scholarly journals Inhibition of Human Scleral Fibroblast Cell Attachment to Collagen Type I by TGFBIp

2009 ◽  
Vol 50 (8) ◽  
pp. 3542 ◽  
Author(s):  
Lilian Shelton ◽  
Jody A. Summers Rada
1987 ◽  
Vol 66 (9) ◽  
pp. 1449-1455 ◽  
Author(s):  
S. Pitaru ◽  
M. Soldinger ◽  
D. Madgar ◽  
Z. Metzger

The purpose of this study was to assess the effect of endotoxin adsorbed to dental surfaces and to collagen type I on the migration, attachment, and orientation of human gingival fibroblasts (HGF). Transversely cut porcine tooth root slices (RS), 200 μm thick, were prepared. Half of the RS obtained were partially demineralized in EDTA. Half of the demineralized and non-demineralized RS were incubated with 400 μg/mL of endotoxin for 24 hr, whereas the other half were maintained in PBS and served as controls. Experimental and control RS were placed on confluent layers of HFG and cultured for six days. Cell migration toward and cell attachment to the periphery of the RS and the formation of oriented cell sheets were assessed by means of photographic techniques. Additionally, six-day-old cultures were fixed and processed for SEM observation. In separate experiments, the effect of endotoxin on cell attachment to collagen type I and on contraction of three-dimensional collagen gels was assessed. It was found that: (i) bacterial endotoxin inhibited migration and attachment of HGF to both demineralized and non-demineralized cementum and interfered with the development of oriented cellular structure ; (ii) the inhibitory effect was significantly more pronounced for non-demineralized than for demineralized cementum; (iii) the morphology of HGF attached to endotoxin-treated dental surfaces was altered compared with that of their controls; and (iv) bacterial endotoxin inhibited cell attachment to collagen type I and delayed the contraction of collagen gel.


2014 ◽  
Vol 2 (9) ◽  
pp. 1222-1229 ◽  
Author(s):  
Ricardo M. Gouveia ◽  
Roanne R. Jones ◽  
Ian W. Hamley ◽  
Che J. Connon

Collagen type-I gels incorporating self-assembled Fmoc-RGDS during polymerisation become functionalised, providing a scaffold for enhanced cell attachment and survival, and with improved mechanical and structural properties.


2008 ◽  
Vol 396-398 ◽  
pp. 41-45
Author(s):  
D.W. Lee ◽  
E.J. Lee ◽  
Sung Su Chun ◽  
Myun Whan Ahn ◽  
I.W. Song ◽  
...  

A collagen material was chemically grafted on hydroxyapatite (HA) to enhance bone cell attachment because the collagen is a major constituent of connective tissues and has been regarded as one of the most excellent coating materials for bone bonding. First, HA disks were prepared with 12mm diameter and 1mm thickness. And then collagen (type I) was immobilbized on the HA surface using a 3-APTES coupling agent on HA disk surfaces. MC3T3-E1 osteoblasts were seeded on the collagen-grafted and non-grated HA disks and cultured for 4 hrs to evaluate the cell adhesion on the HA discs. The Attached cell morphology on discs was observed with a fluorescent optical microscopy (FOM) and a scanning electron microscopy (SEM). The osteoblasts on the collagen-grafted sample were more spread than those on the non-grafted sample. It is believed that collagen-grafted HA surface provides suitable sites for cell attaching due to the high biocompatibility of collagen.


Langmuir ◽  
2014 ◽  
Vol 30 (31) ◽  
pp. 9477-9483 ◽  
Author(s):  
Helena P. Felgueiras ◽  
Sven D. Sommerfeld ◽  
N. Sanjeeva Murthy ◽  
Joachim Kohn ◽  
Véronique Migonney

1991 ◽  
Vol 274 (2) ◽  
pp. 615-617 ◽  
Author(s):  
P Kern ◽  
M Menasche ◽  
L Robert

The biosynthesis of type I, type V and type VI collagens was studied by incubation of calf corneas in vitro with [3H]proline as a marker. Pepsin-solubilized collagen types were isolated by salt fractionation and quantified by SDS/PAGE. Expressed as proportions of the total hydroxyproline solubilized, corneal stroma comprised 75% type I, 8% type V and 17% type VI collagen. The rates of [3H]proline incorporation, linear up to 24 h for each collagen type, were highest for type VI collagen and lowest for type I collagen. From pulse-chase experiments, the calculated apparent half-lives for types I, V and VI collagens were 36 h, 10 h and 6 h respectively.


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