title: Proteoglycans and glycosaminoglycan fine structure in the mouse tail tendon fascicle.
abstract: The isolated mouse tail tendon fascicle, a functional and homogenous volume of tendon extracellular matrix, was utilized as an experimental system to examine the structure function relationships in tendon. Our previous work using this model system demonstrated relationships between mean collagen fibril diameter and fascicle mechanical properties in isolated tail tendon fascicles from three different groups of mice (3-week and 8-week control and 8-week Mov13 transgenic) K.A. Derwin, L.J. Soslowsky, J. Biomech. Eng. 121 (1999) 598-604. These groups of mice were chosen to obtain tendon tissues with varying collagen fibril structure and/or biochemistry, such that relationships with material properties could be investigated. To further investigate the molecular details of matrix composition and organization underlying tendon function, we report now on the preparation, characterization, and quantitation of fascicle PGs (proteoglycans) from these three groups. The chondroitin sulfate/dermatan sulfate (CS/DS)-substituted PGs, biglycan and decorin, which are the abundant proteoglycans of whole tendons, were also shown to be the predominant PGs in isolated fascicles. Furthermore, similar to the postnatal maturation changes in matrix composition previously reported for whole tendons, isolated fascicles from 8-week mice had lower CS/DS PG contents (both decorin and biglycan) and a higher collagen content than 3-week mice. In addition, CS/DS chains substituted on PGs from 8-week fascicles were shorter (based on a number average) and richer in disulfated disaccharide residues than chains from 3-week mice. Fascicles from 8-week Mov13 transgenic mice were found to contain similar amounts of total collagen and total CS/DS PG as age-matched controls, and CS/DS chain lengths and sulfation also appeared normal. However, both decorin and biglycan in Mov13 tissue migrated slightly faster on sodium dodecyl sulfate polyacrylamide gel electorphoresis (SDS-PAGE) than the corresponding species from 8-week control, and biglycan from the 8-week Mov 13 fascicles appeared to migrate as a more polydisperse band, suggesting the presence of a unique PG population in the transgenic tissue. These observations, together with our biomechanical data [Derwin and Soslowsky, 1999] suggest that compensatory pathways of extracellular matrix assembly and maturation may exist, and that tissue mechanical properties may not be simply determined by the contents of individual matrix components or collagen fibril size.
authors.affiliation: Orthopaedic Research Laboratories, University of Michigan, Ann Arbor, USA. derwink@bme.ri.ccf.org
authors.forename: K A
authors.initials: KA
authors.lastname: Derwin
authors.forename: L J
authors.initials: LJ
authors.lastname: Soslowsky
authors.forename: J H
authors.initials: JH
authors.lastname: Kimura
authors.forename: A H
authors.initials: AH
authors.lastname: Plaas
mesh_terms: D000818:Animals; D003094:Collagen / Q000378:metabolism; D000090602:Collagen Type I, alpha 1 Chain; D006025:Glycosaminoglycans / Q000378:metabolism* / Q000648:ultrastructure*; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D011509:Proteoglycans / Q000378:metabolism* / Q000648:ultrastructure*; D013623:Tail; D013710:Tendons / Q000378:metabolism* / Q000648:ultrastructure*
chemical_list: C000716128:Col1a1 protein, mouse; D000090602:Collagen Type I, alpha 1 Chain; D006025:Glycosaminoglycans; D011509:Proteoglycans; C013786:A73025; D003094:Collagen