation. MMP-9 is expressed by the embryo's trophoblast cells, whereas tissue inhibitor of metalloproteinases 3 (TIMP-3) is expressed by the maternal uterine cells immediately adjacent to the trophoblast. We examined the functional roles of MMP-9 and TIMP-3 during in vitro ECM degradation by mouse embryos. Blastocysts were treated with either MMP-9 antisense or sense oligonucleotides and incubated on an ECM gel. The extent of ECM degradation exhibited by the blastocysts due to proteinase secretion was quantified. Embryos exposed to MMP-9 antisense oligonucleotides exhibited reduced ECM-degrading activity as compared with controls, and this reduced activity was correlated with the level of MMP-9 secreted by the embryos. The functional role of TIMP-3 was then examined by incubating blastocysts on an ECM gel that had been impregnated with various amounts of TIMP-3. In a dose-dependent manner, increases in TIMP-3 resulted in a reduction in ECM degradation and were correlated with diminished MMP-9 activity. These results provide important functional evidence that in vitro ECM degradation is regulated by embryo-derived MMP-9 and ECM-derived TIMP-3.

Animals↗

PubMed2002

Extracellular matrix and matrix metalloproteinase changes in human corneas after complicated laser-assisted in situ keratomileusis (LASIK).

PURPOSE: To characterize extracellular matrix (ECM) and nine matrix metalloproteinase (MMP) changes in two corneas that underwent a complicated laser-assisted in situ keratomileusis (LASIK) procedure. METHODS: The first patient underwent bilateral LASIK. The flap on the left eye was transected in several locations and placed back. This cornea later developed edema, and the removed flap was analyzed after lamellar keratoplasty. The second patient had a LASIK flap lifted, replaced twice, and then completely removed. The epithelium grew over the stroma, but haze and severe ectasia occurred. After penetrating keratoplasty, the recipient cornea was analyzed. An autopsy cornea from a person who underwent uneventful LASIK and ten normal autopsy corneas served as controls. Corneas were analyzed by immunohistochemistry. RESULTS: Both flap regions in the treated corneas had marked alterations of ECM components and MMPs. Stromal deposits of various ECM proteins, including those normally absent in the central cornea (tenascin-C, fibrillin-1, type XIV collagen), were found. Rare myofibroblasts and inflammatory cells were present. The epithelial basement membrane (BM) was altered in both cases. The most dramatic change was poor or no staining for alpha3-alpha6 type IV collagen chains and thrombospondin. The limbal alpha1-alpha2 type IV collagen and laminin-2 (alpha2beta1gamma1) appeared in the central epithelial BM. Other components were altered to a lesser extent. The anterior stroma was positive for MMP-1 and MMP-2, and some MMP-7 was seen in the epithelium. These ECM and MMP patterns were not seen in uneventful LASIK or normal corneas. CONCLUSIONS: In the flaps of LASIK-treated corneas, fibrosed areas of anterior stroma had increased levels of MMP-1 and MMP-2 that may have caused loss of specific type IV collagen isoforms in the epithelial BM. These changes may reflect an ongoing wound healing process and contribute to the development of ectasia.

Adult↗

PubMed2006

Extracellular matrix protein 1 inhibits the activity of matrix metalloproteinase 9 through high-affinity protein/protein interactions.

Extracellular matrix protein 1 (ECM1), an approximately 85-kDa glycoprotein with broad tissue distribution, harbors mutations in lipoid proteinosis (LP), a heritable disease characterized by reduplication of basement membranes and hyalinization of dermis, associated with neurologic disorders. The mechanisms leading from ECM1 mutations to LP phenotype are unknown. In this study, we explored ECM1 protein-protein interactions utilizing yeast two-hybrid genetic screen of human placental library, which identified nine interacting proteins, including matrix metalloproteinase 9 (MMP9). The interactions were confirmed by beta-galactosidase assay with isolated clones and by co-immunoprecipitation which narrowed the interacting segment in ECM1 to the C-terminal tandem repeat 2 (amino acids 236-361). This peptide segment also inhibited MMP9 activity in a gelatin-based ELISA assay. We propose that ECM1-mediated reduction in MMP9 proteolytic activity may have relevance to pathogenesis of LP.

