Biomaterial Database

Myofibrillar protein and collagen breakdown in mature male rats fed protein or energy deficient diets. 1982

S Santidrián

The urinary output of N tau-methylhistidine (3-methylhistidine: 3-Mehis) and total hydroxy proline (OH-pro) were evaluated to assess the effect of a low-protein diet (low-P) or a low-energy diet (low-E), given for 21 days, on the rates of myofibrillar protein and collagen breakdown in mature male rats. As compared to the control rats, the animals fed the deficient diets showed a significant reduction in the rate of growth and plasma insulin. No major changes were found in the weight of several muscles excised from the animals at the end of the experiment. Total OH-pro was significantly reduced in the low-P rats and 3-Mehis was unchanged when results were normalized to either muscle weight or creatinine output. In conclusion, collagen breakdown was found to be very sensitive to protein depletion in the mature rat, but myofibrillar protein breakdown was not notably affected by protein or calorie malnutrition.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D008762	Methylhistidines	Histidine substituted in any position with one or more methyl groups.	Methylhistidine
D009132	Muscles	Contractile tissue that produces movement in animals.	Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009929	Organ Size	The measurement of an organ in volume, mass, or heaviness.	Organ Volume,Organ Weight,Size, Organ,Weight, Organ
D011488	Protein Deficiency	A nutritional condition produced by a deficiency of proteins in the diet, characterized by adaptive enzyme changes in the liver, increase in amino acid synthetases, and diminution of urea formation, thus conserving nitrogen and reducing its loss in the urine. Growth, immune response, repair, and production of enzymes and hormones are all impaired in severe protein deficiency. Protein deficiency may also arise in the face of adequate protein intake if the protein is of poor quality (i.e., the content of one or more amino acids is inadequate and thus becomes the limiting factor in protein utilization). (From Merck Manual, 16th ed; Harrison's Principles of Internal Medicine, 12th ed, p406)	Deficiency, Protein,Deficiencies, Protein,Protein Deficiencies
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002149	Energy Intake	Total number of calories taken in daily whether ingested or by parenteral routes.	Caloric Intake,Calorie Intake,Intake, Calorie,Intake, Energy
D003094	Collagen	A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).	Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D004044	Dietary Proteins	Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.	Proteins, Dietary,Dietary Protein,Protein, Dietary
D006909	Hydroxyproline	A hydroxylated form of the imino acid proline. A deficiency in ASCORBIC ACID can result in impaired hydroxyproline formation.	Oxyproline,4-Hydroxyproline,cis-4-Hydroxyproline,4 Hydroxyproline,cis 4 Hydroxyproline