Ask about this productRelated genes to: RNPEPL1 Blocking Peptide
- Gene:
- RNPEPL1 NIH gene
- Name:
- arginyl aminopeptidase like 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-09-01
- Date modifiied:
- 2016-07-29
Related products to: RNPEPL1 Blocking Peptide
Related articles to: RNPEPL1 Blocking Peptide
- The aim of this study was to explore the prognostic significance of necrotic cell death triggered by sodium overload (NECSO)-related genes in lung adenocarcinoma (LUAD) and construct a prognostic model with high predictive efficiency. The findings will enable a precise stratification of the prognostic risk of patients with LUAD. Analysis of the constructed prognostic model, immune cell infiltration, and tumor mutational burden (TMB) will facilitate the development of individualized precision medical protocols. - Source: PubMed
Publication date: 2026/03/02
Liang LiWang XiaoqiLiu HuihuiHuang TingZhu QuanLu FangguoChen Chunjing - Necrosis by sodium overload (NECSO), a necrotic pathway triggered by sodium overload, has been implicated in various cellular processes. Its link to lung adenocarcinoma (LUAD) remained unexplored; this study investigated the potential relationship between NECSO and LUAD. - Source: PubMed
Publication date: 2025/10/28
Yuan JianxuZhou DalinYu Shengjie - Hepatocellular carcinoma (HCC) is the most common primary liver cancer worldwide. Cancer cells' local infiltration, proliferation, and spread are mainly influenced by the protein hydrolyzing function of different matrix metalloproteinases (MMPs). However, no study has determined the relationship between MMPs and prognostic prediction in HCC. - Source: PubMed
Publication date: 2024/05/16
Yuan XingxingYang LiuxinGao JiaweiMao XuZhang YaliYuan Wei - - Source: PubMed
- It is now evident that the M1 family of aminopeptidases play important roles in many pathophysiological processes. Among them, the enzymatic properties of arginyl aminopeptidase-like 1 (RNPEPL1) are characterized only by its truncated form. No peptide substrate has been identified. To characterize the enzymatic properties of RNPEPL1 in more detail, the full-length protein was expressed in Escherichia coli and purified to homogeneity. The full-length RNPEPL1 showed rather restricted substrate specificity and basic amino acid preference towards synthetic substrates, which was different from the previously reported specificity characterized by the truncated form. Searching for peptide substrates, we found that several peptides, such as Met-enkephalin and kallidin, were cleaved. RNPEPL1 cleaved bradykinin to de-[Arg]-bradykinin despite the presence of proline at the P2'-position. The enzyme cleaved Met-enkephalin but not dynorphin A1-17. Similar to aminopeptidase B, the full-length RNPEPL1 showed basic amino acid preference towards both synthetic and peptide substrates. In addition to the unusual cleavage of bradykinin, this enzyme shows chain length-dependent cleavage of peptide substrates sharing N-terminal amino acid sequence. This is the first study to report the enzymatic properties of the full-length human RNPEPL1 as an aminopeptidase enzyme. - Source: PubMed
Ohnishi AtsushiTsujimoto Masafumi