Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A quantitative study on splice variants of N-acylethanolamine acid amidase in human prostate cancer cells and other cells.

Biochimica et biophysica acta - 1 Dec 2016

Sakura Yuma, Tsuboi Kazuhito, Uyama Toru, Zhang Xia, Taoka Rikiya, Sugimoto Mikio, Kakehi Yoshiyuki, Ueda Natsuo

Abstract excerpt

N-Acylethanolamine acid amidase (NAAA) is a lysosomal enzyme, hydrolyzing various bioactive N-acylethanolamines with a preference for palmitoylethanolamide. Human NAAA mRNA was previously reported to consist of multiple 3'-end splice variants. However, their tissue distributions and roles have not been examined yet. In the present study, we first identified four major splice variants (tentatively referred to as...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amidohydrolases
Share to Ethanolamines

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Evaluation Studies as Topic

Share to HEK293 Cells

Share to HeLa Cells

Share to MCF-7 Cells

Share to Prostatic Neoplasms

Share to RNA Splicing

Source

Identifiers

PMID: 27693242
DOI: 10.1016/j.bbalip.2016.09.018

Genes

NAAA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A quantitative study on splice variants of N-acylethanolamine acid amidase in human prostate cancer cells and other cells.PMID 27693242Read ↗

Prostate-specific membrane antigen is a hydrolase with substrate and pharmacologic characteristics of a neuropeptidase.Semantic proximity Read ↗

SERPINA1 long transcripts produce non-secretory alpha1-antitrypsin isoform: In vitro translation in living cells.Semantic proximity Read ↗

Characterization of two spliced variants of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells.Semantic proximity Read ↗

GCPII Variants, Paralogs and OrthologsSemantic proximity Read ↗

Genomic organization of human arylamine N-acetyltransferase Type I reveals alternative promoters that generate different 5'-UTR splice variants with altered translational activities.Semantic proximity Read ↗

MAOA-a novel decision maker of apoptosis and autophagy in hormone refractory neuroendocrine prostate cancer cellsSemantic proximity Read ↗

T2E (TMPRSS2-ERG) fusion transcripts are associated with higher levels of AMACR mRNA and a subsequent prostate cancer diagnosis in patients with atypical small acinar proliferation.Semantic proximity Read ↗

Development of an Isoform-Discriminating RT-qPCR Assay for Transcript-Level Profiling of Human ASAH2 in Colorectal Cancer Cell ModelsSemantic proximity Read ↗

Human acid ceramidase is overexpressed but not mutated in prostate cancer.Semantic proximity Read ↗

Autophagy is differentially induced in prostate cancer LNCaP, DU145 and PC-3 cells via distinct splicing profiles of ATG5Semantic proximity Read ↗

Cloning of mouse gamma-glutamyl hydrolase in the form of two cDNA variants with different 5' ends and encoding alternate leader peptide sequences.Semantic proximity Read ↗

Isolation and Expression of Novel Human Glutamate Carboxypeptidases with N-Acetylated α-Linked Acidic Dipeptidase and Dipeptidyl Peptidase IV ActivitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.