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Human ACPP Protein expressed in Human - ABIN934761
Drake, White, Fuller, Igwe, Clements, Nyalwidhe, Given, Lance, Semmes: Clinical collection and protein properties of expressed prostatic secretions as a source for biomarkers of prostatic disease. in Journal of proteomics 2009
Enhanced TDPase and TMPase activities may contribute to the reduction of TDP level in AD patients. The results imply that an imbalance of phosphorylation-dephosphorylation related to thiamine and glucose metabolism may be a potential target for AD prevention and therapy.
Thirteen single nucleotide polymorphism (SNPs) in acid phosphatase prostate (ACPP) were suggested as candidate causal alleles that underlie ACPP regulation and expression.
we have measured the intramolecular diffusion of the full length and 8-residue deletion peptides at two different pHs (show PCBD1 Proteins) and found a correlation with fibrillization lag (show STMN1 Proteins) time. These results can be explained by a simple kinetic model of the early stages of aggregation in which oligomerization is controlled by the rate of peptide reconfiguration.
Prostatic acid phosphatase delays prostate cancer cell growth in G1 phase of the cell cycle.
Studies suggest that understanding of prostatic acid phosphatase function and regulation of expression will have a significant impact on understanding prostate cancer (PCa (show FLVCR1 Proteins)) progression and therapy.
Certain factors identified within semen, termed semen-derived enhancers of virus infection (SEVI), fragments of prostatic acid phosphatase, have been shown to significantly enhance HIV-1 infectivity.
ACPP increases significantly in epithelial cells of ovarian carcinoma, which indicates that it may be a candidate biomarker for diagnosis of epithelia-derived ovarian cancer in women.
Data indicate that hypoxia regulates prostatic acid phosphatase (PAP) through hypoxia-inducible factor 2 alpha (show EPAS1 Proteins) (HIF2alpha (show EPAS1 Proteins)) and from stimulated A2B (show ADORA2B Proteins) adenosine receptors.
GCNT1 (show GCNT1 Proteins) is over-expressed in prostate cancer and is associated with higher levels of core 2 O-sLe(x) in PSA (show PLAG1 Proteins), PAP (show REG3A Proteins) and MUC1 (show MUC1 Proteins) proteins.
Data indicate that prostate acid phosphatase-based peptide vaccine PAP (show REG3A Proteins)-114-128 peptide appears to be a relevant for the treatment of prostate cancer.
PAP (show ASAP1 Proteins)-immunoreactivity was present in type I and one of type III taste cells of taste buds. Thus, it is suggested that PAP (show ASAP1 Proteins) might be a responsible ectoenzyme for metabolism of extracellular nucleotides, being involved in the regulation of taste signaling in taste buds.
These findings demonstrate that PAP (show ASAP1 Proteins) secreted by PCa (show ENPP1 Proteins) cells in OB bone metastases increases osteoprotegerin (show TNFRSF11B Proteins) and plays a critical role in the vicious cross talk between cancer and bone cells.
functional PAP (show ASAP1 Proteins)(thorn) neurons are essential for the analgesic effect, which is mediated by NGF (show NGFB Proteins)-trkA (show NTRK1 Proteins) signaling.
TMPAP is involved in the control of GABAergic tone in the brain also through exocytosis, and that PAP (show ASAP1 Proteins) deficiency produces a distinct neurological phenotype.
In male mouse saliva (show RAG1AP1 Proteins) prostatic acid phosphatase regulates salivation.
Data indicate that prostate acid phosphatase-based peptide vaccine PAP (show ASAP1 Proteins)-114-128 peptide appears to be a relevant for the treatment of prostate cancer.
this PAP (show ASAP1 Proteins)-/- mouse model shows that TMPAP is required for the normal function of prostate in mice, and its deficiency leads to prostate adenocarcinoma.
Both prostatic acid phosphatase and ecto-5'-nucleotidase generate adenosine in the dorsal spinal cord.
Prostatic acid phosphatase is required for the antinociceptive effects of thiamine and benfotiamine.
Experiments indicate that PAP (show ASAP1 Proteins) and NT5E (show NT5E Proteins) are the main ectonucleotidases that generate adenosine in nociceptive circuits and indicate these enzymes transform pulsatile or sustained nucleotide release into an inhibitory adenosinergic signal.
The obtained N-terminal amino-acid sequence of boar PTAP showed 92% identity with the N-terminal amino-acid sequence of human PAP (show PDAP1 Proteins). The determined sequence of a 354 bp nucleotide fragment showed 90% identity with the corresponding sequence of human PAP (show PDAP1 Proteins).
This gene encodes an enzyme that catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. It is synthesized under androgen regulation and is secreted by the epithelial cells of the prostate gland. An alternatively spliced transcript variant encoding a longer isoform has been found for this gene. This isoform contains a transmembrane domain and is localized in the plasma membrane-endosomal-lysosomal pathway.
, prostatic acid phosphatase
, prostatic acid phosphotase
, thiamine monophosphatase
, fluoride-resistant acid phosphatase
, lysosomal acid phosphatase
, prostatic acid phosphatase (rPAP)
, acid phosphatase, prostate
, tyrosine acid phosphatase
, prostatic acid phosphatase-like
, testicular acid phosphatase homolog