Elevated activity of semicarbazide-sensitive amine oxidase in blood from patients with skeletal metastases of prostate cancer

• Published in: Clinical science (1979) Vol. 97; no. 1; pp. 111 - 115
• Main Authors: EKBLOM, J, GRÖNVALL, J, LENNERNÄST, B, NILSSON, S, GARPENSTRAND, H, ORELAND, L
• Format: Conference Proceeding Journal Article
• Language: English
• Published: London Portland Press 01.07.1999
• Subjects: Aged; Amine Oxidase (Copper-Containing); Amine Oxidase (Copper-Containing) - blood; Animals; Autoradiography; Biological and medical sciences; blood; Bone Neoplasms; Bone Neoplasms - blood; Bone Neoplasms - enzymology; Bone Neoplasms - secondary; Cancer and Oncology; Cancer och onkologi; Diseases of the osteoarticular system; enzymology; Fractures; Fractures, Spontaneous - blood; Fractures, Spontaneous - enzymology; Humans; Male; Medical sciences; metabolism; Mice; Neoplasm Proteins; Neoplasm Proteins - blood; pathology; Prostatic Neoplasms; Prostatic Neoplasms - enzymology; Prostatic Neoplasms - pathology; secondary; Semicarbazides; Semicarbazides - metabolism; Spontaneous; Tumors of striated muscle and skeleton; Urinary system disease; Prostate disease; Pathophysiology; Rodentia; Diseases of the osteoarticular system; Male; Bone disease; Metastasis; Malignant tumor; Vertebrata; Mammalia; Semicarbazide-sensitive amine oxydase; Mouse; Animal; Complication; Skeleton; Male genital diseases; Prostate
• ISSN: 0143-5221; 1470-8736
• DOI: 10.1042/CS19990017

The semicarbazide-sensitive amine oxidases constitute a group of copper-containing enzymes whose physiological function is unclear. The enzymes are present in various tissues, including blood plasma. At present, the source of the plasma enzyme in humans is not known. Results of a recent study suggested that semicarbazide-sensitive amine oxidase is expressed in the skeleton, e.g. in the spine. Using an indirect autoradiographic method in mice, we provide evidence that semicarbazide-sensitive amine oxidase is present in high abundance in bone tissue. Specific activities of semicarbazide-sensitive amine oxidase were estimated in blood samples from subjects with femoral bone fractures. Moreover, enzyme activities were also measured in patients suffering from prostate cancer with skeletal metastases. The level of specific semicarbazide-sensitive amine oxidase activity in serum was significantly elevated in patients with skeletal metastases compared with both healthy controls and patients having prostate cancer without signs of skeletal metastases. Based on the results of the present study, we propose that semicarbazide-sensitive amine oxidase in blood plasma may originate, at least in part, from the skeleton.