scholarly journals Suppressive Activity of Vitamin D3 on Matrix Metalloproteinase Production From Cholesteatoma Keratinocytes In Vitro

2005 ◽  
Vol 2005 (4) ◽  
pp. 210-215 ◽  
Author(s):  
Hitome Kobayashi ◽  
Kazuhito Asano ◽  
Ken-ichi Kanai ◽  
Harumi Suzaki
Keyword(s):  
Extracellular Matrix ◽  
Matrix Metalloproteinase ◽  
Vitamin D3 ◽  
Biological Activities ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Suppressive Activity ◽  
Tissue Specimens ◽  
Culture Supernatants ◽  
Dose Dependent

There is much evidence that degradation of the extracellular matrix is essential for the development of cholesteatomas and that this is induced by activation of matrix metalloproteinases (MMPs). Vitamin D3 (VD3) has several well-recognised biological activities, including suppression of MMP production. The present study, therefore, was undertaken to examine whether VD3 could suppress MMP production from cholesteatoma keratinocytes in vitro. Keratinocytes (2.5×105cells/mL) induced from cholesteatoma tissue specimens were cultured with various concentrations of VD3. After one hour, lipopolysaccharide was added to the cell cultures at 100μg/mL. The culture supernatants were then collected and assayed for MMP-1 and MMP-3 by ELISA. We also used ELISA to measure the levels of both TIMP (tissue inhibitor of metalloproteinase)-1 and TIMP-2 in culture supernatants. Addition of VD3 into keratinocyte cultures caused the suppression of MMP and TIMP production, which was increased by LPS stimulation. This was dose-dependent. The present results showing the suppressive activity of VD3 on the production of MMPs, which are responsible for tissue remodeling, strongly suggest that VD3 would be a good candidate for an agent in the medical treatment of, or prophylaxis for, cholesteatomas.

Bovine granulosa cells express extracellular matrix proteins and their regulators during luteinization in culture

1996 ◽  
Vol 8 (2) ◽  
pp. 259 ◽  
Author(s):  
Y Zhao ◽  
MR Luck
Keyword(s):  
Extracellular Matrix ◽  
Granulosa Cells ◽  
Culture Media ◽  
Gelatin Zymography ◽  
Fold Increase ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Subunit Gene ◽  
Gelatinase Activity ◽  
Cell Extracts

This study investigated the ability of bovine granulosa cells to express and secrete collagen, metalloproteinase (MMP) activity and a tissue inhibitor of metalloproteinase (TIMP-1) during luteinization in vitro. Cells from mature (1-2 mL fluid volume) bovine follicles were cultured over 4 days in serum-free medium. Their luteinization during culture was confirmed by a 10-fold increase in progesterone secretion. Samples of cell extracts, culture media and follicular fluid were subjected to Western blotting to identify secreted proteins and to gelatin zymography to detect enzyme activity. Poly A+ RNA, isolated from cells before and after culture, was probed to detect expression of collagen alpha 1(I), collagen alpha 3(IV) and TIMP-1. The results revealed that: (1) the collagen alpha 1(I) subunit gene was expressed in cells before culture but with greater intensity by Day 4 culture; collagen I protein, on the other hand, was not detectable in culture medium; (2) the collagen alpha 3(IV) subunit gene was expressed at a low level in uncultured cells and could be detected on Day 4 of culture; low amounts of the protein were detected in medium; (3) a 92-kDa band of gelatinase activity (presumed MMP-9) was present in all medium samples, together with bands of unidentified activity; and (5) the TIMP-1 gene was expressed in uncultured cells but its expression increased markedly up to Day 4 of culture. These results show that granulosa luteinization is associated with an increase in the expression of collagen, collagen-degrading enzymes and TIMP-1. Collagen protein, however, may be only poorly synthesized in this culture model. The results suggest that granulosa-derived cells are a likely source of components of the extracellular matrix during post-ovulatory remodelling of early luteal tissue.

