scholarly journals Cell migration through three-dimensional gels of native collagen fibres: collagenolytic activity is not required for the migration of two permanent cell lines

1980 ◽  
Vol 46 (1) ◽  
pp. 171-186 ◽  
Author(s):  
S.L. Schor ◽  
T.D. Allen ◽  
C.J. Harrison

Three dimensional gels of native type I collagen fibres have been used as a substratum for the growth and migration of Chinese hamster ovary cells (fibroblastoid cell line) and RPMI-3460 melanoma cells (tumorigenic cell line from Syrian hamster). Quantitative data concerning the migration of these cells from the gel surface into the 3-dimensional collagen gel matrix have been obtained. The migration of both cell types into the collagen gel matrix is not accompanied by the degradation of collagen fibres. The possible implications of these observations for tumour cell invasion in vivo are discussed.

1981 ◽  
Vol 49 (1) ◽  
pp. 299-310 ◽  
Author(s):  
S.L. Schor ◽  
A.M. Schor ◽  
G.W. Bazill

Data are presented indicating that the adhesion of Chinese hamster ovary cells (CHO) to films of denatured type I collagen occurs by a fibronectin-dependent mechanism, whereas the adhesion of these cells to 3-dimensional gels of native type I collagen fibres may occur by either a rapid, fibronectin-dependent mechanism or by a slower, fibronectin-independent mechanism, whereas the adhesion of these cells to 3-dimensional gels of native type I collagen fibres may occur by either a rapid, fibronectin-dependent mechanism or by a slower, fibronectin-independent mechanism. Data are also presented indicating that fibronectin promotes the migration of CHO cells on native type I collagen fibres.


Author(s):  
Lowell T. Edgar ◽  
Steve A. Maas ◽  
James E. Guilkey ◽  
Jeffrey A. Weiss

Recent developments in tissue engineering have created demand for the ability to create microvascular networks with specific topologies in vitro. During angiogenesis, sprouting endothelial cells apply traction forces and migrate along components of the extracellular matrix (ECM), resulting in neovessel elongation [1]. The fibrillar structure of the ECM serves as the major pathway for mechanotransduction between contact-dependent cells. Using a three-dimensional (3D) organ culture model of microvessel fragments within a type-I collagen gel, we have shown that subjecting the culture to different boundary conditions during angiogenesis can lead to drastically different vascular topologies [2]. Fragments cultured in a rectangular gel that were free to contract grew into a randomly oriented network [3, 4]. When the long-axis of the gel was constrained as to prevent contraction, microvessels and collagen fibers were found aligned along the constrained axis (Fig. 1) [4].


2004 ◽  
Vol 167 (4) ◽  
pp. 757-767 ◽  
Author(s):  
Tae-Hwa Chun ◽  
Farideh Sabeh ◽  
Ichiro Ota ◽  
Hedwig Murphy ◽  
Kevin T. McDonagh ◽  
...  

During angiogenesis, endothelial cells initiate a tissue-invasive program within an interstitial matrix comprised largely of type I collagen. Extracellular matrix–degradative enzymes, including the matrix metalloproteinases (MMPs) MMP-2 and MMP-9, are thought to play key roles in angiogenesis by binding to docking sites on the cell surface after activation by plasmin- and/or membrane-type (MT) 1-MMP–dependent processes. To identify proteinases critical to neovessel formation, an ex vivo model of angiogenesis has been established wherein tissue explants from gene-targeted mice are embedded within a three-dimensional, type I collagen matrix. Unexpectedly, neither MMP-2, MMP-9, their cognate cell-surface receptors (i.e., β3 integrin and CD44), nor plasminogen are essential for collagenolytic activity, endothelial cell invasion, or neovessel formation. Instead, the membrane-anchored MMP, MT1-MMP, confers endothelial cells with the ability to express invasive and tubulogenic activity in a collagen-rich milieu, in vitro or in vivo, where it plays an indispensable role in driving neovessel formation.


2008 ◽  
Vol 133 (2) ◽  
pp. 245-252 ◽  
Author(s):  
Yuji Hirano ◽  
Naoki Ishiguro ◽  
Masahiro Sokabe ◽  
Masaharu Takigawa ◽  
Keiji Naruse

Biomaterials ◽  
2006 ◽  
Vol 27 (1) ◽  
pp. 79-90 ◽  
Author(s):  
Laurent Galois ◽  
Sandrine Hutasse ◽  
Delphine Cortial ◽  
Cécile F. Rousseau ◽  
Laurent Grossin ◽  
...  

