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2009 | 56 | 3 | 481-486
Article title

High sequence homology between protein tyrosine acid phosphatase from boar seminal vesicles and human prostatic acid phosphatase

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EN
Abstracts
EN
Boar seminal vesicle protein tyrosine acid phosphatase (PTAP) and human prostatic acid phosphatase (PAP) show high affinity for protein phosphotyrosine residues. The physico-chemical and kinetic properties of the boar and human enzymes are different. The main objective of this study was to establish the nucleotide sequence of cDNA encoding boar PTAP and compare it with that of human PAP cDNA. Also, the amino-acid sequence of boar PTAP was compared with the sequence of human PAP. PTAP was isolated from boar seminal vesicle fluid and sequenced. cDNA to boar seminal vesicle RNA was synthesized, amplified by PCR, cloned in E. coli and sequenced. The obtained N-terminal amino-acid sequence of boar PTAP showed 92% identity with the N-terminal amino-acid sequence of human PAP. The determined sequence of a 354 bp nucleotide fragment (GenBank accession number: GQ184596) showed 90% identity with the corresponding sequence of human PAP. On the basis of this sequence a 118 amino acid fragment of boar PTAP was predicted. This fragment showed 89% identity with the corresponding fragment of human PAP and had a similar hydropathy profile. The compared sequences differ in terms of their isoelectric points and amino-acid composition. This may explain the differences in substrate specificity and inhibitor resistance of boar PTAP and human PAP.
Year
Volume
56
Issue
3
Pages
481-486
Physical description
Dates
published
2009
received
2009-05-26
revised
2009-09-08
accepted
2009-09-15
(unknown)
2009-09-17
Contributors
  • Department of Animal Biochemistry and Biotechnology, University of Warmia and Mazury in Olsztyn, Olsztyn, Poland
  • Institute of Biotechnology and Antibiotics, Warszawa, Poland
  • Department of Animal Biochemistry and Biotechnology, University of Warmia and Mazury in Olsztyn, Olsztyn, Poland
References
  • Altshul SF, Madden TL, Schaffer AA, Zhang J, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
  • Apostol I, Kuciel R, Wasylewska E, Ostrowski WS (1985) Phosphotyrosine as a substrate of acid and alkaline phosphatase. Acta Biochim Polon 32: 187-197.
  • Bem S, Ostrowski WS (2001) Effect of tartaric acid on conformation and stability of human prostatic phosphatase: an infrared spectroscopic and calorimetric study. Acta Biochim Polon 48: 755-762.
  • Birnboim HC, Doly J (1979) A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res 7: 1513-1523.
  • Chomczyński P, Sacchi N (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156-159.
  • Clark JM (1988) Novel non-templated nucleotide addition reactions catalyzed by prokaryotic and eukaryotic DNA polymerases. Nucleic Acids Res 16: 9677-9686.
  • Dybczyński I, Płucienniczak A (1988) A protocol for DNA fragment extraction from polyacrylamide gels. Biotechniques 6: 924-926.
  • Kalab P, Peknicova J, Geussova G, Moos J (1998) Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway. Mol Reprod Dev 51: 304-314.
  • Kyte J, Doolittle R (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132.
  • Lin MF, Meng TC, Rao PS, Chang C, Schntal AH, Lin FF (1998) Expression of human prostatic acid phosphatase correlates with androgen-stimulated cell proliferation in prostate cancer cell lines. J Biol Chem 273: 5939-5947.
  • Luchter-Wasylewska E, Wasylewski M, Röhm K-H (2003) Concentration-dependent dissociation/association of human prostatic acid phosphatase. J Protein Chem 22: 243-247.
  • Mann T, Lutwak-Mann C (1981) Male reproductive function and semen. Themes and trends in physiology, biochemistry and investigative andrology. Springer Verlag, Berlin.
  • Naz RK (1996) Involvement of protein tyrosine phosphorylation of human sperm in capacitation/acrosome reaction and zona pellucida binding. Front Biosci 1: d206-d213.
  • Ostrowski WS, Kuciel R (1994) Human prostatic acid phosphatase: selected properties and practical applications. Clin Chim Acta 226: 121-129.
  • Pohlmann R, Krentler C, Schmidt B, Schroder W, Lorkowski G, Culley J, Mersmann G, Geier C, Waheed A, Gottschalk S, Grzeschik K-H, Hasilik A, Figura K (1988) Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment. EMBO J 7: 2343-2350.
  • Roiko K, Janne OA, Vihko P (1990) Primary structure of rat secretory acid phosphatase and comparison to other acid phosphatases. Gene 89: 223-229.
  • Sambrook J, Fritsh EF, Maniatis T (1989) Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Laboratory Press.
  • Si Y, Okuno M (1999) Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation. Biol Reprod 61: 240-246.
  • Solar HT, Bahl OP (1987) Chemical method for the deglycosylation of proteins using trifluoromethanesulfonic acid (TFMS). Arch Biochem Biophys 259: 52-57.
  • Urner F, Sakkas D (2003) Protein phosphorylation in mammalian spermatozoa. Reproduction 125: 17-26.
  • van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL (1991) Covalent structure, disulfide bonding and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem 266: 2313-2319.
  • van Poucke M, Yerle M, Tuggle C, Piumi F, Genet C, van Zeveren A, Peelman LJ (2001) Integration of porcine chromosome 13 maps. Cytogenet Cell Genet 93: 297-303.
  • Veeramani S, Yan T-C, Chen S-J, Lin F-F, Petersen JE, Shaheduzzaman S, Srivastava S, MacDonald RG, Lin M-F (2005) Cellular prostatic acid phosphatase: a protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer. Endocr Relat Cancer 12: 805-822.
  • Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML (1988) Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett 236: 275-281.
  • Visconti PE, Kopf GS (1998) Regulation of protein phosphorylation during sperm capacitation. Biol Reprod 59: 1-6.
  • Wysocki P, Strzeżek J (2000) Molecular forms of acid phosphatase of boar seminal plasma. Anim Sci Pap Rep 18: 99-106.
  • Wysocki P, Strzeżek J (2003) Purification and characterization of a protein tyrosine acid phosphatase from boar seminal vesicle glands. Theriogenology 59: 1011-1025.
  • Wysocki P, Strzeżek J (2006) Isolation and biochemical characteristics of a molecular form of epididymal acid phosphatase of boar seminal plasma. Theriogenology 66: 2152-2159.
  • Wysocki P, Koncicka K, Strzeżek J (2009) Is the phosphorylation status of tyrosine proteins a marker for cryo-capacitation of boar spermatozoa? Bull Vet Inst Pulawy 53: 229-232.
  • Yousef GM, Diamandis M, Jung K, Diamandis EP (2001) Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis. Genomics 74: 385-395.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv56p481kz
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