Musculoskeletal disorders such as lumbar disk disease are among the
most common conditions for which patients seek medical care. Although clinical
studies have provided insights into disease prevalence and clinical management,
recent research advances have yielded understanding about the molecular mechanisms
that may be involved and the genetic mutations that may contribute to a variety
of musculoskeletal and connective tissue disorders.
Members of the collagen protein family are the most abundant structural
components of the extracellular matrix of connective tissues.1
In bone, cartilage, tendon, and skin the collagens are organized into ropelike
fibrils, called heterotypic because they are composed of multiple collagen
types. Collagen types differ in length and chain composition, but all have
in common a triple-helical structure and a primary sequence composed of uninterrupted
repeats of the sequence Gly-X-Y, where gly is glycine, X is often proline,
and Y is often hydroxyproline. Type II collagen is the most abundant collagen
of cartilagenous tissues and is referred to as the major collagen. It forms
heterotypic fibrils with the successively less abundant (hence "minor") collagens,
types IX and XI. The collagenous fibrils provide the strength necessary for
tissues to resist tensile forces. In cartilage, where resistance to compressive
forces is also a major issue, the tissue also has a significant proportion
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