RESUMEN
CD38 is a type II transmembrane glycoprotein which is expressed by hematopoietic and nonhematopoietic cells in human. It has two functions of ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities and the sum of these two enzyme activities is identical with NAD glycohydrolase (NADase) activity. The levels of NADase activity in human cervical carcinoma and normal cancer tissue were measured. With a total of 12 patients with cervical cancer and 11 women with normal cervix, cancer tissues were found to have significantly higher NADase and ADP-ribosyl cyclase activities than the control group. Moreover, immunoblot analysis showed an increase of immunoreactivity against CD38 in cervical cancer tissues compared with normal tissues. Immunohistochemical data indicated that the increase of CD38 expression was due to increased infiltration of lymphocytes.
Asunto(s)
Antígenos CD , Linfocitos/patología , NAD+ Nucleosidasa/biosíntesis , Neoplasias del Cuello Uterino/enzimología , ADP-Ribosil Ciclasa , ADP-Ribosil Ciclasa 1 , Antígenos de Diferenciación/metabolismo , Femenino , Humanos , Inmunohistoquímica , Glicoproteínas de Membrana , NAD+ Nucleosidasa/metabolismo , Neoplasias del Cuello Uterino/patologíaRESUMEN
NAD glycohydrolase (NADase; EC 3.2.2.5) is an enzyme that catalyzes hydrolysis of NAD to produce ADP-ribose and nicotinamide. We recently demonstrated that self-inactivation of NADase from rabbit erythrocytes was due to an auto-ADP-ribosylation. In the present study, a mechanism of self-inactivation of NADase from Neurospora crassa by its substrate was investigated by using intact mycelia of N. crassa and purified NADase, which had molecular characteristics different from mammalian NADases. The results suggested that inactivation of NADase from N. crassa was also due to an auto-ADP-ribosylation. These findings indicate that the auto-modification of NADase is one of the universal phenomena to regulate enzyme functions.