Pravastatin increases the expression of the tissue inhibitor of matrix metalloproteinase-1 and the oncogeneBaxin human aortic abdominal aneurysms

2008 ◽  
Vol 86 (7) ◽  
pp. 431-437 ◽  
Author(s):  
Petra J. Mateos-Cáceres ◽  
Antonio J. López-Farré ◽  
Pilar C. Morata ◽  
Priscila Ramos-Mozo ◽  
Carlos Macaya ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Apoptotic Index ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Tissue Inhibitor ◽  
Hmg Coa Reductase ◽  
Matrix Metalloproteinase 1 ◽  
Abdominal Aortic ◽  
Coa Reductase ◽  
Metalloproteinase 9

The effect of pravastatin on matrix metalloproteinase-9 (MMP-9) and the level of tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2 was studied in explants of human abdominal aortic aneurysm (AAA) obtained from 13 patients. The effect of pravastatin on the apoptotic status of human AAA explants was also examined. Total MMP-9 content did not differ in human AAA explants incubated in vitro in the presence or absence of pravastatin (10−6mol/L) for 48 h. TIMP-1 levels were significantly increased in pravastatin-incubated AAA explants, but TIMP-2 production was not modified by pravastatin. Western blot experiments showed that, whereas Bax expression was increased in pravastatin-incubated AAA explants, the expression of Bcl-2 was not modified. On the other hand, the ratio of the expression of Bax to Bcl-2, an apoptotic index, was not modified by pravastatin. In the human AAA explants, the increase in Bax expression, but not the increase in TIMP-1 expression elicited by pravastatin, was reversed by l-mevalonate, a downstream HMG-CoA reductase metabolite, suggesting that the expression of Bax and TIMP-1 followed HMG-CoA reductase-dependent and -independent pathways, respectively. In conclusion, pravastatin increases both TIMP-1 and Bax expression in human AAA explants without changes in either MMP-9 activity or the apoptotic status.

scholarly journals Comparative extraction, phytochemical screening and in vitro biological activities of Eclipta prostrata extract

2020 ◽  
Vol 10 (4-s) ◽  
pp. 148-152
Author(s):  
Zafar Alam Khan ◽  
Salaj Khare ◽  
B.K. Dubey
Keyword(s):  
Therapeutic Potential ◽  
Biological Activities ◽  
Chemical Constituents ◽  
Antidiabetic Activity ◽  
Diffusion Method ◽  
Phytochemical Analysis ◽  
Eclipta Prostrata ◽  
Promising Source ◽  
Dose Dependent

Medicinal plants possess therapeutic potential and are used to treat various diseases around the world. Eclipta prostrate (L.) is a medicinal herb that has extensive application in the native medicinal system. In any therapeutic activity chemical constituents play an important role. Eclipta prostrata has been investigated in this study for its antioxidant, antimicrobial and antidiabetic activity in vitro. The well-known research protocol available in the literature established qualitative analysis of the different phytochemical constituents and quantitative analysis of total phenol and flavonoids. The hydroalcoholic extracts of the leaves and seeds of Eclipta prostrata exhibited significant and dose-dependent antioxidant activity including ability to donate electron. To analyze the antimicrobial activity, Leaves hydroalcoholic extracts and Eclipta prostrate seeds were tested against two selected strains using a well-diffusion method and showing significant inhibitory action against all the strain tested. In addition, the dose-dependent α-amylase inhibitory activity with an IC50 value of acarbose, leaves, and seed extract was found to be 364.89μg/ml and 438.43μg/ml, respectively, indicating that Eclipta prostrate is a promising source as an herbal medicine. Keywords: Eclipta prostrate, Phytochemical Analysis, Antioxidant, Antimicrobial, Antidiabetic Activity.

Rat olfactory neurons can utilize the endogenous lectin, L-14, in a novel adhesion mechanism

Development ◽  
1994 ◽  
Vol 120 (6) ◽  
pp. 1373-1384 ◽  
Author(s):  
N.K. Mahanthappa ◽  
D.N. Cooper ◽  
S.H. Barondes ◽  
G.A. Schwarting
Keyword(s):  
Extracellular Matrix ◽  
Olfactory Nerve ◽  
System A ◽  
System L ◽  
L 14 ◽  
Dose Dependent ◽  
Putative Member ◽  
Binding Lectin

