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PubMed2001

Effects of bicalutamide and leuprolide on prostate-specific antigen (PSA), acid phosphatase (ACP) and prostatic acid phosphatase (PAP) in men with benign prostatic hyperplasia (BPH).

The effects of the nonsteroidal antiandrogen bicalutamide (Casodex(TM)) and the luteinizing hormone releasing hormone agonist leuprolide depot (Procren Depot(TM), Lupron Depot(TM)) on serum prostate-specific antigen (PSA), acid phosphatase (ACP), and prostatic acid phosphatase (PAP) in patients with benign prostatic hyperplasia (BPH) were determined. Thirty patients with BPH were randomised to receive bicalutamide 50 mg orally once daily or a placebo for 24 weeks, followed by 24 weeks of follow-up (bicalutamide study). In another study 55 men were randomised between 3.75 mg leuprolide depot intramuscularly at every 28 days for 24 weeks or placebo injections (leuprolide study). In both studies blood sampling was performed at baseline, at week 12 at week 24 and 24 weeks after the end of therapy. Androgen suppression with bicalutamide 50 mg daily for 24 weeks resulted in a median of 56% reduction of PSA (P<0.001 when compared to placebo). Acid phosphatase and PAP did not change. Leuprolide resulted in a median of 87% reduction of serum PSA (P<0.001) and a 39% reduction of PAP (P=0.023), whereas ACP was unchanged. Both bicalutamide and leuprolide induced a pronounced decline in serum PSA in BPH patients. The studies suggest a stronger androgen suppressive effect of leuprolide than of bicalutamide, but this difference might largely be due to too low a dosage of bicalutamide. ACP and PAP were relatively insensitive to androgen suppression. Our study suggests a different degree of androgen suppression on PSA originating from benign tissue versus cancer tissue, and that the direction of this discrepancy might be different for various androgen suppressive regimens.Prostate Cancer and Prostatic Diseases (2001) 4, 173-177.

Journal Article↗
PubMed1990

An enzyme with a double identity: purple acid phosphatase and tartrate-resistant acid phosphatase.

The tartrate-resistant acid phosphatases or purple acid phosphatases constitute a class of related mammalian enzymes. Spectroscopic and magnetic studies have revealed that the purple phosphatases contain a novel dinuclear iron active site that is responsible for the purple color. More biologically and biomedically oriented research has shown that the tartrate-resistant acid phosphatases generally occur in osteoclasts and white blood cells, where they appear to be localized in lysosomes or similar organelles. Despite the different names given the enzymes by researchers in the two fields, recent sequence determinations and immunological studies indicate that the enzymes are identical. The status of research in both fields is reviewed in an attempt to present a unified picture of the structure, function, and mode of action of these unique metalloproteins.

Acid Phosphatase↗
PubMed1990

Primary structure of rat secretory acid phosphatase and comparison to other acid phosphatases.

Overlapping cDNA clones encoding rat prostatic acid phosphatase (rPAP) were isolated by using two human prostatic acid phosphatase (hPAP)-encoding cDNAs to screen rat prostatic cDNA libraries. The isolated cDNAs encompassed a total of 1626 nucleotides (nt), of which 1143 nt corresponded to the protein coding sequence encoding a mature polypeptide of 350 amino acids (aa) and a 31-aa long signal peptide-like sequence. The deduced Mr of the mature rPAP was 40,599. RNA blot analysis indicated the presence of three mRNA species (4.9, 2.3 and 1.5 kb in size) in the rat prostate. The deduced aa sequences of rPAP and hPAP show 75% identity, whereas the similarity between rPAP and human lysosomal acid phosphatase (hLAP) is only 45%. Furthermore, the sequence similarity between rPAP and rat lysosomal acid phosphatase (rLAP) is 46% at the aa level. Similar to hPAP, but unlike hLAP and rLAP, the rPAP sequence lacks a membrane-anchoring domain indicating the secretory character of this phosphatase. All six cysteines present in the overlapping areas of the mature rPAP, hPAP, rLAP and hLAP proteins are positionally conserved, suggesting that these residues are important for the tertiary structure of acid phosphatases (APs). The previously reported active site residues, two arginines and one histidine, are also conserved in these APs.

Acid Phosphatase↗
PubMed1998

Conservation of the active site motif in Aspergillus niger (ficuum) pH 6.0 optimum acid phosphatase and kidney bean purple acid phosphatase.

Aspergillus niger (ficuum) and the kidney bean purple acid phosphatases retained all the essential amino acids in the active site despite a low degree of total sequence homology. This high degree of homology in the sequence motif of A. niger fungal acid phosphatase (Apase6) active site with Kidney bean metallo phosphoesterase (KBPAP) and the absence of the RHG-XRXP sequence motif indicates Apase6 to be a metallophosphoesterase rather than a histidine acid phosphatase.

6-Phytase↗
PubMed2004

[Allele polymorphism of alkaline phosphatase, acid soluble phosphatase, and vitamin D-binding protein genes in postmenopausal osteoporosis].

AIM: To study polymorphism of genes involved in mechanisms regulating metabolism of bone tissue: alkaline (ALPL) and acid (ACP1) phosphatases, vitamin D-binding protein (GC); to ascertain associations of their genotypes and alleles with osteoporosis (OP) and mineral density of spinal and femoral bone tissue (BTMD). MATERIAL AND METHODS: Relevant genetic examination was made in 70 females with OP diagnosed by the WHO criteria (1994) aged 60-79 years (mean age 71.0 +/- 6.2 years) and 51 OP-free females in the same age interval (mean age 69.0 +/- 5.6 years). Polymorphic sites of the genes were examined by polymerase chain reaction. Trinucleotide repeat, ARG105GLN polymorphism of restrictive fragment length (PRFL), [GC, TRH420LYS] PRFL were studied for ALPL gene, ACP1 gene and GC gene, respectively. RESULTS: Association was found between frequencies of genotypes SS, 2F and FS, F allele of GC gene with OP as well as between PRFL of the spine, femur and some GC genotypes in OP women. Genes ALPL and ACP1 were not associated with OP. CONCLUSION: It is suggested that genotypes SS, 2F and FS have marked functional differences in fixation and transport of vitamin D active metabolites involved in metabolism of bone tissue in OP.

Absorptiometry, Photon↗