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Validated All-in-One™ qPCR Primer for SAT1(NM_002970.3) Search again
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.
Validated result:
Summary
Spermidine/spermine N(1)-acetyltransferase (SSAT; EC 2.3.1.57) is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. It catalyzes the N(1)-acetylation of spermidine and spermine and, by the successive activity of polyamine oxidase, spermine can be converted to spermidine and spermidine to putrescine (Casero et al., 1991 [PubMed 1985966]).[supplied by OMIM].
Gene References into function
- Induction of alternatively spliced spermidine/spermine N1-acetyltransferase mRNA in the human kidney cells infected by venezuelan equine encephalitis and tick-borne encephalitis viruses
- overexpression of SSAT and the consequent putrescine accumulation are involved in the keratosis follicularis spinulosa decalvans phenotype
- characterization of promoter function in Hela cells by study of a factor, bound to the responsive element, that underwent modification by binding with another factor after X-ray irradiation
- genomic identification and biochemical characterization of an isoenzyme
- SSAT has a role in apoptosis induced by sulindac sulfone, which leads to reduced tissue polyamine contents in human colon cancer cells
- Transgenic SSAT-overexpressing mice are less active than syngeneic mice and show reduced aggressive behavior; furthermore, SSAT-OE mice have reduced muscle tone and grip strength, although they do not differ from syngeneic mice in several agility tasks.
- SSAT has a role in kidney ischemia-reperfusion injury
- spermidine acetyltransferase directly binds to the alpha9 cytoplasmic domain and mediates alpha9-dependent enhancement of cell migration
- Restoring high inducibility of SSAT activity subverts the reduced sensitivity to cisplatin of SSAT-deficient ovarian cancer cells.
- SSAT and SMO(PAOh1) activities are the major mediators of the cellular response of breast tumor cells to polyamines while PAO plays little or no role in this response
- Activation of SSAT by aspirin and different NSAIDs may be a common property of NSAIDs that plays an important role in their chemopreventive actions in colorectal cancer.
- tertiary structure of hSSAT reported in this article provides a sound basis for the in-depth study of its structure-function relationship
- The inhibition of IkappaB and activation of NFkappaB activate SSAT.
- a common mediator of inflammation can lead to the induction of SSAT expression by activating the NFkappaB signaling pathway in non-small cell lung cancer cells
- Pharmacological activation of PPARgamma and/or induction of SSAT may represent a therapeutic or preventive strategy for treating colorectal cancer.
- These results indicate that the disruption of polyamine homeostasis due to enhanced SSAT activity leads to DNA damage and reduced cell proliferation via activation of DNA repair and cell cycle checkpoint and disruption of Raf --> MEK --> ERK pathways.
- The structure of the SSAT-spermine-acetyl-coenzyme A complex suggested that Tyr140 acts as general acid and Glu92, through one or more water molecules, acts as the general base during catalysis.
- SSAT1, which shares 46% amino acid identity with SSAT2, also binds to HIF-1alpha and promotes its ubiquitination/degradation. However, in contrast to SSAT2, SSAT1 acts by stabilizing the interaction of HIF-1alpha with RACK1
- interaction between SLC3A2 and SAT1 suggests that these proteins may facilitate excretion of acetylated polyamines.
