In vitro studies of Anti-Inflammatory agents and prostaglandin e2 effects on stimulated normal human fibroblast cultures

1994 ◽  
Vol 2 (4) ◽  
pp. 377-387 ◽  
Author(s):  
A. Lanas ◽  
P. Haggerty ◽  
B. I. Hirschowitz
1978 ◽  
Vol 173 (2) ◽  
pp. 433-439 ◽  
Author(s):  
P Willcox

1. Secretion of the lysosomal enzyme beta-N-acetylglucosaminidase (EC 3.2.1.30) by normal human fibroblast cultures was linear with respect to time up to 96h. 2. Two forms of the A isoenzyme of beta-N-acetylglucosaminidase were found in the culture medium. One form was similar to the isoenzyme found in other extracellular fluids, such as plasma and tears, the other resembled the intracellular (lysosomal) enzyme. The presence of the two isoenzymes in the culture medium appears to reflect two distinct secretory processes. 3. It is suggested that plasma acid hydrolases may be destined for incorporation into lysosomes in a manner analogous to that described for the packaging of lysosomal enzymes by fibroblasts.


2008 ◽  
Vol 319 (2) ◽  
pp. 553
Author(s):  
Leonard J. Sciorra ◽  
Aileen Grace Arriola ◽  
Binod Aryal ◽  
Bigyan Bista ◽  
Joshua M. Cipolla ◽  
...  

1979 ◽  
Vol 81 (1) ◽  
pp. 83-91 ◽  
Author(s):  
K Hedman ◽  
M Kurkinen ◽  
K Alitalo ◽  
A Vaheri ◽  
S Johansson ◽  
...  

The pericellular matrix of human fibroblast cultures was isolated, using sequential extraction with sodium deoxycholate and hypotonic buffer in the presence of protease inhibitor. The matrix attached to the growth substratum had a "sackcloth-like" structure as seen by phase contrast, immunofluorescence, and scanning electron microscopy, and it had a vaguely filamentous ultrastructure similar to that seen in intact cell layers. The matrix consisted of hyaluronic acid and heparan sulfate as the major glycosaminoglycan components and fibronectin and procollagen as major polypeptides as shown by metabolic labeling, gel electrophoresis, immunofluorescence, and collagenase digestion. This pericellular matrix can be regarded as an in vitro equivalent of the loose connective tissue matrix.


2020 ◽  
Vol 76 (7) ◽  
pp. 663-672
Author(s):  
Charmaine Arderne ◽  
Kyle Fraser Batchelor ◽  
Bhawna Uprety ◽  
Rahul Chandran ◽  
Heidi Abrahamse

The reactivity of the cobalt(III) complexes dichlorido[tris(2-aminoethyl)amine]cobalt(III) chloride, [CoCl2(tren)]Cl, and dichlorido(triethylenetetramine)cobalt(III) chloride, [CoCl2(trien)]Cl, towards different amino acids (L-proline, L-asparagine, L-histidine and L-aspartic acid) was explored in detail. This study presents the crystal structures of three amino acidate cobalt(III) complexes, namely, (L-prolinato-κ2 N,O)[tris(2-aminoethyl)amine-κ4 N,N′,N′′,N′′′]cobalt(III) diiodide monohydrate, [Co(C5H8NO2)(C6H18N4)]I2·H2O, I, (L-asparaginato-κ2 N,O)[tris(2-aminoethyl)amine-κ4 N,N′,N′′,N′′′]cobalt(III) chloride perchlorate, [Co(C4H7N2O3)(C6H18N4)](Cl)(ClO4), II, and (L-prolinato-κ2 N,O)(triethylenetetramine-κ4 N,N′,N′′,N′′′)cobalt(III) chloride perchlorate, [Co(C4H7N2O3)(C6H18N4)](Cl)(ClO4), V. The syntheses of the complexes were followed by characterization using UV–Vis spectroscopy of the reaction mixtures and the initial rates of reaction were obtained by calculating the slopes of absorbance versus time plots. The initial rates suggest a stronger reactivity and hence greater affinity of the cobalt(III) complexes towards basic amino acids. The biocompatibility of the complexes was also assessed by evaluating the cytotoxicity of the complexes on cultured normal human fibroblast cells (WS1) in vitro. The compounds were found to be nontoxic after 24 h of incubation at concentrations up to 25 mM.


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