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

The aspartic protease napsin A suppresses tumor growth independent of its catalytic activity.

Laboratory investigation; a journal of technical methods and pathology - 1 Mar 2008

Ueno Takayuki, Elmberger Göran, Weaver Timothy E, Toi Masakazu, Linder Stig

Abstract excerpt

Members of the aspartic protease family have been implicated in cancer progression. The aspartic protease napsin A is expressed in type II cells of the lung, where it is involved in the processing of surfactant protein B (SP-B). Napsin A is also expressed in kidney, where its function is unknown. Here, we examined napsin A mRNA expression in human kidney tissues using in situ hybridization. Whereas strong napsin...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid Endopeptidases
Share to Cell Culture Techniques

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Clone Cells

Share to Collagen

Share to Histidine

Share to Mice, SCID

Share to Transplantation, Heterologous

Share to Tumor Burden

Source

Identifiers

PMID: 18195689
DOI: 10.1038/labinvest.3700718

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 · 9 closest

The aspartic protease napsin A suppresses tumor growth independent of its catalytic activity.PMID 18195689Read ↗

Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomasSemantic proximity Read ↗

RNA interference suppression of A100A4 reduces the growth and metastatic phenotype of human renal cancer cells via NF-kB-dependent MMP-2 and bcl-2 pathway.Semantic proximity Read ↗

Expression, Intracellular Localization, and Maturation of Cysteine Cathepsins in Renal Embryonic and Cancer Cell LinesSemantic proximity Read ↗

Overexpressed proprotein convertase 1/3 induces an epithelial-mesenchymal transition in airway epithelium.Semantic proximity Read ↗

Progastrin overexpression imparts tumorigenic/metastatic potential to embryonic epithelial cells: phenotypic differences between transformed and nontransformed stem cells.Semantic proximity Read ↗

Antisense RNA-mediated deficiency of the calpain protease, nCL-4, in NIH3T3 cells is associated with neoplastic transformation and tumorigenesis.Semantic proximity Read ↗

Juxtacrine activation of epidermal growth factor (EGF) receptor by membrane-anchored heparin-binding EGF-like growth factor protects epithelial cells from anoikis while maintaining an epithelial phenotype.Semantic proximity Read ↗

Proteolytic activation of the human epithelial sodium channel by trypsin IV and trypsin I involves distinct cleavage sites.Semantic proximity Read ↗

Role for dipeptidyl peptidase IV in tumor suppression of human non small cell lung carcinoma cells.Semantic proximity Read ↗

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