title: Change in synthesis of sulfated glycoconjugates during muscle development, maturation and aging in embryonic to senescent CBF-1 mouse.
abstract: Previous biochemical and morphological studies have demonstrated a change in the synthetic pattern of sulfated proteoglycans during skeletal musculogenesis in the embryonic chick. These studies revealed that a transition occurs in both composition and deposition of sulfated glycoconjugates that parallels the developmental state of the tissue. The current study was undertaken to ascertain whether this transition in the embryonic chick is a conserved developmental process during musculogenesis in the mouse. Leg musculature from embryonic, newborn, juvenile, adolescent, young adult, mature adult and senescent mice, radiolabeled in vivo with [35S]sulfate, was analyzed for relative size and composition of newly synthesized sulfated macromolecules. The data reveal a transition in the synthesis of sulfated proteoglycans and glycoproteins that parallels the myogenic differentiative state of the mouse leg muscle. Embryonic mouse leg musculature synthesizes relatively large proteoglycans consisting of large chondroitin sulfate glycosaminoglycan chains. Subsequently, these major newly synthesized proteoglycans are replaced synthetically by smaller molecules composed of mixtures of dermatan sulfate, chondroitin sulfate and heparan sulfate glycosaminoglycans (newborn through 2 weeks); dermatan sulfate, heparan sulfate and chondroitin sulfate glycosaminoglycans (13 months) and heparan sulfate and dermatan sulfate glycosaminoglycans (25-26 months). The sulfated glycoproteins demonstrate a reciprocal synthetic pattern. Early in development sulfated glycoproteins form a small proportion of the newly synthesized sulfated material. With increasing developmental and maturational age, the proportion of sulfated glycoproteins increases. This continues until they become the predominant sulfated moieties synthesized by senescent mouse muscle. The results from this study thus extend observations initially made in chick to muscle development in the mouse and, therefore, suggest that the transition in synthesis of sulfated glycoconjugates is a conserved developmental process during musculogenesis.
authors.affiliation: Department of Biology, Case Western Reserve University, Cleveland, Ohio 44106.
authors.forename: H E
authors.initials: HE
authors.lastname: Young
authors.forename: D A
authors.initials: DA
authors.lastname: Carrino
authors.forename: A I
authors.initials: AI
authors.lastname: Caplan
mesh_terms: D000375:Aging / Q000378:metabolism*; D000818:Animals; D051152:Clusterin; D004622:Embryo, Mammalian / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism; D005260:Female; D006001:Glycoconjugates / Q000096:biosynthesis*; D006023:Glycoproteins / Q000096:biosynthesis; D007700:Kinetics; D051379:Mice; D008815:Mice, Inbred Strains; D018832:Molecular Chaperones; D024510:Muscle Development; D009124:Muscle Proteins / Q000096:biosynthesis; D009132:Muscles / Q000378:metabolism*; D013464:Sulfuric Acids
chemical_list: C495243:Clu protein, mouse; D051152:Clusterin; D006001:Glycoconjugates; D006023:Glycoproteins; D018832:Molecular Chaperones; D009124:Muscle Proteins; D013464:Sulfuric Acids