N-terminal amino acid sequence of two novel tumor-derived adenylate cyclase-stimulating proteins: identification of parathyroid hormone-like and parathyroid hormone-unlike domains.
A 17,000 dalton human adenylate cyclase-stimulating protein has previously been purified from a human tumor associated with humoral hypercalcemia of malignancy. This report describes the purification of a related 7,000-9,000 MW protein from a second tumor, and provides N-terminal amino acid sequence of these two peptides. The sequences of the peptides are identical, defining the smaller peptide as an N-terminal portion of the larger peptide. The two peptides possess one region of strong homology with parathyroid hormone and a second divergent region. These structural similarities and differences may explain the similarities and differences which occur in patients with hyperparathyroidism and humoral hypercalcemia of malignancy.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000595:Amino Acid Sequence; D002294:Carcinoma, Squamous Cell / Q000032:analysis* / Q000150:complications; D004789:Enzyme Activation; D006801:Humans; D006934:Hypercalcemia / Q000209:etiology; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000302:isolation & purification*; D010281:Parathyroid Hormone / Q000032:analysis*; D010449:Peptide Mapping
D009363:Neoplasm Proteins; D010281:Parathyroid Hormone; C053371:parathyroid hormone-like adenylate cyclase-stimulating protein, human; D000262:Adenylyl Cyclases