Biosensing Techniques↗

PubMed2004

Hyperoxia decreases matrix metalloproteinase-9 and increases tissue inhibitor of matrix metalloproteinase-1 protein in the newborn rat lung: association with arrested alveolarization.

Matrix metalloproteinases (MMP) are likely effectors of normal lung development, especially branching morphogenesis, angiogenesis, and extracellular matrix degradation. Because hyperoxia exposure (>95% O(2)) from d 4 to 14 in newborn rat pups leads to arrest of alveolarization and mimics newborn chronic lung disease, we tested whether hyperoxia altered MMP-2 and -9 mRNA, protein, and enzymatic activity, and the mRNA and protein expression of the endogenous tissue inhibitor of MMP, TIMP-1. No changes due to hyperoxia exposure were observed in MMP-2 mRNA or pro-enzyme (72 kD) protein levels between d 6 and 14, although the overall protein mass and zymographic activity of the active (68 kD) enzyme were diminished (p < 0.05, ANOVA). However, hyperoxia significantly decreased levels of MMP-9 mRNA and pro-MMP-9 protein and diminished overall MMP-9 pro-enzyme activity. TIMP-1 mRNA was not elevated by hyperoxia until d 14, but protein levels were significantly (p < 0.001) elevated by hyperoxia from d 9 to 14. To estimate the potential of MMP inhibition to arrest alveolarization, administration of doxycycline (20 mg/kg, twice daily by gavage), a pan-MMP proteolysis inhibitor, arrested lung alveolarization. We conclude that hyperoxia decreases MMP-9 mRNA, protein, and activity and elevates TIMP-1 protein, and these changes have the potential to contribute to the arrest of normal lung development.

Animals↗

PubMed1998

Coordinated and cell-specific regulation of membrane type matrix metalloproteinase 1 (MT1-MMP) and its substrate matrix metalloproteinase 2 (MMP-2) by physiological signals during follicular development and ovulation.

In the ovary, extensive tissue remodeling is required during both follicular development and the break down of the follicular wall at the time of ovulation. Extracellular proteases such as serine proteases and matrix metalloproteinases (MMPs) are thought to play pivotal roles in these processes. In this paper, we have used in situ hybridization to study the regulation and distribution of mRNA coding for MMP-2 (gelatinase A) and its cell surface activator membrane-type MMP1 (MT1-MMP) during gonadotropin induced ovulation in the rat. In ovaries of untreated immature (23 day old) rats, the levels of MT1-MMP and MMP-2 mRNA were low. MMP-2 mRNA was found in theca-interstitial cells while MT1-MMP mRNA was found in both granulosa and theca-interstitial cells and both messages were induced after stimulation with PMSG. After an ovulatory dose of hCG, the expression of MT1-MMP was dramatically down regulated in the granulosa cell layers of large preovulatory follicles but the expression remained and appeared to be up regulated together with MMP-2 in the theca-interstitial cells surrounding the large preovulatory follicles. The expression kinetics and tissue distribution supports the notion that MT1-MMP may have dual functions in the ovary. Initially MT1-MMP may act as a matrix degrading protease inside the follicle during follicular development and later, just prior to ovulation, as an activator of proMMP-2 in theca-interstitial cells surrounding preovulatory follicles.

Animals↗

PubMed2004

[Dynamic expression of matrix metalloproteinase-2, membrane type-matrix metalloproteinase-2 in experimental hepatic fibrosis and its reversal in rat].