2010 ◽  
Vol 47 (2) ◽  
pp. 114-124 ◽  
Author(s):  
Shinsaku Togo ◽  
Tadashi Sato ◽  
Hisatoshi Sugiura ◽  
Xingqi Wang ◽  
Hesham Basma ◽  
...  

2000 ◽  
Vol 278 (5) ◽  
pp. L1032-L1038 ◽  
Author(s):  
X. D. Liu ◽  
C. M. Skold ◽  
T. Umino ◽  
J. R. Spurzem ◽  
D. J. Romberger ◽  
...  

Nitric oxide (NO) relaxes vascular smooth muscle in part through an accumulation of cGMP in the target cells. We hypothesized that a similar effect may also exist on collagen gel contraction mediated by human fetal lung (HFL1) fibroblasts, a model of wound contraction. To evaluate this, HFL1 cells were cultured in three-dimensional type I collagen gels and floated in serum-free DMEM with and without various NO donors. Gel size was measured with an image analyzer. Sodium nitroprusside (SNP, 100 μM) significantly augmented collagen gel contraction by HFL1 cells (78.5 ± 0.8 vs. 58.3 ± 2.1, P < 0.01), whereas S-nitroso- N-acetylpenicillamine, 5-amino-3-(4-morpholinyl)-1,2,3-oxadiazolium chloride, NONOate, and N G-monomethyl-l-arginine did not affect the contraction. Sodium ferricyanide, sodium nitrate, or sodium nitrite was not active. The augmentory effect of SNP could not be blocked by 1 H-[1,2,4]-oxadiazolo-[4,3- a]-quinoxalin-1-one, whereas it was partially reversed by 8-(4-chlorophenylthio) (CPT)-cGMP. To further explore the mechanisms by which SNP acted, fibronectin and PGE2 production were measured by immunoassay after 2 days of gel contraction. SNP inhibited PGE2 production and increased fibronectin production by HFL1 cells in a concentration-dependent manner. CPT-cGMP had opposite effects on fibronectin and PGE2 production. Addition of exogenous PGE2 blocked SNP-augmented contraction and fibronectin production by HFL1 cells. Therefore, SNP was able to augment human lung fibroblast-mediated collagen gel contraction, an effect that appears to be independent of NO production and not mediated through cGMP. Decreased PGE2 production and augmented fibronectin production may have a role in this effect. These data suggest that human lung fibroblasts in three-dimensional type I collagen gels respond distinctly to SNP by mechanisms unrelated to the NO-cGMP pathway.


2007 ◽  
Vol 361-363 ◽  
pp. 943-946
Author(s):  
S. Motojima ◽  
N. Igeta ◽  
Michiyo Honda ◽  
Nobuyuki Kanzawa ◽  
Mamoru Aizawa

We have successfully fabricated apatite-fiber scaffolds (AFSs) that enable three-dimensional cell culture. The AFSs possessing large pores of 100~250 μm and micro pores of about 5 μm were fabricated by firing the green compacts consisting of the single-crystal apatite fibers and the carbon beads with a size of 150 μm. In order to enhance the mechanical properties of the AFSs, we have improved the process of AFS fabrication: Collagen gel (type I) solutions were introduced into the pores in the scaffolds; in addition, the resulting apatite/collagen scaffolds were chemically modified by thermally dehydrated cross-linking. Actually, the results of compressive strength tests show that the value of the AFS with chemically cross-linked I-collagen was about twice as high as that of the conventional AFS without I-collagen. We conclude that combination of I-collagen and thermal dehydrated cross-linking is effective for enhancement of the mechanical properties of AFSs.


1987 ◽  
Vol 7 (2) ◽  
pp. 569-577 ◽  
Author(s):  
J E Looney ◽  
J L Hamlin

We isolated overlapping recombinant cosmids that represent the equivalent of two complete dihydrofolate reductase amplicon types from the methotrexate-resistant CHO cell line CHOC400. The type I amplicons are 260 kilobases long, are arranged in head-to-tail fashion, and represent 10 to 15% of the amplicons in the CHOC400 genome. The type II amplicons are 220 kilobases long, are arranged in head-to-head and tail-to-tail configurations, and constituted the majority of the remaining amplicons in CHOC400 cells. The type II amplicon sequences are represented entirely within the type I unit. These are the first complete amplicons to be cloned from a mammalian cell line.


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