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
2005 ◽  
Vol 2005 (4) ◽  
pp. 364-373 ◽  
Author(s):  
Vega Villar-Suárez ◽  
B. Colaço ◽  
I. Calles-Venal ◽  
I. G. Bravo ◽  
J. G. Fernández-Álvarez ◽  
...  

Isolated chondrocytes dedifferentiate to a fibroblast-like shape on plastic substrata and proliferate extensively, but rarely form nodules. However, when dissociation is not complete and some cartilage remnants are included in the culture, proliferation decreases and cells grow in a reticular pattern with numerous nodules, which occasionally form small cartilage-like fragments. In an attempt to reproduce this stable chondrogenic state, we added a cartilage protein extract, a sugar extract, and hyaluronan to the medium of previously dedifferentiated chondrocytes. When protein extract was added, many cartilaginous nodules appeared. Hyaluronan produced changes in cell phenotype and behaviour, but not nodule formation. Protein extract has positive effects on the differentiation of previously proliferated chondrocytes and permits nodule formation and the extensive production of type-II collagen. A comparison with incompletely dissociated chondrocyte cultures suggests that the presence of some living cells anchored to their natural extracellular matrix provides some important additional factors for the phenotypical stability of chondrocytes on plastic surfaces. In order to elucidate if it is possible that the incidence of apoptosis is related to the results, we also characterized the molecular traits of apoptosis.


2019 ◽  
Vol 34 (4-5) ◽  
pp. 373-385
Author(s):  
Kuan Wei Lee ◽  
Tang-Ching Kuan ◽  
Ming Wei Lee ◽  
Chen Show Yang ◽  
Lain-Chyr Hwang ◽  
...  

Extracellular matrix has an important part of the role in tissue engineering and regenerative medicine, so it is necessary to understand the various interactions between cells and extracellular matrix. Type II collagen and hyaluronic acid are the major structural components of the extracellular matrix of articular cartilage, and they are involved in fibril formation, entanglement and binding. The aim of this study was to prepare type II collagen fibrils with surface grafted with hyaluronic acid modified at the reducing end. The topographic pattern of type II collagen fibrils showed a significant change after the surface coupling of hyaluronic acid according to atomic force microscopy scanning. The presence of hyaluronic acid on the type II collagen fibrillar surface was confirmed by the specific binding of nanogold labelled with lectin. No significant increase in cell proliferation was detected by a WST-1 assay. According to histochemical examination, the maintenance of the round shape of chondrocytes and increased glycosaminoglycan secretion revealed that these cell pellets with Col II- g-hyaluronic acid molecules contained un-dedifferentiated chondrocytes in vitro. In the mixture with the 220-kDa Col II- g-hyaluronic acid copolymer, the expression of type II collagen and aggrecan genes in chondrocytes increased as demonstrated by real-time polymerase chain reaction analysis. Experimental results show that the amount of hyaluronic acid added during culturing of chondrocytes can maintain the functionality of chondrocytes and thus allow for increased cell proliferation that is suitable for tissue repair of human cartilage.


1989 ◽  
Vol 99 (5) ◽  
pp. 547???553 ◽  
Author(s):  
Tsukasa Ishibe ◽  
In Seong Choe ◽  
Tai June Yoo

1982 ◽  
Vol 201 (1) ◽  
pp. 215-219 ◽  
Author(s):  
U Puistola

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.


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