Faculty Opinions recommendation of Developmental and osteoarthritic changes in Col6a1-knockout mice: biomechanics of type VI collagen in the cartilage pericellular matrix.

Author(s):  
Yefu Li ◽  
Lin Xu
2009 ◽  
Vol 60 (3) ◽  
pp. 771-779 ◽  
Author(s):  
Leonidas G. Alexopoulos ◽  
Inchan Youn ◽  
Paolo Bonaldo ◽  
Farshid Guilak

2007 ◽  
Vol 342-343 ◽  
pp. 133-136
Author(s):  
Jae Bong Choi

The objective of this study was to quantify the zonal difference of the in situ chondron’s Poisson effect under different magnitudes of compression. Fluorescence immunolabeling for type VI collagen was used to identify the pericellular matrix (PCM) and chondron, and a series of fluorescent confocal images were recorded and reconstructed to form quantitative three-dimensional models. The zonal variations in the mechanical response of the chondron do not appear to be due to zonal differences in PCM properties, but rather seem to result from significant inhomogeneities in relative stiffnesses of the extracellular matrix (ECM) and PCM with depth.


Cartilage ◽  
2019 ◽  
pp. 194760351987083 ◽  
Author(s):  
Hamza A. Owida ◽  
Nicola L. Kuiper ◽  
Ying Yang

Objective In native articular cartilage, chondrocytes are surrounded by a thin pericellular matrix (PCM) forming chondrons. The PCM is exclusively rich in type VI collagen. The retention of the PCM has a significant influence on the metabolic activity of the chondrocytes. Design This study investigated the influence of 2 hydrogels (hyaluronic acid [HA] and agarose) and 2 media compositions (basal and chondrogenic) on the preservation/maintenance and acceleration of PCM formation over a 21-day time course. Different combinations of chondrocytes, chondrons, and mesenchymal stem cells (MSCs) were studied. Results Both hydrogels preserved chondrons PCM from day 1 up to 21-day culture regardless of media composition. Type VI collagen immunostaining of the cultured chondrons appeared both dense and homogenous. The presence of MSCs did not influence this outcome. At day 1, type VI collagen was not present around chondrocytes alone or their co-culture with MSCs. In the HA hydrogel, type VI collagen was located within the PCM after 7 days in both mono- and co-cultures. In the agarose hydrogel, collagen VI was located within the PCM at 7 days (co-cultures) and 14 days (monocultures). In both hydrogel systems, chondrogenic media enhanced the production of key extracellular matrix components in both mono- and co-cultures in comparison to basal media (11.5% and 14% more in glycosaminoglycans and type II collagen for chondrocytes samples at day 21 culture samples, respectively). However, the media types did not enhance type VI collagen synthesis. Conclusion Altogether, a 3D chondrogenic hydrogel environment is the primary condition for maintenance and acceleration of PCM formation.


Author(s):  
Eunjung Kim ◽  
Farshid Guilak ◽  
Mansoor A. Haider

The pericellular matrix (PCM) of articular cartilage is the narrow tissue region surrounding all chondrocytes. Together, the chondrocyte and its surrounding PCM have been termed the chondron. In normal cartilage, the presence of type VI collagen is exclusive to the PCM, and the PCM is believed to play a critical role in regulating biomechanical cell-matrix interactions. Since the PCM is stiffer than the chondrocyte, it has been hypothesized to play a critical role in protecting the cell while, simultaneously, facilitating the transmission of mechanical signals to the cell. Previous studies that represent the cell, PCM and extracellular matrix (ECM) as linear biphasic materials have supported this hypothesized role for the PCM [1–4]. Previous in vitro micropipette studies of isolated chondrons [5–7] have shown that the PCM Young’s modulus ranges between 25–70kPa in middle and deep zone cartilage, separating it by an order of magnitude from both the chondrocyte stiffness (∼1kPa) and ECM stiffness (∼1MPa). In recent years, Choi et al. [8] measured changes in the three-dimensional morphology of the chondron, in situ within the ECM, under equilibrium unconfined compression of porcine cartilage explants subjected to 10–50% compressive strain (Fig. 1). Their study employed a novel 3D confocal microscopy technique, based on immunolabeling of type VI collagen, that yielded ellipsoidal approximations of undeformed and deformed chondron shapes in the superficial, middle and deep zones of the explant. In this study, an efficient computational model, based on the boundary element method (BEM), was developed and used to estimate cartilage PCM linear elastic properties based on the data reported in Choi et al. [8] for the case of middle zone cartilage under 10% compressive strain.


2012 ◽  
Vol 9 (76) ◽  
pp. 2997-3007 ◽  
Author(s):  
Rebecca E. Wilusz ◽  
Louis E. DeFrate ◽  
Farshid Guilak

The pericellular matrix (PCM) is a narrow region that is rich in type VI collagen that surrounds each chondrocyte within the extracellular matrix (ECM) of articular cartilage. Previous studies have demonstrated that the chondrocyte micromechanical environment depends on the relative properties of the chondrocyte, its PCM and the ECM. The objective of this study was to measure the influence of type VI collagen on site-specific micromechanical properties of cartilage in situ by combining atomic force microscopy stiffness mapping with immunofluorescence imaging of PCM and ECM regions in cryo-sectioned tissue samples. This method was used to test the hypotheses that PCM biomechanical properties correlate with the presence of type VI collagen and are uniform with depth from the articular surface. Control experiments verified that immunolabelling did not affect the properties of the ECM or PCM. PCM biomechanical properties correlated with the presence of type VI collagen, and matrix regions lacking type VI collagen immediately adjacent to the PCM exhibited higher elastic moduli than regions positive for type VI collagen. PCM elastic moduli were similar in all three zones. Our findings provide further support for type VI collagen in defining the chondrocyte PCM and contributing to its biological and biomechanical properties.


2015 ◽  
Vol 67 (5) ◽  
pp. 1286-1294 ◽  
Author(s):  
Nicole A. Zelenski ◽  
Holly A. Leddy ◽  
Johannah Sanchez-Adams ◽  
Jinzi Zhang ◽  
Paolo Bonaldo ◽  
...  

1993 ◽  
Vol 4 (11) ◽  
pp. 1097-1108 ◽  
Author(s):  
A Nishiyama ◽  
W B Stallcup

NG2 is a membrane-associated chondroitin sulfate proteoglycan with a core protein of 300 kD. Previously it was shown immunochemically that the core protein of NG2 can bind type VI collagen (Stallcup, W., Dahlin, K., and P. Healy. 1990. J. Cell Biol. 111:3177-3188). We have extended our studies on the interaction of NG2 and type VI collagen by transfecting cells with the full-length rat NG2 cDNA. B28 rat neural cells and U251MG human glioma cells used for transfection do not synthesize NG2. Both cell lines secrete type VI collagen into tissue culture medium but do not anchor it at the cell surface. Upon transfection of these cells with the NG2 cDNA, NG2 was correctly localized to the cell surface. Furthermore, type VI collagen could now be detected on the surface of NG2-positive cells in a pattern that coincided with that of NG2. This ability of NG2 to anchor type VI collagen to the cell surface could be abolished by incubating the cells in the presence of anti-NG2 monoclonal antibodies. These findings indicate that NG2 functions as a cell surface receptor for type VI collagen and may play a role in modulating the assembly of pericellular matrix.


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