OBJECTIVE: To investigate the expression dynamics and significance of matrix metalloproteinase-2 (MMP-2) membrane type-matrix metalloproteinase-2 (MT-MMP-2) in hepatic fibrosis and its reversal counterpart. METHODS: An experimental CCl4 induced hepatic fibrosis rat model was established by intraperitoneal administration of carbon tetrachloride for 2, 4, 6, 8, 10 weeks, and normal rats were used as a control group. The immunohistochemical methods and in situ hybridization were used to detect MMP-2,MT-MMP-2 mRNA and related antigens in the liver. RESULTS: MMP-2,MT-MMP-2 mRNA and related antigens were expressed in mesenchymal cells and parts of hepatocytes besides active pathological changes, especially in the fibrous septum and portal area. Expression of MMP-2,MT-MMP-2 mRNA and related antigens were increased in hepatic fibrosis and decreased gradually in its reversal counterpart. CONCLUSION: This study suggested that mesenchymal cells are the main cellular origins of MMPs. The levels of MMP-2 and MT-MMP-2 antigens and gene expression were closely related to hepatic fibrosis. MMP-2 and MT-MMP-2 may play important roles in hepatic fibrosis and its reversal counterpart.

Animals↗

PubMed2005

[The protein expression difference of transforming growth factor beta1, matrix metalloproteinases 1,7,9 and tissue inhibitors of matrix metalloproteinases-1 between chronic rhinosinusitis, nasal polyps and normal mucosa tissues].

OBJECTIVE: To compare the expression difference of transforming growth factor beta1 (TGF-beta1), matrix metalloproteinases1,7,9 (MMP-1,7,9 ) and tissue inhibitors of matrix metalloproteinases-1 (TIMP-1) protein among the chronic rhinosinusitis tissues, nasal polyps tissues and normal nasal mucosa tissues. METHOD: The protein expression of TGF-beta1, MMP-1, MMP-7, MMP-9 and TIMP-1 in chronic rhinosinusitis tissues from 22 patients, in nasal polyps tissues from 21 patients and in inferior turbinate tissues from 15 patients underwent nasal septum operation was detected by enzyme-linked immunosorbent assay (ELISA). RESULT: (1) In chronic rhinosinusitis and nasal polyps tissues, compared with controls, the expression of TGF-beta1, MMP-7, MMP-9, TIMP-1 protein was significant increased (P < 0.05); (2) The expression of TGF-beta1 and TIMP-1 in chronic rhinosinusitis tissues was significant increased versus that in nasal polyps tissues (P < 0.05); (3) Concentration of MMP-7 protein in nasal polyps tissues was found significant higher than that in chronic rhinosinusitis tissues (P < 0.01). CONCLUSION: Different TGF-beta1, MMP-7, TIMP-1 protein level in chronic rhinosinusitis and nasal polyps tissues might be the molecular basis of the different histopathological character of chronic rhinosinusitis and nasal polyp tissues.

Adolescent↗

PubMed1997

Imbalance of expression of matrix metalloproteinases (MMPs) and tissue inhibitors of the matrix metalloproteinases (TIMPs) in human pancreatic carcinoma.

Degradation of the extracellular matrix (ECM) is an essential step in tumour invasion and metastasis. The matrix metalloproteinases (MMPs) each have different substrate specificities within the ECM and are important in its degradation. MMP activity is dependent on the levels of activated MMP and tissue inhibitors of matrix metalloproteinases (TIMPs). The expression of MMPs and TIMPs in pancreatic carcinoma, normal pancreas, and pancreatic carcinoma cell lines has been determined by Northern analysis. The transcripts have been localized by in situ hybridization and the MMP2 protein by immunohistochemistry. Expression of MMP2, -7, and -11 was greater in pancreatic carcinoma than in normal pancreas (P < 0.01). MMP7 expression in normal pancreas and MMP7 and -11 expression in tumours was always seen the TIMP1 expression. TIMP2 was expressed in only half of the tumours and a previously undescribed transcript size is reported for TIMP2. MTMMP was expressed concurrently with MMP2 in 64 per cent of tumours, but concurrent MMP2 and TIMP2 expression occurred in only half. MMP2 mRNA was found more often in the tumour stroma than with the other MMPs or TIMPs (P < 0.02). It is concluded that while overexpression of MMP7 and -11 may be countered by TIMP1, the aggressive phenotype of pancreatic carcinoma may occur because of overexpression of MMP2, activated by MTMMP and associated with a reduced expression of TIMP2.

