Biomaterial Database

Postnatal development and differentiation of myofibres in functionally diverse porcine skeletal muscles. 1997

A P Harrison, and R Latorre, and M J Dauncey

Department of Cellular Physiology, The Babraham Institute, Cambridge, England.

Marked changes in muscle function occur after birth, with the response being dependent on developmental stage. Therefore, postnatal cellular ontogeny of functionally distinct skeletal muscles was investigated in the pig, a large mammal born at a relatively advanced stage of development. Assessment of myofibre contractile (type I slow/type II fast) and metabolic (oxidative/glycolytic) properties at Days 0, 2, 5 and 14 revealed type-specific differences in hypertrophy and differentiation. Type I fibre proportions increased significantly in soleus and diaphragm, especially between Days 0 and 5, and rhomboideus showed a similar trend, but in longissimus there was a slight decrease during Days 0-2. Cytochrome oxidase activity was relatively high and similar among myofibres in all muscles at birth, and fibres with low activity were not detected until Day 5. In contrast with previous reports, glycolytic fibres were present in all muscles at birth; postnatal changes in alpha-glycerophosphate dehydrogenase activity were both muscle- and myofibre-specific. Hence, although myosin ATPase activity and metabolic properties of porcine myofibres are well developed at birth, they continue to mature postnatally. This suggests that postnatal muscle development can be modulated by extrinsic factors, even in mammals born at a relatively advanced stage of development.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D009119	Muscle Contraction	A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.	Inotropism,Muscular Contraction,Contraction, Muscle,Contraction, Muscular,Contractions, Muscle,Contractions, Muscular,Inotropisms,Muscle Contractions,Muscular Contractions
D010084	Oxidation-Reduction	A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).	Redox,Oxidation Reduction
D002454	Cell Differentiation	Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.	Differentiation, Cell,Cell Differentiations,Differentiations, Cell
D003576	Electron Transport Complex IV	A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.	Cytochrome Oxidase,Cytochrome aa3,Cytochrome-c Oxidase,Cytochrome Oxidase Subunit III,Cytochrome a,a3,Cytochrome c Oxidase Subunit VIa,Cytochrome-c Oxidase (Complex IV),Cytochrome-c Oxidase Subunit III,Cytochrome-c Oxidase Subunit IV,Ferrocytochrome c Oxygen Oxidoreductase,Heme aa3 Cytochrome Oxidase,Pre-CTOX p25,Signal Peptide p25-Subunit IV Cytochrome Oxidase,Subunit III, Cytochrome Oxidase,p25 Presequence Peptide-Cytochrome Oxidase,Cytochrome c Oxidase,Cytochrome c Oxidase Subunit III,Cytochrome c Oxidase Subunit IV,Oxidase, Cytochrome,Oxidase, Cytochrome-c,Signal Peptide p25 Subunit IV Cytochrome Oxidase,p25 Presequence Peptide Cytochrome Oxidase
D005993	Glycerolphosphate Dehydrogenase		Alpha-Glycerophosphate Dehydrogenase,Glycerol-3-Phosphate Dehydrogenase,Glycerophosphate Dehydrogenase,Glycerophosphate Oxidase,Alpha Glycerophosphate Dehydrogenase,Dehydrogenase, Alpha-Glycerophosphate,Dehydrogenase, Glycerol-3-Phosphate,Dehydrogenase, Glycerolphosphate,Dehydrogenase, Glycerophosphate,Glycerol 3 Phosphate Dehydrogenase,Oxidase, Glycerophosphate
D006019	Glycolysis	A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.	Embden-Meyerhof Pathway,Embden-Meyerhof-Parnas Pathway,Embden Meyerhof Parnas Pathway,Embden Meyerhof Pathway,Embden-Meyerhof Pathways,Pathway, Embden-Meyerhof,Pathway, Embden-Meyerhof-Parnas,Pathways, Embden-Meyerhof
D000375	Aging	The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.	Senescence,Aging, Biological,Biological Aging
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013552	Swine	Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).	Phacochoerus,Pigs,Suidae,Warthogs,Wart Hogs,Hog, Wart,Hogs, Wart,Wart Hog