scholarly journals Modulation of the Catalytic Activity of Neutrophil Collagenase MMP-8 on Bovine Collagen I

2002 ◽  
Vol 277 (26) ◽  
pp. 23123-23130 ◽  
Author(s):  
Magda Gioia ◽  
Giovanni Francesco Fasciglione ◽  
Stefano Marini ◽  
Silvana D'Alessio ◽  
Giampiero De Sanctis ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Collagen I ◽  
Bovine Collagen ◽  
Neutrophil Collagenase

scholarly journals Cleavage of Bovine Collagen I by Neutrophil Collagenase MMP-8

2000 ◽  
Vol 275 (25) ◽  
pp. 18657-18663 ◽  
Author(s):  
Stefano Marini ◽  
Giovanni Francesco Fasciglione ◽  
Giampiero de Sanctis ◽  
Silvana D'Alessio ◽  
Vincenzo Politi ◽  
...  
Keyword(s):  
Collagen I ◽  
Bovine Collagen ◽  
Neutrophil Collagenase

scholarly journals Rapid Spheroid Assays in a 3-Dimensional Cell Culture Chip

2020 ◽  
Author(s):  
Jia Lin Teh ◽  
Siti Fairus Abdul Rahman ◽  
Gregory Domnic ◽  
Lengishwarra Satiyasilan ◽  
Nelson Jeng Yeou Chear ◽  
...  
Keyword(s):  
Cell Culture ◽  
Cell Biology ◽  
Drug Sensitivity ◽  
3D Cell Culture ◽  
Collagen Matrix ◽  
High Volume ◽  
Collagen I ◽  
Bovine Collagen ◽  
High Concentrations ◽  
Drug Compound

Abstract Objective: The spheroid model provides a physiological platform to study cancer cell biology and drug sensitivity. Usage of bovine collagen I for spheroid assays is costly especially when experiments are conducted in 24-well plates, as high volume of bovine collagen I is needed. The aim of the study was to downsize spheroid assays to a microfluidic 3D cell culture chip and compare the growth, invasion and response to drug/compound of spheroids embedded in the 3D chip to spheroids embedded in 24-well plates.Results: Spheroids generated from nasopharyngeal carcinoma cell line HK-1 continuously grew and invaded into collagen matrix in a 24-well plate. Similar observations were noticed with spheroids embedded in the 3D chip. Large spheroids in both 24-well plate and the 3D chip disintegrated and invaded into the collagen matrix. Preliminary drug sensitivity assays showed that the growth and invasion of spheroids were inhibited when spheroids were treated with combination of cisplatin and paynantheine at high concentrations, in a 24-well plate. Comparable findings were obtained when spheroids were treated with the same drug combination in the 3D chip. Moving forward, spheroid assays could be performed in the 3D chip in a more high-throughput manner with minimal time and cost.

scholarly journals Characterization of the Mechanisms by which Gelatinase A, Neutrophil Collagenase, and Membrane-Type Metalloproteinase MMP-14 Recognize Collagen I and Enzymatically Process the Two α-Chains

2007 ◽  
Vol 368 (4) ◽  
pp. 1101-1113 ◽  
Author(s):  
Magda Gioia ◽  
Susanna Monaco ◽  
Giovanni Francesco Fasciglione ◽  
Anna Coletti ◽  
Andrea Modesti ◽  
...  
Keyword(s):  
Collagen I ◽  
Gelatinase A ◽  
Neutrophil Collagenase ◽  
Membrane Type

scholarly journals Rapid spheroid assays in a 3-dimensional cell culture chip

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Jia Lin Teh ◽  
Siti Fairus Abdul Rahman ◽  
Gregory Domnic ◽  
Lengishwarra Satiyasilan ◽  
Nelson Jeng Yeou Chear ◽  
...  
Keyword(s):  
Cell Culture ◽  
Cell Biology ◽  
Drug Sensitivity ◽  
3D Cell Culture ◽  
Collagen Matrix ◽  
High Volume ◽  
Collagen I ◽  
Bovine Collagen ◽  
High Concentrations ◽  
Drug Compound

Abstract Objective The spheroid model provides a physiological platform to study cancer cell biology and drug sensitivity. Usage of bovine collagen I for spheroid assays is costly especially when experiments are conducted in 24-well plates, as high volume of bovine collagen I is needed. The aim of the study was to downsize spheroid assays to a microfluidic 3D cell culture chip and compare the growth, invasion and response to drug/compound of spheroids embedded in the 3D chip to spheroids embedded in 24-well plates. Results Spheroids generated from nasopharyngeal carcinoma cell line HK-1 continuously grew and invaded into collagen matrix in a 24-well plate. Similar observations were noticed with spheroids embedded in the 3D chip. Large spheroids in both 24-well plate and the 3D chip disintegrated and invaded into the collagen matrix. Preliminary drug sensitivity assays showed that the growth and invasion of spheroids were inhibited when spheroids were treated with combination of cisplatin and paynantheine at high concentrations, in a 24-well plate. Comparable findings were obtained when spheroids were treated with the same drug combination in the 3D chip. Moving forward, spheroid assays could be performed in the 3D chip in a more high-throughput manner with minimal time and cost.

