Appeal No. 1997-2140
Application 08/357,820
DISCUSSION
Matrix metalloproteinases comprise a family of enzymes collectively capable of
degrading all components of extracellular matrix. Members of the family include several
collagenases, a 92 kDa gelatinase, a 72 kDa gelatinase, three stromalysins, macrophage
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metalloelastase, matrilysin, etc. The 92 kDa gelatinase consists of five structural
domains: the amino-terminal and zinc-binding catalytic domains shared by all members of
the secreted metalloproteinase gene family, the collagen binding fibronectin-like domain
shared with the 72 kDa gelatinase, a carboxyl-terminal hemopexin-like domain shared by
all matrix metalloproteinases except matrilysin, and a unique 54 amino acid proline-rich
domain homologous to the "-2 chain of type V collagen. The metalloproteinases are
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secreted as zymogens, and undergo activation extracellularly through amino-terminal
proteolytic processing. Once activated, the 92 kDa gelatinase, as its name indicates, has
the ability to degrade gelatin (denatured collagen); it also degrades insoluble elastin.
There are three other metalloproteinases with the ability to degrade insoluble elastin: the
72 kDa gelatinase, matrilysin and macrophage metalloelastase. Specification, pages 2
and 3; Goldberg, columns 1 and 2, and Figure 6.
Claim 3 is directed to cDNA encoding the zinc-binding catalytic domain of the 92
kDa gelatinase, but lacking the three fibronectin-like type II repeats normally present in the
2The 92 kDa gelatinase is also known in the art as gelatinase B, and as MMP-9;
the 72 kDa gelatinase is also known as gelatinase A, and as MMP-2.
3A zymogen is an inactive enzyme precursor, also known as a proenzyme.
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