Insulin-like growth factors and binding proteins in ruminants and their nutritional regulation. 1992

M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
Department of Animal Science, Cornell University, Ithaca, NY 14853.

Insulin-like growth factors (IGF) are important mediators of growth, lactation, reproduction, and health. Considerable information on their role in ruminant animals has been learned in the past several years, but the precise mechanisms of their action are not known. The exact biological response of target cells is undoubtedly determined by the developmental state of the cell and synergism with other growth factors. Overall, somatomedins and their binding proteins seem to be major links between cellular developmental processes and nutrient supply. The mechanism by which nutrients control biological actions of somatomedins is not known but clearly involves the synthesis of IGF, as well as their binding proteins and receptors. In ruminants, severe feed restriction decreases circulating concentrations of IGF-I, whereas subtle alterations typical of those that occur in production systems have minimal effect. However, the responses of IGF to somatotropin are affected by modest alterations in nutritional status, including differences in nutritional status that are typically encountered in animal production systems.

UI MeSH Term Description Entries
D007774 Lactation The processes of milk secretion by the maternal MAMMARY GLANDS after PARTURITION. The proliferation of the mammary glandular tissue, milk synthesis, and milk expulsion or let down are regulated by the interactions of several hormones including ESTRADIOL; PROGESTERONE; PROLACTIN; and OXYTOCIN. Lactation, Prolonged,Milk Secretion,Lactations, Prolonged,Milk Secretions,Prolonged Lactation,Prolonged Lactations
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
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
D000824 Animal Nutritional Physiological Phenomena Nutritional physiology of animals. Animal Nutrition Physiology,Animal Nutritional Physiology Phenomena,Animal Nutritional Physiological Phenomenon,Animal Nutritional Physiology,Animal Nutritional Physiology Phenomenon,Veterinary Nutritional Physiology,Nutrition Physiologies, Animal,Nutrition Physiology, Animal,Nutritional Physiology, Animal,Nutritional Physiology, Veterinary,Physiology, Animal Nutrition,Physiology, Animal Nutritional,Physiology, Veterinary Nutritional
D012418 Ruminants A suborder of the order ARTIODACTYLA whose members have the distinguishing feature of a four-chambered stomach, including the capacious RUMEN. Horns or antlers are usually present, at least in males. Goats, Mountain,Ruminantia,Oreamnos americanus,Goat, Mountain,Mountain Goat,Mountain Goats,Ruminant
D013002 Somatomedins Insulin-like polypeptides made by the liver and some fibroblasts and released into the blood when stimulated by SOMATOTROPIN. They cause sulfate incorporation into collagen, RNA, and DNA synthesis, which are prerequisites to cell division and growth of the organism. Sulfation Factor,Somatomedin,Factor, Sulfation
D017451 Receptors, Somatomedin Cell surface receptors that bind somatomedins and trigger intracellular changes which influence the behavior of cells. Studies have disclosed two types of receptors for this family of peptide hormones. The type I receptor is homologous to the insulin receptor and has tyrosine kinase activity. The type II receptor is identical to the mannose-6-phosphate receptor which is important in trafficking of lysosomal enzymes. Receptors, Insulin-Like Growth Factors,Somatomedin Receptors,Insulin-Like Growth Factor Receptor,Insulin-Like Growth Factor Receptors,Somatomedin Receptor,Insulin Like Growth Factor Receptor,Insulin Like Growth Factor Receptors,Receptor, Somatomedin,Receptors, Insulin Like Growth Factors
D018969 Insulin-Like Growth Factor Binding Proteins A family of soluble proteins that bind insulin-like growth factors and modulate their biological actions at the cellular level. (Int J Gynaecol Obstet 1992;39(1):3-9) IGF Binding Protein,IGF-Binding Protein,IGF-Binding Proteins,IGFBP,Insulin-Like Growth Factor Binding Protein,Somatomedin-Binding Protein,Somatomedin-Binding Proteins,Binding Protein, IGF,IGF Binding Proteins,Insulin Like Growth Factor Binding Protein,Protein, IGF Binding,Protein, IGF-Binding,Protein, Somatomedin-Binding,Somatomedin Binding Protein,Somatomedin Binding Proteins

Related Publications

M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
July 1998, The Journal of endocrinology,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
February 1997, Endocrine journal,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
July 1990, Acta endocrinologica,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
July 1990, Physiological reviews,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
April 1994, Acta paediatrica (Oslo, Norway : 1992). Supplement,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
January 1988, Comparative biochemistry and physiology. B, Comparative biochemistry,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
January 1996, Hormone research,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
January 1995, Journees annuelles de diabetologie de l'Hotel-Dieu,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
February 1995, Endocrine reviews,
M A McGuire, and J L Vicini, and D E Bauman, and J J Veenhuizen
November 1997, European journal of endocrinology,
Copied contents to your clipboard!