High resolution electron microscopy of lanthanum phosphate crystals

1978 ◽  
Vol 36 (1) ◽  
pp. 274-275
Author(s):  
J. C. Wheatley ◽  
J. M. Cowley
Keyword(s):  
Electron Microscopy ◽  
Catalytic Activity ◽  
High Resolution ◽  
Petroleum Industry ◽  
High Resolution Electron Microscopy ◽  
Lanthanum Phosphate ◽  
Good Catalyst ◽  
Resolution Electron ◽  
Good Catalytic Activity ◽  
Physical And Chemical

Rare-earth phosphates are of particular interest because of their catalytic properties associated with the hydrolysis of many aromatic chlorides in the petroleum industry. Lanthanum phosphates (LaPO4) which have been doped with small amounts of copper have shown increased catalytic activity (1). However the physical and chemical characteristics of the samples leading to good catalytic activity are not known.Many catalysts are amorphous and thus do not easily lend themselves to methods of investigation which would include electron microscopy. However, the LaPO4, crystals are quite suitable samples for high resolution techniques.The samples used were obtained from William L. Kehl of Gulf Research and Development Company. The electron microscopy was carried out on a JEOL JEM-100B which had been modified for high resolution microscopy (2). Standard high resolution techniques were employed. Three different sample types were observed: 669A-1-5-7 (poor catalyst), H-L-2 (good catalyst) and 27-011 (good catalyst).

The design and catalytic performance of molybdenum active sites on an MCM-41 framework for the aerobic oxidation of 5-hydroxymethylfurfural to 2,5-diformylfuran

2019 ◽  
Vol 9 (3) ◽  
pp. 811-821 ◽  
Author(s):  
Zhao-Meng Wang ◽  
Li-Juan Liu ◽  
Bo Xiang ◽  
Yue Wang ◽  
Ya-Jing Lyu ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Active Sites ◽  
Aerobic Oxidation ◽  
Catalytic Performance ◽  
Mcm 41

The catalytic activity decreases as –(SiO)3Mo(OH)(O) > –(SiO)2Mo(O)2 > –(O)4–MoO.

Prolonged Expression of Procoagulant Activity of Human Platelets Degranulated by Thrombin

1995 ◽  
Vol 74 (03) ◽  
pp. 958-961 ◽  
Author(s):  
Raelene L Kinlough-Rathbone ◽  
Dennis W Perry
Keyword(s):  
Catalytic Activity ◽  
Thrombus Formation ◽  
Annexin V ◽  
Human Platelets ◽  
Procoagulant Activity ◽  
Prothrombinase Complex ◽  
Arterial Thrombus ◽  
Flowing Blood

SummaryPlatelets are exposed to thrombin when they take part in arterial thrombus formation, and they may return to the circulation when they are freed by fibrinolysis and dislodged by flowing blood. Thrombin causes the expression of procoagulant activity on platelets, and if this activity persists, the recirculating platelets may contribute to subsequent thrombosis. We have developed techniques to degranulate human platelets by treatment with thrombin, and recover them as single, discrete platelets that aggregate in response to both weak and strong agonists. In the present study we examined the duration of procoagulant activity on the surface of thrombin-degranulated platelets by two methods: a prothrombinase assay, and the binding of 125I-labeled annexin. Control platelets generated 0.9 ± 0.4 U thrombin per 107 platelets in 15 min. Suspensions of thrombin-degranulated platelets formed 5.4 ± 0.1 U thrombin per 107 platelets in this time. Binding of 125I-annexin V was also greater with thrombin-treated platelets than with control platelets (controls: 1.7 ±0.1 ng annexin/107 platelets; thrombin-degranulated platelets: 6.8 ± 0.2 ng annexin/107 platelets). With thrombin-degranulated platelets, increased procoagulant activity and annexin binding persisted for at least 4 h after degranulation and resuspension, indicating that the catalytic activity for the prothrombinase complex is not reversed during this time. These platelets maintained their ability to aggregate for 4 h, even in response to the weak agonist, ADP. Thus, platelets that have taken part in thrombus formation and returned to the circulation may contribute to the promotion of further thrombotic events because of the persistence of procoagulant activity on their surface.

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