Biosynthesis of type II collagen. Removal of amino- and carboxy-terminal extensions from procollagen synthesized by chick embryo cartilage cells

Biochemistry ◽  
1977 ◽  
Vol 16 (15) ◽  
pp. 3421-3429 ◽  
Author(s):  
Jouni Uitto
Keyword(s):  
Chick Embryo ◽  
Type Ii Collagen ◽  
Type Ii ◽  
Cartilage Cells ◽  
Carboxy Terminal

Type II Collagen Distribution in the Ear of the Developing Chick Embryo

1989 ◽  
Vol 99 (5) ◽  
pp. 547???553 ◽  
Author(s):  
Tsukasa Ishibe ◽  
In Seong Choe ◽  
Tai June Yoo
Keyword(s):  
Chick Embryo ◽  
Type Ii Collagen ◽  
Type Ii

Retention of carboxypropeptides in type-II collagen fibrils in chick embryo chondrocyte cultures

1988 ◽  
Vol 252 (3) ◽  
pp. 619-624 ◽  
Author(s):  
Florence Ruggiero ◽  
Michael Pfäffle ◽  
Klaus von der Mark ◽  
Robert Garrone
Keyword(s):  
Chick Embryo ◽  
Type Ii Collagen ◽  
Collagen Fibrils ◽  
Type Ii ◽  
Chondrocyte Cultures

scholarly journals Catalytic properties of lysyl hydroxylase from cells synthesizing genetically different collagen types

1982 ◽  
Vol 201 (1) ◽  
pp. 215-219 ◽  
Author(s):  
U Puistola
Keyword(s):  
Chick Embryo ◽  
Type I Collagen ◽  
Type Ii Collagen ◽  
Type I ◽  
Type Ii ◽  
Collagen Types ◽  
Enzyme Preparations ◽  
Lysyl Hydroxylase ◽  
Type Iv ◽  
Sarcoma Cells

Crude preparations of lysyl hydroxylase were extracted from chick-embryo tendons synthesizing exclusively type I collagen, chick-embryo sterna synthesizing exclusively type II collagen and HT-1080 sarcoma cells synthesizing exclusively type IV collagen. No differences were found in the Km values for Fe2+, 2-oxoglutarate and ascorbate between these three enzymes preparations. Similarly no differences were found in the Km values for type I and type II protocollagens and the rate at which type IV protocollagen is hydroxylated between these enzyme preparations. The extent to which type I protocollagen could be hydroxylated by the three enzymes was likewise identical. These data strongly argue against the existence of collagen-type-specific lysyl hydroxylase isoenzymes.

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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