Partial characterization of ovine skeletal muscle proteoglycans and collagen.

Ovine longissimus dorsi and biceps femoris muscles were analyzed for proteoglycan content, collagen and lysine aldehyde-derived collagen crosslinking concentrations at 2-4 days, six-month-old, and six-year-old stages of development. Tissue extracted proteoglycan molecular sieve distribution on a Sephacryl S-200HR column revealed two proteoglycan populations with estimated relative molecular weight ranges of 200,000 to 250,000 daltons and 23,000 to 70,000 daltons. The molecular sieve distribution was similar between the two muscles within a developmental age, but changed as a function of developmental age. Primary culture from both the longissimus dorsi and biceps femoris muscle liberated proteoglycans into the culture medium. In contrast to the tissue extracted proteoglycans, at the six-year-old stage of development, culture medium liberated proteoglycan Sephacryl S-200HR molecular sieve distribution differed between the two muscles. In both the tissue extracted and medium liberated proteoglycans at all developmental stages, nitrous acid deamination demonstrated the presence of heparan sulfate. Immunoblot analysis of the tissue extracted proteoglycans indicated the presence of decorin at each developmental stage. Longissimus dorsi and biceps femoris collagen concentrations (5.13 +/- 0.9 vs. 5.53 +/- 1.5%, respectively) and crosslink concentrations (0.07 +/- 0.01 moles HP/mole collagen) were initially similar between the two muscles; however, by six-months the muscles differed in both collagen concentration (1.72 +/- 0.5 and 2.53 +/- 0.7%, respectively) and crosslinking (0.24 +/- 0.02 and 0.27 +/- 0.03 moles HP/mole collagen, respectively). At six years of age, both the longissimus dorsi and biceps femoris exhibited slightly elevated collagen concentrations (2.49 and 3.05%, respectively) while crosslinking values were decreased relative to values at six-months of age (0.11 +/- 0.01 and 0.18 +/- 0.01 moles HP/mole of collagen, respectively). The results from this study indicate that skeletal muscle proteoglycans and collagen show developmental changes, which suggests that they are subject to developmental regulation.