L-14 is a divalent, lactosamine-binding lectin expressed in many vertebrate tissues. In the rat nervous system, L-14 expression has been observed previously in restricted neuronal subsets within the dorsal root ganglia and spinal cord. In this study we report that L-14 is expressed by nonneuronal cells in the rat olfactory nerve. We demonstrate that L-14 binds and co-localizes with two ligands in the rat olfactory system: a beta-lactosamine-containing glycolipid, and a putative member of the laminin family. The former is expressed on the surfaces of nascent olfactory axons originating from neuron cell bodies in the olfactory epithelium. The latter is present in the extracellular matrix of the axonal path leading to synaptic targets in the olfactory bulb. In vitro, we find that recombinant L-14 promotes primary olfactory neuron adhesion to two laminin family members, and promotes intercellular adhesion. Both activities are dose-dependent, and are independent of integrin-mediated mechanisms. We have thus found that L-14 can serve two distinct adhesive functions in vitro, and propose that L-14 in vivo can promote olfactory axon fasciculation by crosslinking adjacent axons and promote axonal adhesion to the extracellular matrix.

scholarly journals Apatite Reduces Amelogenin Proteolysis by MMP-20 and KLK4 in vitro

2010 ◽  
Vol 89 (4) ◽  
pp. 344-348 ◽  
Author(s):  
Z. Sun ◽  
W. Carpiaux ◽  
D. Fan ◽  
Y. Fan ◽  
R. Lakshminarayanan ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Proteolytic Activity ◽  
Proteolytic Processing ◽  
Enamel Formation ◽  
Dependent Relationship ◽  
Kallikrein 4 ◽  
Synthetic Hydroxyapatite ◽  
Dose Dependent

Two enamel proteases, matrix metalloproteinase-20 (MMP-20) and kallikrein 4 (KLK4), are known to cleave amelogenin and are necessary for proper enamel formation. However, the effect of hydroxyapatite (HAP) on the proteolytic activity of these enzymes remains unclear. To investigate whether apatite affects normal amelogenin proteolysis, we used 2 different isoforms of amelogenin combined with the appropriate enzymes to analyze proteolytic processing rates in the presence or absence of synthetic hydroxyapatite (HAP) crystals (N = 3). We found a distinct dose-dependent relationship between the amount of HAP present in the proteolysis mixture and the rate of rP172 degradation by rpMMP-20, whereas the effect of HAP on proteolysis of either rP172 or rP148 by rhKLK4 was less prominent.

Extracellular matrix metalloproteinase inducer (EMMPRIN) is present in smooth muscle cells of human aneurysmal aorta and is induced by angiotensin II in vitro

2009 ◽  
Vol 116 (11) ◽  
pp. 819-826 ◽  
Author(s):  
Xiao-feng Chen ◽  
Jian-an Wang ◽  
Jun Hou ◽  
Chun Gui ◽  
Li-jiang Tang ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Smooth Muscle ◽  
Angiotensin Ii ◽  
Aortic Aneurysm ◽  
Aortic Dissection ◽  
Matrix Metalloproteinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Extracellular Matrix Metalloproteinase Inducer

The aim of the present study was to determine whether EMMPRIN (extracellular matrix metalloproteinase inducer) is present and is up-regulated in human aneurysmal aortas, and to assess a possible association with AngII (angiotensin II)-induced aneurysm formation. The presence of EMMPRIN was assessed in 41 surgical specimens from patients with a TAA (thoracic aortic aneurysm) (Type A aortic dissection, n=12; Type B aortic dissection, n=7; and TAA without dissection, n=7) or an AAA (abdominal aortic aneurysm, n=15) by immunohistochemistry. EMMPRIN expression in aortic aneurysm tissues was compared with 12 aortas obtained during autopsy (free of any vascular diseases), and scored for both staining intensity and the percentage of vascular cells stained. EMMPRIN protein levels in cultured human aortic SMCs (smooth muscle cells) following stimulation of AngII were analysed by Western blotting. Significant EMMPRIN immunoreactivity was detected in aortic aneurysm lesions from patients with TAAs and AAAs. In the aneurysmal wall, α-actin-positive SMCs were the main source of EMMPRIN. The frequency of EMMPRIN overexpression was significantly higher (P=0.026) in TAAs with dissection (68.4%) than TAAs without dissection (14.3%). AngII stimulation up-regulated the expression of EMMPIRN in cultured human aortic SMCs, which was suppressed by the addition of the AT1R (AngII type 1 receptor) antagonist losartan. In conclusion, the present study is the first to report the expression of EMMPRIN in aortic aneurysmal diseases, and we speculate that EMMPRIN may be important in the pathogenesis of these diseases. Whether these abnormalities are potential therapeutic targets deserve further investigation.

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