1.56 Å structure of mature truncated human fibroblast collagenase

1994 ◽  
Vol 19 (2) ◽  
pp. 98-109 ◽  
Author(s):  
John C. Spurlino ◽  
Angela M. Smallwood ◽  
Dennis D. Carlton ◽  
Tracey M. Banks ◽  
Karen J. Vavra ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Fibroblast Collagenase

Polyclonal Antibodies Against Human Fibroblast Collagenase and the Design of an Enzyme-Linked Immunosorbent Assay to Measure TIMP-Collagenase Complex

Matrix ◽  
1992 ◽  
Vol 12 (2) ◽  
pp. 108-115 ◽  
Author(s):  
Ian M. Clark ◽  
John K. Wright ◽  
Tim E. Cawston ◽  
Brian L. Hazleman
Keyword(s):  
Immunosorbent Assay ◽  
Human Fibroblast ◽  
Polyclonal Antibodies ◽  
Enzyme Linked Immunosorbent Assay ◽  
Fibroblast Collagenase

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.

scholarly journals Fragments of human fibroblast collagenase. Purification and characterization

1989 ◽  
Vol 263 (1) ◽  
pp. 201-206 ◽  
Author(s):  
I M Clark ◽  
T E Cawston
Keyword(s):  
Active Site ◽  
Human Fibroblast ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Terminal Part ◽  
Purification And Characterization ◽  
Activity Profile ◽  
Fibroblast Collagenase ◽  
Sequencing Studies ◽  
Minor Form ◽  
Differential Binding

On purification, human fibroblast collagenase breaks down into two major forms (Mr22,000 and Mr 27,000) and one minor form (Mr 25,000). The most likely mechanism is autolysis, although the presence of contaminating enzymes cannot be excluded. From N-terminal sequencing studies, the 22,000-Mr fragment contains the active site; differential binding to concanavalin A shows the 25,000-Mr fragment is a glycosylated form of the 22,000-Mr fragment. These low-Mr forms can be separated by Zn2+-chelate chromatography. An activity profile of this column, combined with data from substrate gels, indicates no activity against collagen in the 22,000-Mr and 25,000-Mr forms, but rather, activity casein and gelatin. The 27,000-Mr form has no activity. The 22,000/25,000-Mr form can act as an activator for collagenase in a similar way to that reported for stromelysin. The activity of the 22,000/25,000-Mr form is not inhibited by the tissue inhibitor of metalloproteinases (TIMP). The 27,000-Mr C-terminal part of the collagenase molecule therefore appears to be important in maintaining the substrate-specificity of the enzyme, and also plays a role in the binding of TIMP.

The efficient expression of human fibroblast collagenase in Escherichia coli and the discovery of flavonoid inhibitors

2012 ◽  
Vol 28 (4) ◽  
pp. 741-746 ◽  
Author(s):  
Weiqiang Lu ◽  
Junsheng Zhu ◽  
Shien Zou ◽  
Xi Li ◽  
Jin Huang
Keyword(s):  
Escherichia Coli ◽  
Human Fibroblast ◽  
Fibroblast Collagenase ◽  
Efficient Expression

Effect of Tunicamycin on the Biosynthesis of Human Fibroblast Collagenase

1987 ◽  
Vol 7 (4) ◽  
pp. 285-293
Author(s):  
Chu Chang Chua ◽  
Roger L. Ladda
Keyword(s):  
Human Fibroblast ◽  
Fibroblast Collagenase

NMR Solution Structure of the Catalytic Fragment of Human Fibroblast Collagenase Complexed with a Sulfonamide Derivative of a Hydroxamic Acid Compound‡

Biochemistry ◽  
1999 ◽  
Vol 38 (22) ◽  
pp. 7085-7096 ◽  
Author(s):  
Franklin J. Moy ◽  
Pranab K. Chanda ◽  
James M. Chen ◽  
Scott Cosmi ◽  
Wade Edris ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Hydroxamic Acid ◽  
Solution Structure ◽  
Nmr Solution Structure ◽  
Sulfonamide Derivative ◽  
Fibroblast Collagenase ◽  
Catalytic Fragment ◽  
Acid Compound

scholarly journals Characterization of the Phe-81 and Val-82 Human Fibroblast Collagenase Catalytic Domain Purified fromEscherichia coli

1995 ◽  
Vol 270 (38) ◽  
pp. 22507-22513 ◽  
Author(s):  
Michael R. Gehring ◽  
Brad Condon ◽  
Stephen A. Margosiak ◽  
Chen-Chen Kan
Keyword(s):  
Human Fibroblast ◽  
Catalytic Domain ◽  
Fromescherichia Coli ◽  
Fibroblast Collagenase

scholarly journals Human fibroblast collagenase: glycosylation and tissue-specific levels of enzyme synthesis.

1986 ◽  
Vol 83 (11) ◽  
pp. 3756-3760 ◽  
Author(s):  
S. M. Wilhelm ◽  
A. Z. Eisen ◽  
M. Teter ◽  
S. D. Clark ◽  
A. Kronberger ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Enzyme Synthesis ◽  
Tissue Specific ◽  
Fibroblast Collagenase

Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor

1994 ◽  
Vol 1 (2) ◽  
pp. 106-110 ◽  
Author(s):  
N. Borkakoti ◽  
F.K. Winkler ◽  
D.H. Williams ◽  
A. D'Arcy ◽  
M.J. Broadhurst ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Catalytic Domain ◽  
Fibroblast Collagenase
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