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GLUT4 is the facilitated glucose transporter expressed exclusively in adipocytes and muscle cells, and is also known as the “insulin-responsive“ glucose transporter. GLUT4 translocates from an ill-defined intracellular compartment to the plasma membrane in response to insulin. The total cellular content of GLUT4 is significantly decreased in adipose cells from many patients with Type II diabetes mellitus, and animals with some types of experimental diabetes.

May act as a glucose transporter in neurons; may mediate increasd glucose uptake in response to neuronal injury. Glucose is fundamental to the metabolism of mammalian cells. Several glucose transporter protein (Glut) isoforms have been identified and shown to function in response to insulin and IGF1 induced signaling. GLUT3 is detectable in a few normal cell type spermatids in testis with active spermatogenesis, placental trophoblast membranes, and neurons in brain. GLUT3 staining is also de

Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.

Glucagon plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.

Enables 5S rRNA binding activity. Involved in several processes, including mitotic metaphase plate congression; protein localization to nucleolus; and ribosomal large subunit assembly. Located in condensed nuclear chromosome; nucleolus; and nucleoplasm. [provided by Alliance of Genome Resources, Apr 2022]

Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration. Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors. The lactotransferrin trans