Blotting, Northern↗

PubMed1995

Conservative sorting of F0-ATPase subunit 9: export from matrix requires delta pH across inner membrane and matrix ATP.

In an attempt to understand the mechanisms of sorting of mitochondrial inner membrane proteins, we have analyzed the import of subunit 9 of the mitochondrial F1F0-ATPase (Su9) from Neurospora crassa, an integral inner membrane protein. A chimeric protein was used consisting of the presequence and the first transmembrane domain of Su9 fused to mouse dihydrofolate reductase (preSu9(1-112)-DHFR). This protein attains the correct topology across the inner membrane (Nout-Cin) following import. The transmembrane domain becomes first completely imported into the matrix, where after processing of the presequence, it mediates membrane insertion and export of the N-terminal tail. Import and export steps can be experimentally dissected into two distinct events. Translocation of the N-terminal hydrophilic tail out of the matrix was blocked when the presequence was not processed, indicating an important role of the sequences and charges flanking the hydrophobic domain. Furthermore, export was supported by a delta pH and required matrix ATP hydrolysis. Thus the hydrophobic transmembrane domain operates as a membrane insertion signal and not as a stop-transfer signal. Our findings suggest that several aspects of this sorting process have been conserved from their prokaryotic ancestors.

Adenosine Triphosphate↗

PubMed2007

Rapid on-plate and one-pot derivatization of carbonyl compounds for enhanced detection by reactive matrix LDI-TOF MS using the tailor-made reactive matrix, 4-dimethylamino-6-(4-methoxy-1-naphthyl)-1,3,5-triazine-2-hydrazine (DMNTH).

In this study, a very sensitive and economical high-throughput methodology has been developed for the analysis of small carbonyl compounds using rapid derivatization with 4-dimethylamino-6-(4-methoxy-1-naphthyl)-1,3,5-triazine-2-hydrazine (DMNTH), a derivatizing agent developed by the Karst group at the University of Münster. DMNTH is highly ionizable by the UV laser and reacts selectively and rapidly with carbonyl moieties. The resulting hydrazone is easily detectable by laser desorption ionization time of flight mass spectrometry (LDI-TOF MS), eliminating the need for the matrix assisted variant (MALDI) and the associated issue of matrix optimization, which greatly simplifies the analysis. It has been demonstrated that a range of carbonyl compounds can be conveniently analyzed by this reactive matrix LDI-TOF MS (RM-LDI-TOF MS) procedure and that furfural DMNThydrazone (prior labeled and labeled in situ) can be used as an internal standard for semiquantitative analysis. Amounts as low as 0.5 ng ml(-1) of 4-methoxybenzaldehyde have been detected using a one-pot derivatization methodology. Rapid on-plate derivatization was also found to be a simple approach for fast and reliable screening of various analytes, although with slightly higher detection limits. To test its applicability in complex matrices, analysis of furfural spiked in beer has been demonstrated. This RM-LDI-TOF MS method shows considerable promise for the analysis of carbonyl compounds in water, particularly for disinfection by-products that result from reaction of natural organic matter with oxidative disinfectants.

Journal Article↗

PubMed1993

Matrix-assisted laser desorption time-of-flight mass spectrometry of oligonucleotides using 3-hydroxypicolinic acid as an ultraviolet-sensitive matrix.

