Acid phosphatase activity in gerbil prostate: comparative study in male and female during postnatal development Ana Maria Galvan Custo´dio a , Rejane Maira Go´es b , Sebastia˜o Roberto Taboga b, ) a Department of Cell Biology, UNICAMP, Campinas, SP., PO Box 6109, 13084-971 Brazil b Laborato ´rio de Microscopia e Microana ´lise, Departamento de Biologia, IBILCE/UNESP, Rua Cristo ´va ˜o Colombo, 2265, Jardim Nazareth 15054-000, Sa ˜o Jose ´ do Rio Preto, SP., Brazil Received 24 February 2003; revised 4 December 2003; accepted 8 December 2003 Abstract The prostate is present in both male and female mammals. It is composed of secretory epithelium, connective stroma, smooth muscle and neuroendocrine cells, which are under hormonal regulation. Acid phosphatases catalyze the hydrolysis of orthophosphate monoesters. We have compared the expression of acid phosphatases in gerbil (Meriones unguiculatus) prostate glands in both sexes using young, adult and old animals. Eighteen prostates were isolated, frozen, sectioned, fixed, incubated with sodium b-glycerophosphate sodium, washed with acetate buffer solution, treated with ammonium sulfide and counterstained with Methyl-Green aqueous solution. Ultracytochemical analyses were also conducted. This substrate revealed total acid phosphatase activity. The expression of the enzyme was heterogeneous, occurring in all ages during postnatal development. The data revealed that the female prostate matured before the male prostate. In addition, acid phosphatase activity in both sexes was regulated by androgen variation concomitant with development. Ó 2004 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved. Keywords: Female prostate; Male prostate; Gerbil; Enzyme cytochemistry; Acid phosphatase 1. Introduction Acid phosphatases (AP) are ubiquitous enzymes, which catalyze the hydrolysis of orthophosphate mono- esters under acid conditions. Despite a common func- tional identity, these hydrolases can be differentiated according to structural, catalytic and immunological properties, tissue distribution and subcellular location (Suter et al., 2001). They are also differentiated in respect of chromosomal origin, molecular weight, amino acid homology and sequence length and resistance to L (C) tartrate and to fluoride (Bull et al., 2001). According to Bull et al. (2001) five important classes of APs are found in humans: prostatic (PAP); lysosomal (LAP); erythrocytic (EAP); macrophage (MAP) and osteoclastic (OcAP). These classes were detected in erythrocytes, leukocytes, platelets, liver, spleen, kidney, bones and other tissues (Bull et al., 2001; Cerri et al., 1999; Safting et al., 1997). Large amounts of AP are produced by the acinar epithelium cells of normal pro- state and are found in the lysosomes and secretory vacuoles (Ellis and Brawer, 1994). Furthermore, an over or under expression of APs has been verified in several pathological conditions such as prostatic, renal, bone and hepatic diseases and in different neoplastic processes (Sternberg, 1996). Therefore, AP activity has become a useful serological and histological marker of disease (Bull et al., 2001). The AP activity in the prostate has been assayed in numerous studies. Tenniswood et al. (1976) reported that AP synthesis is androgen dependent. The specific function of AP in the male prostate is unclear; however, this enzyme class participates in the hydrolysis of ) Corresponding author. Tel.: C55-17-2212386; fax: C55-17- 2212390. E-mail address: taboga@bio.ibilce.unesp.br (S. Roberto Taboga). www.elsevier.com/locate/cellbi Cell Biology International 28 (2004) 335e344 1065-6995/$ - see front matter Ó 2004 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved. doi:10.1016/j.cellbi.2003.12.008