Acrosina
Acrosina é uma enzima que actua como uma protease. Em seres humanos, a acrosina é codificada pelo gene ACR.[1][2] A acrosina é libertada pelo acrossoma dos espermatozoides como consequência da reacção acrossómica. Auxilia na penetração da zona pelúcida.
Acrosina | |||
---|---|---|---|
Identificadores | |||
Símbolo | ACR | ||
IDs externos | OMIM: 102480 MGI: 87884 HomoloGene: 855 ChEMBL: 2738 GeneCards: ACR Gene | ||
Número EC | 3.4.21.10 | ||
Ortólogos | |||
Espécies | Humano | Rato | |
Entrez | 49 | 11434 | |
Ensembl | ENSG00000100312 | ENSMUSG00000022622 | |
UniProt | P10323 | P23578 | |
RefSeq (mRNA) | NM_001097 | NM_001205049 | |
RefSeq (proteína) | NP_001088 | NP_001191978 | |
Localização (UCSC) |
Chr 22: 51.18 – 51.18 Mb |
Chr 15: 89.57 – 89.57 Mb | |
Busca PubMed | [1] | [2] | |
Função
editarA acrosina é a principal proteinase presente no acrossoma de espermatozóides maduros. É uma típica serina protease com especificidade semelhante a tripsina. É acumulada no acromossoma na sua forma percursora, a pró-acrosina. A enzima activa funciona na lise da zona pelúcida, facilitando dessa forma a penetração do espermatozóide através das camadas glicoproteicas mais interiores do óvulo. O mRNA para a acrosina é sintetizado nos estágios pós-meióticos da espermatogénese. Na pró-acrosina humana aparece em primeiro lugar nos esparmatídeos haplóides.[3]
Referências
- ↑ Adham IM, Klemm U, Maier WM, Engel W (janeiro de 1990). «Molecular cloning of human preproacrosin cDNA». Hum. Genet. 84 (2): 125–8. PMID 2298447. doi:10.1007/bf00208925
- ↑ Honda A, Siruntawineti J, Baba T (2002). «Role of acrosomal matrix proteases in sperm-zona pellucida interactions». Hum. Reprod. Update. 8 (5): 405–12. PMID 12398221. doi:10.1093/humupd/8.5.405
- ↑ «Entrez Gene: acrosin»
Leitura adicional
editar- Elce JS, McIntyre EJ (1982). «Purification of bovine and human acrosin». Can. J. Biochem. 60 (1): 8–14. PMID 6802470. doi:10.1139/o82-002
- Zheng X, Geiger M, Ecke S,; et al. (1994). «Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa». Am. J. Physiol. 267 (2 Pt 1): C466–72. PMID 7521127
- Kimura K, Wakamatsu A, Suzuki Y,; et al. (2006). «Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes». Genome Res. 16 (1): 55–65. PMC 1356129 . PMID 16344560. doi:10.1101/gr.4039406
- Klemm U, Müller-Esterl W, Engel W (1991). «Acrosin, the peculiar sperm-specific serine protease». Hum. Genet. 87 (6): 635–41. PMID 1937464. doi:10.1007/bf00201716
- Kim J, Bhinge AA, Morgan XC, Iyer VR (2005). «Mapping DNA-protein interactions in large genomes by sequence tag analysis of genomic enrichment». Nat. Methods. 2 (1): 47–53. PMID 15782160. doi:10.1038/nmeth726
- Moreno RD, Hoshi M, Barros C (1999). «Functional interactions between sulphated polysaccharides and proacrosin: implications in sperm binding and digestion of zona pellucida». Zygote. 7 (2): 105–11. PMID 10418103. doi:10.1017/S0967199499000453
- Liu RZ, Lu YL, Xu ZG,; et al. (2003). «[The effect of semen antisperm antibody on human sperm acrosin activity]». Zhonghua Nan Ke Xue. 9 (4): 252–3. PMID 12931362
- Steven FS, Griffin MM, Chantler EN (1982). «Inhibition of human and bovine sperm acrosin by divalent metal ions. Possible role of zinc as a regulator of acrosin activity». Int. J. Androl. 5 (4): 401–12. PMID 6815104. doi:10.1111/j.1365-2605.1982.tb00270.x
- Marà SI, Rawe V, Biancotti JC,; et al. (2003). «Biochemical and molecular studies of the proacrosin/acrosin system in patients with unexplained infertility». Fertil. Steril. 79 Suppl 3: 1676–9. PMID 12801583
- Glogowski J, Demianowicz W, Piros B, Ciereszko A (1998). «Determination of acrosin activity of boar spermatozoa by the clinical method: optimization of the assay and changes during short-term storage of semen». Theriogenology. 50 (6): 861–72. PMID 10734459. doi:10.1016/S0093-691X(98)00191-5
- Furlong LI, Veaute C, Vazquez-Levin MH (2005). «Binding of recombinant human proacrosin/acrosin to zona pellucida glycoproteins. II. Participation of mannose residues in the interaction». Fertil. Steril. 83 (6): 1791–6. PMID 15950652. doi:10.1016/j.fertnstert.2004.12.043
- Furlong LI, Harris JD, Vazquez-Levin MH (2005). «Binding of recombinant human proacrosin/acrosin to zona pellucida (ZP) glycoproteins. I. Studies with recombinant human ZPA, ZPB, and ZPC». Fertil. Steril. 83 (6): 1780–90. PMID 15950651. doi:10.1016/j.fertnstert.2004.12.042
- Hartley JL, Temple GF, Brasch MA (2000). «DNA Cloning Using In Vitro Site-Specific Recombination». Genome Res. 10 (11): 1788–95. PMC 310948 . PMID 11076863. doi:10.1101/gr.143000
- Collins JE, Wright CL, Edwards CA,; et al. (2004). «A genome annotation-driven approach to cloning the human ORFeome». Genome Biol. 5 (10): R84. PMC 545604 . PMID 15461802. doi:10.1186/gb-2004-5-10-r84
- Dubé C, Leclerc P, Baba T,; et al. (2005). «The proacrosin binding protein, sp32, is tyrosine phosphorylated during capacitation of pig sperm». J. Androl. 26 (4): 519–28. PMID 15955892. doi:10.2164/jandrol.04163
- Strausberg RL, Feingold EA, Grouse LH,; et al. (2002). «Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences». Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899
- Zahn A, Furlong LI, Biancotti JC,; et al. (2002). «Evaluation of the proacrosin/acrosin system and its mechanism of activation in human sperm extracts». J. Reprod. Immunol. 54 (1–2): 43–63. PMID 11839395. doi:10.1016/S0165-0378(01)00080-8
- Howes E, Pascall JC, Engel W, Jones R (2001). «Interactions between mouse ZP2 glycoprotein and proacrosin; a mechanism for secondary binding of sperm to the zona pellucida during fertilization». J. Cell. Sci. 114 (Pt 22): 4127–36. PMID 11739644
- Yudin AI, Vandevoort CA, Li MW, Overstreet JW (1999). «PH-20 but not acrosin is involved in sperm penetration of the macaque zona pellucida». Mol. Reprod. Dev. 53 (3): 350–62. PMID 10369396. doi:10.1002/(SICI)1098-2795(199907)53:3<350::AID-MRD11>3.0.CO;2-9