Biomaterial Database

Effects of pre and perinatal malnutrition on muscle fibres from fast and slow rat muscles. 1978

K F Howells, and D R Mathews, and T C Jordan

Pre and perinatal malnutrition of rats was effected by means of limiting the mothers' food intake by 50% during pregnancy and lactation. Male offspring were sacrificed at 36 weeks of age and the anterior tibialis (ANTIB) and soleus (SOL) muscles were prepared for histochemical demonstration of Type I, IIA and IIB muslce fibre types using myosin ATPase and succinic dehydrogenase activity. Muscle weights and mean muscle fibre area determinations showed greater decreases in ANTIB than SOL, SOL muscle fibre areas being relatively unaffected by the undernutrition regimen. The proportions present of the muscle fibre types differed in ANTIB and to a small extent on SOL. In the former muscle, some decreases in area in certain of the fibres were associated with increases in the percentages present, showing a tendency to maintain the physiological cross-sectional area of the muscle.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D008431	Maternal-Fetal Exchange	Exchange of substances between the maternal blood and the fetal blood at the PLACENTA via PLACENTAL CIRCULATION. The placental barrier excludes microbial or viral transmission.	Transplacental Exposure,Exchange, Maternal-Fetal,Exposure, Transplacental,Maternal Fetal Exchange
D009132	Muscles	Contractile tissue that produces movement in animals.	Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009218	Myosins	A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.	Myosin ATPase,ATPase, Actin-Activated,ATPase, Actomyosin,ATPase, Myosin,Actin-Activated ATPase,Actomyosin ATPase,Actomyosin Adenosinetriphosphatase,Adenosine Triphosphatase, Myosin,Adenosinetriphosphatase, Actomyosin,Adenosinetriphosphatase, Myosin,Myosin,Myosin Adenosinetriphosphatase,ATPase, Actin Activated,Actin Activated ATPase,Myosin Adenosine Triphosphatase
D009748	Nutrition Disorders	Disorders caused by nutritional imbalance, either overnutrition or undernutrition.	Nutritional Disorders,Nutrition Disorder,Nutritional Disorder
D009929	Organ Size	The measurement of an organ in volume, mass, or heaviness.	Organ Volume,Organ Weight,Size, Organ,Weight, Organ
D011247	Pregnancy	The status during which female mammals carry their developing young (EMBRYOS or FETUSES) in utero before birth, beginning from FERTILIZATION to BIRTH.	Gestation,Pregnancies
D005260	Female		Females
D006651	Histocytochemistry	Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.	Cytochemistry
D000251	Adenosine Triphosphatases	A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.	ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine