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Cartilage Volume

The intake of antioxidant food sources by these individuals was estimated from a food frequency questionnaire at baseline. In 10 years later after that, their cartilage volume, bone area, cartilage defects and bone marrow lesions were assessed approximately using magnetic resonance imaging (MRI). [Pg.24]

Fibrillation, loss of volume, and degradation of articular cartilage... [Pg.880]

Copper is an essential component of numerous key metalloenzymes which are critical in melanin formation, myelin formation and crosslinking of collagen and elastin. Copper plays a vital role in hemopoiesis, maintenance of vascular and skeletal integrity, and structure and function of the nervous system. Thus a deficiency of copper can lead to a variety of adverse effects such as increased fragility in bones, aneurysm formation in arteries and a loss of lysyl oxidase activity in cartilage.54 57 Articles on copper also appear in Siget1, volumes 3 and 5, all of volumes 12 and 13, and volume 14,... [Pg.766]

Punched discs of similar size standardize the sur-face/volume ratio, and give more reproducible results than chips of cartilage obtained by scalpel dissection. A disadvantage is the greater amount of cartilage needed, which makes it unsuitable for human tissue obtained from joint replacement surgery. [Pg.246]

The large volume occupied by high molecular size HA chains, including the aqueous solvent volume underlies the ability to distend and maintain extracellular spaces and tissue hydration. In fact, the moisture of skin is attributed to the rich HA content of the dermal compartment. For example, HA is present in significant amounts in hyaline cartilages, enough to fill the tissue volume in the absence of other constituents. Therefore, HA has been assigned various roles in the homeostasis of the extracellular space [17]. [Pg.800]

Schematic representation of cartilage proteoglycan. The monomers, consisting of glycosaminoglycan chains linked to a core protein by covalent linkage, extend laterally at intervals from opposite sides of a very long filament of hyaluronate. The interaction between the core protein and hyaluronate is noncovalent and is aided by the link protein. The entire structure is highly hydrated and occupies a large volume. [Reproduced with permission from W. J. Lennarz, The Biochemistry of Glycoproteins and Proteoglycans, Plenum Press, New York, 1980]. Schematic representation of cartilage proteoglycan. The monomers, consisting of glycosaminoglycan chains linked to a core protein by covalent linkage, extend laterally at intervals from opposite sides of a very long filament of hyaluronate. The interaction between the core protein and hyaluronate is noncovalent and is aided by the link protein. The entire structure is highly hydrated and occupies a large volume. [Reproduced with permission from W. J. Lennarz, The Biochemistry of Glycoproteins and Proteoglycans, Plenum Press, New York, 1980].

See other pages where Cartilage Volume is mentioned: [Pg.36]    [Pg.1688]    [Pg.121]    [Pg.340]    [Pg.341]    [Pg.24]    [Pg.150]    [Pg.36]    [Pg.1688]    [Pg.121]    [Pg.340]    [Pg.341]    [Pg.24]    [Pg.150]    [Pg.179]    [Pg.41]    [Pg.205]    [Pg.219]    [Pg.456]    [Pg.350]    [Pg.283]    [Pg.272]    [Pg.174]    [Pg.170]    [Pg.398]    [Pg.53]    [Pg.121]    [Pg.187]    [Pg.156]    [Pg.237]    [Pg.323]    [Pg.249]    [Pg.129]    [Pg.174]    [Pg.699]    [Pg.699]    [Pg.156]    [Pg.422]    [Pg.3120]    [Pg.36]    [Pg.588]    [Pg.185]    [Pg.285]    [Pg.17]    [Pg.156]    [Pg.227]    [Pg.106]    [Pg.192]    [Pg.322]    [Pg.425]   
See also in sourсe #XX -- [ Pg.340 ]




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