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Validated All-in-One™ qPCR Primer for FOLH1(NM_004476.3) Search again
Product ID:
HQP153991
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
FGCP, FOLH, GCP2, GCPII, NAALAD1, PSM, PSMA, mGCP
Gene Description:
folate hydrolase 1
Target Gene Accession:
NM_004476.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes a type II transmembrane glycoprotein belonging to the M28 peptidase family. The protein acts as a glutamate carboxypeptidase on different alternative substrates, including the nutrient folate and the neuropeptide N-acetyl-l-aspartyl-l-glutamate and is expressed in a number of tissues such as prostate, central and peripheral nervous system and kidney. A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity.
Gene References into function
- expressed in prostate tissue, and especially in prostate cancer tissue
- GCP2 polymorphism explained nearly 50% of the variance of red blood cell folate in ESRD
- GCP2 1561C>T is associated with elevated folate levels but not homocysteine levels in kidney transplant patients
- PSMA expression is regulated by NFATc1 with an AP-3 binding site
- N-linked carbohydrate structures are important for the folate hydrolase function of the protein. Removal of sugars partially or completely causes PSMA to be enzymatically inactive, improperly folded, resulting in increased rate of degradation.
- PSMA is internalized via a clathrin-dependent endocytic mechanism and that internalization of PSMA is mediated by the five N-terminal amino acids
- proteins binding PSMA
- Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity
- PSMA gene lacks specificity for detecting prostate epithelial cells
- Knockdown of PSMA expression increased invasiveness of LNCaP cells by 5-fold.
- Transcriptional activity of the PSMA promoter/enhancer is prostate specific.
- Structure and relevance to the development of chemotherapeutics and cancer-imaging agents.
- PSMA may function as a receptor internalizing a putative ligand, an enzyme playing a role in nutrient uptake, and a peptidase involved in signal transduction in prostate epithelial cells. [review]
- acquisition of folding determinants in the Golgi is an essential prerequisite for protein trafficking and sorting of PSMA
- The folate hydrolase activity of PSMA may provide a growth advantage to prostate cancer cells in low folate and physiological folate environments.
- PSMA binds to caveolin-1 and undergoes internalization via a caveolae-dependent mechanism in microvascular endothelial cells
- In suicide gene therapy, anti-PSMA-liposome complex exerted a significant inhibitory effect on the growth of LNCaP xenograft, in contrast to normal IgG-liposome complex.
- Using pure recombinant GCPII and homologous GCPIII, we conclude that GCPII is responsible for the majority of overall NAAG-hydrolyzing activity in the human brain.
- Polymorphism is associated with higher plasma folate and lower homocysteine concentrations in women who abstain from alcohol.
- Pattern differences in GCP II gene promoter expression in SVG and LNCaP cells suggest that sequences beyond 240 bp may be important for tissue-specific GCP II expression.
- the residues forming the S1 pocket might be more important for the 'fine-tuning' of GCPII substrate specificity
- the intracellular transport of PSMA occurs through populations of DRMs distinct for each biosynthetic form and cellular compartment
- Tissues such as prostate and testes exhibit different GCPII expression levels among the species studied (human, rats, swine).
- Crystal structures of human GCPII in complex with phosphapeptide analogs show the S1 pocket of GCPII and the data indicate the importance of Asn519, Arg463, Arg534, and Arg536 for recognition of the penultimate (i.e., P1) substrate residues.
- prostate-specific membrane antigen is expressed in tumor-associated neovasculature of the majority of renal cortical tumors
- PSMA is underexpressed in advanced stage endometrial adenocarcinoma (EAC); loss of PSMA expression can be considered as a prognostic marker in patients with EAC; loss of PSMA expression in a subset of EAC cases could be due to epigenetic silencing
- Neonatal methylmalonic acid was predicted by maternal methylmalonic acid and GCPII
- prostate-specific membrane antigen is expressed in neovasculature from physiologic regenerative and reparative conditions
- PSMA was the most useful marker to identify residual prostatic carcinoma after hormone therapy.
- Ectopic PSMA expression on PC-3 cells increased the invasive capacity of cells in in vitro invasion assays, which could be competed out by folic acid. These results suggest PSMA facilitates the development of prostate cancer
- analysis of interactions between human glutamate carboxypeptidase II and urea-based inhibitors
- PSM' protein is likely not generated by alternative splicing of the PSMA gene but by different mechanism, probably via an endoproteolytic cleavage of the full-length PSMA.
- although the RFC1 80G > A and FOLH1 1561C > T polymorphisms may influence folate status, they are not likely to have a major independent role in the development of colorectal cancer