scholarly journals p38 mitogen-activated kinase is a bidirectional regulator of human fibroblast collagenase-1 induction by three-dimensional collagen lattices

2001 ◽  
Vol 355 (2) ◽  
pp. 437 ◽  
Author(s):  
Jiahua XU ◽  
Richard A. CLARK ◽  
William C. PARKS
Keyword(s):  
Human Fibroblast ◽  
Three Dimensional ◽  
Fibroblast Collagenase ◽  
Collagen Lattices

scholarly journals Lymphocyte locomotion and attachment on two-dimensional surfaces and in three-dimensional matrices

1982 ◽  
Vol 92 (3) ◽  
pp. 747-752 ◽  
Author(s):  
WS Haston ◽  
JM Shields ◽  
PC Wilkinson
Keyword(s):  
Three Dimensional ◽  
Two Dimensional ◽  
Collagen Gels ◽  
Peripheral Lymph Node ◽  
Cellulose Esters ◽  
Peripheral Lymph ◽  
The Matrix ◽  
Identical Material ◽  
Variable Morphology ◽  
Collagen Lattices

The adhesion and locomotion of mouse peripheral lymph node lymphocytes on 2-D protein- coated substrata and in 3-D matrices were compared. Lymphocytes did not adhere to, or migrate on, 2-D substrata suck as serum- or fibronectin-coated glass. They did attach to and migrate in hydrated 3-D collagen lattices. When the collagen was dehydrated to form a 2-D surface, lymphocyte attachment to it was reduced. We propose that lymphocytes, which are poorly adhesive, are able to attach to and migrate in 3-D matrices by a nonadhesive mechanism such as the extension and expansion of pseudopodia through gaps in the matrix, which could provide purchase for movement in the absence of discrete intermolecular adhesions. This was supported by studies using serum-coated micropore filters, since lymphocytes attached to and migrated into filters with pore sizes large enough (3 or 8 mum) to allow pseudopod penetration but did not attach to filters made of an identical material (cellulose esters) but of narrow pore size (0.22 or 0.45 mum). Cinematographic studies of lymphocyte locomotion in collagen gels were also consistent with the above hypothesis, since lymphocytes showed a more variable morphology than is typically seen on plane surfaces, with formation of many small pseudopodia expanded to give a marked constriction between the cell and the pseudopod. These extensions often remained fixed with respect to the environment as the lymphocyte moved away from or past them. This suggests that the pseudopodia were inserted into gaps in the gel matrix and acted as anchorage points for locomotion.

scholarly journals COLLAGEN SUBSTRATA FOR STUDIES ON CELL BEHAVIOR

1972 ◽  
Vol 54 (3) ◽  
pp. 626-637 ◽  
Author(s):  
Tom Elsdale ◽  
Jonathan Bard
Keyword(s):  
Soft Tissue ◽  
Simple Technique ◽  
Three Dimensional ◽  
Capillary Forces ◽  
Cell Behavior ◽  
Malignant Cells ◽  
Behavioral Studies ◽  
Human Diploid Cells ◽  
Diploid Cells ◽  
Collagen Lattices

A simple technique is described for the preparation of collagen substrata containing 0 1% of collagen by weight, in the form of native bundles with a 640 A period, the substrata are similar in these respects to soft-tissue matrices These substrate are hydrated collagen lattices (HCLs) in which the watery milieu is held within a fibrous collagen net mainly by capillary forces. HCLs have been characterized in terms of the course of collagen precipitation and aggregation, ultrastructure, and their stability under various conditions. The ways in which HCLs can be employed as both two- and three-dimensional substrata in cell behavioral studies are illustrated with some preliminary observations on the form, motility, adhesion, and growth of human diploid cells and two lines of malignant cells.

scholarly journals Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain

1993 ◽  
Vol 295 (1) ◽  
pp. 273-276 ◽  
Author(s):  
A J Fosang ◽  
K Last ◽  
V Knäuper ◽  
P J Neame ◽  
G Murphy ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Catalytic Domain ◽  
Polymorphonuclear Leucocyte ◽  
Gelatinase A ◽  
Cleavage Sites ◽  
Similar Extent ◽  
Human Sequence ◽  
Fibroblast Collagenase ◽  
Gelatinases A And B

The actions of recombinant human fibroblast collagenase (MMP1), purified polymorphonuclear leucocyte collagenase (MMP8) and their N-terminal catalytic domain fragments against cartilage aggrecan and an aggrecan G1-G2 fragment have been investigated in vitro. After activation with recombinant human stromelysin and typsin, both collagenases were able to degrade human and porcine aggrecans to a similar extent. An N-terminal G1-G2 fragment (150 kDa) was used to identify specific cleavage sites occurring within the proteinase-sensitive interglobular domain between G1 and G2. Two specific sites were found; one at an Asn341-Phe342 bond and another at Asp441-Leu442 (human sequence). This specificity of the collagenases for aggrecan G1-G2 was identical with that of the truncated metalloproteinase matrilysin (MMP7), but different from those of stromelysin (MMP3) and the gelatinases (MMP2 or gelatinase A; MMP9 or gelatinase B) which cleave at the Asn-Phe site, but not the Asp-Leu site. In addition, collagenase catalytic fragments lacking C-terminal hemopexin-like domains were tested and shown to exhibit the same specificities for the G1-G2 fragment as the full-length enzymes. Thus the specificity of the collagenases for cartilage aggrecan was not influenced by the presence or absence of the C-terminal domain. Together with our previous findings, the results show that stromelysin-1, matrilysin, gelatinases A and B and fibroblast and neutrophil collagenases cleave at a common, preferred site in the aggrecan interglobular domain, and additionally that both fibroblast and neutrophil collagenases cleave at a second site in the interglobular domain that is not available to stromelysin or gelatinases.

Sign in / Sign up

Export Citation Format

Share Document