Sg. Velleman et al., PARTIAL CHARACTERIZATION OF OVINE SKELETAL-MUSCLE PROTEOGLYCANS AND COLLAGEN, Connective tissue research, 34(3), 1996, pp. 175-190
Ovine longissimus dorsi and biceps femoris muscles were analyzed for p
roteoglycan content, collagen and lysine aldehyde-derived collagen cro
sslinking concentrations at 2-4 days, six-month-old, and six-year-old
stages of development. Tissue extracted proteoglycan molecular sieve d
istribution on a Sephacryl S-200HR column revealed two proteoglycan po
pulations with estimated relative molecular weight ranges of 200,000 t
o 250,000 daltons and 23,000 to 70,000 daltons. The molecular sieve di
stribution was similar between the two muscles within a developmental
age, but changed as a function of developmental age. Primary culture f
rom both the longissimus dorsi and biceps femoris muscle liberated pro
teoglycans into the culture medium. In contrast to the tissue extracte
d proteoglycans, at the six-year-old stage of development, culture med
ium liberated proteoglycan Sephacryl S-200HR molecular sieve distribut
ion differed between the two muscles. In both the tissue extracted and
medium liberated proteoglycans at all developmental stages, nitrous a
cid deamination demonstrated the presence of heparan sulfate. Immunobl
ot analysis of the tissue extracted proteoglycans indicated the presen
ce of decorin at each developmental stage. Longissimus dorsi and bicep
s femoris collagen concentrations (5.13 +/- 0.9 vs. 5.53 +/- 1.5%, res
pectively) and crosslink concentrations (0.07 +/- 0.01 moles HP/mole c
ollagen) were initially similar between the two muscles; however, by s
ix-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 sligh
tly elevated collagen concentrations (2.49 and 3.05%, respectively) wh
ile crosslinking values were decreased relative to values at six-month
s of age (0.11 +/- 0.01 and 0.18 +/- 0.01 moles HP/mole of collagen, r
espectively). The results from this study indicate that skeletal muscl
e proteoglycans and collagen show developmental changes, which suggest
s that they are subject to developmental regulation.