Isolation and partial characterization of the carboxy-terminal propeptide of type II procollagen from chick embryos

Biochemistry ◽  
1984 ◽  
Vol 23 (4) ◽  
pp. 741-746 ◽  
Author(s):  
Samantha Curran ◽  
Darwin J. Prockop
Keyword(s):  
Partial Characterization ◽  
Chick Embryos ◽  
Type Ii ◽  
Carboxy Terminal

scholarly journals Partial characterization of leucocyte .ALPHA.-glucosidase in late onset glycogenosis type II.

1989 ◽  
Vol 157 (4) ◽  
pp. 355-363 ◽  
Author(s):  
TATSUO KOHRIYAMA ◽  
MASARU KURIYAMA ◽  
RYOICHI HIWATARI ◽  
MITSUHIRO OSAME ◽  
AKIHIRO IGATA
Keyword(s):  
Late Onset ◽  
Partial Characterization ◽  
Type Ii ◽  
Glycogenosis Type ◽  
Glycogenosis Type Ii ◽  
Alpha Glucosidase

scholarly journals Characterization of helical cleavages in type II collagen generated by matrixins

1998 ◽  
Vol 330 (2) ◽  
pp. 633-640 ◽  
Author(s):  
Mireille VANKEMMELBEKE ◽  
M. Philippe DEKEYSER ◽  
P. Anthony HOLLANDER ◽  
J. David BUTTLE ◽  
Jo DEMEESTER
Keyword(s):  
Cleavage Site ◽  
Articular Surface ◽  
Type Ii Collagen ◽  
Secondary Site ◽  
Type Ii ◽  
Cleavage Sites ◽  
Tissue Destruction ◽  
Carboxy Terminal

Several vertebrate collagenases have been reported to cleave type II collagen, leading to irreversible tissue destruction in osteoarthritis. We have investigated the action of MMP-1 and MMP-13 on type II collagen by use of neoepitope antibodies and N-terminal sequencing. Previous studies have suggested that the initial cleavage of type II collagen by MMP-13 is followed by a second cleavage, three amino acids carboxy-terminal to the primary cleavage site. We show here that this cleavage is also produced by APMA-activated MMP-1 in combination with MMP-3 (i.e. fully activated MMP-1). The use of a selective inhibitor of MMP-3 has shown that it is this enzyme, rather than interstitial collagenase which had been exposed to MMP-3, which makes the second cleavage. In addition we have identified, through N-terminal sequencing, a third cleavage site, three residues carboxy-terminal to the secondary site. Since MMP-2 is thought to be responsible for gelatinolytic action on type II collagen we have investigated the effect of MMP-2 after the initial helical cleavage made by either MMP-1 or MMP-13. A combination of MMPs-1, -2 and -3 results in both the second and third cleavage sites; adding MMP-2 to MMP-13 did not alter the cleavage pattern produced by MMP-13 on its own. We conclude that none of the three cleavage sites will provide information about the specific identity of the collagenolytic enzymes involved in collagen cleavage in situ. Staining of cartilage sections of osteoarthritis patients with the neoepitope antibodies revealed type II collagen degradation starting at or near the articular surface and extending into the mid and deep zones with increasing degeneration of the cartilage.

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