Matrix-assisted laser desorption time-of-flight mass spectrometry has been used to produce quasi-molecular ion signals from underivatized mixed-base single-stranded DNA oligomers ranging from 10 to 67 nucleotides in length. These results were obtained with a new matrix material, 3-hydroxypicolinic acid (3-hydroxypyridine-2-carboxylic acid) which showed significant improvement over many previously reported matrices studied in terms of mass range available, signal-to-noise ratio, and the ability to analyze mixed-base oligomers. The desorption and simultaneous ionization was by pulsed laser light at 10 to 50 mJ/cm2, studied at 266, 308, and 355 nm. Spectra taken at 266 nm provided the smallest amounts of doubly charged and dimer ions--characteristics desirable for DNA sequencing by this technology. Negative-ion spectra were uniformly superior to positive-ion spectra. This new matrix also is quite effective for molecular weight determinations of peptides and proteins in both positive- and negative-ion modes.

Base Sequence↗

PubMed2004

Glass-chip-based sample preparation and on-chip trypic digestion for matrix-assisted laser desorption/ionization mass spectrometric analysis using a sol-gel/2,5-dihydroxybenzoic acid hybrid matrix.

A glass-chip-based sample preparation method for matrix-assisted laser desorption/ionization mass spectrometric (MALDI-MS) analysis of tryptic digests of proteins and intact cells is described. A MALDI matrix, 2,5-dihydroxybenzoic acid (2,5-DHB), was hybridized with sol-gels to generate a sol-gel-derived material. Taking advantage of the characteristics of sol-gels, the sol-gel-derived material readily adhered to the surface of a glass chip through covalent bonding. Only one step of sample preparation, deposition of the sample solution on the glass chip, was required before MALDI-MS analysis. Because 2,5-DHB was homogeneously dispersed on the sol-gel network structure, good spot-to-spot reproducibility was obtained in MALDI analysis using this approach and the analyte signals were uniform throughout the chip. The modified glass chips were robust and effective for at least 1 week. This glass-chip-based matrix preparation method provides a straightforward approach to developing techniques for analyzing the on-chip enzymatic digestion of proteins and intact cells of microorganisms. Cytochrome C and Escherichia coli were used as analytes to demonstrate the feasibility of this approach. The products of the on-chip enzymatic digests were identified through protein database searches.

Amino Acid Sequence↗

PubMed2007

2B or not 2B, that is the question: further investigations into the use of pencil as a matrix for matrix-assisted laser desorption/ionisation.

The effective use of pencil as a matrix for matrix-assisted laser desorption/ionisation (MALDI) for the study of actinides has previously been demonstrated (Black et al., Rapid Commun. Mass Spectrom. 2006; 20: 1053). Here, the scope of the types of molecules amenable to analysis by this method has been extended, establishing that approximately 90% of a library containing 50 diverse small molecules can be successfully analysed by this technique. Further, the role played by the bulk materials present in the different pencil leads has been investigated and a simple one-step deposition of matrix and calibration materials has been achieved through the fabrication of different calibration pencils (Cali-Pens).

Journal Article↗

PubMed1984

Induction of new proteins in the nuclear matrix of CHO cells by a heat shock: detection of a specific set in the nucleolar matrix.

An early response to an incubation of CHO cells for one hour at 43 degrees C is the appearance in the nuclear matrix of new proteins: 2 proteins (48 and 46 kDa) were associated with the extranucleolar part of the nuclear matrix, 6 other proteins (130, 100, 95, 85, 76 and 70 kDa) were present in matrices prepared from isolated nucleoli. In addition, a large increase in the amount of associated minor components is observed. It is suggested that these early modifications in composition of the matrix are related to the inhibition of rRNA and hnRNA synthesis and maturation.

Animals↗

PubMed1989

DNA fragments which specifically bind to isolated nuclear matrix in vitro interact with matrix-associated DNA topoisomerase II.

A matrix-associated region (MAR)-containing fragment has been selected from the library of cloned chicken nuclear matrix-associated DNA fragments. Factors, which determine the specific binding of DNA fragments have been studied. Using topoisomerase II-specific inhibitor VM 26 we established that nuclear matrix-associated topoisomerase II interacted with the MAR-containing DNA fragment producing specific cleavage sites on DNA of the fragment.

Animals↗