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

Evidence for a matriptase-prostasin proteolytic cascade regulating terminal epidermal differentiation.

The Journal of biological chemistry - 3 Nov 2006

Netzel-Arnett Sarah, Currie Brooke M, Szabo Roman, Lin Chen-Yong, Chen Li-Mei, Chai Karl X, Antalis Toni M, Bugge Thomas H, List Karin

Abstract excerpt

Recent gene ablation studies in mice have shown that matriptase, a type II transmembrane serine protease, and prostasin, a glycosylphosphatidylinositol-anchored membrane serine protease, are both required for processing of the epidermis-specific polyprotein, profilaggrin, stratum corneum formatio...

Read the complete abstract on PubMed

Topics

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

Share to Cell Differentiation
Share to Cell Line
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epidermal Cells

Share to Epidermis

Share to Mice, Transgenic

Share to Serine Endopeptidases

Source

Identifiers

PMID: 16980306
DOI: 10.1074/jbc.C600208200

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16980306-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for a matriptase-prostasin proteolytic cascade regulating terminal epidermal differentiation.PMID 16980306Read ↗

A matriptase-prostasin reciprocal zymogen activation complex with unique features: prostasin as a non-enzymatic co-factor for matriptase activation.Semantic proximity Read ↗

Epithelial integrity is maintained by a matriptase-dependent proteolytic pathway.Semantic proximity Read ↗

Mutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors.Semantic proximity Read ↗

The spatiotemporal control of human matriptase action on its physiological substrates: a case against a direct role for matriptase proteolytic activity in profilaggrin processing and desquamation.Semantic proximity Read ↗

Keratinocyte differentiation and proteolytic pathways in skin (patho) physiologySemantic proximity Read ↗

Strong expression association between matriptase and its substrate prostasin in breast cancerSemantic proximity Read ↗

Matriptase initiates activation of epidermal pro-kallikrein and disease onset in a mouse model of Netherton syndromeSemantic proximity Read ↗

GPI-anchored serine proteases: essential roles in development, homeostasis, and diseaseSemantic proximity Read ↗

Kallikrein-related Peptidase 5 Functions in Proteolytic Processing of Profilaggrin in Cultured Human KeratinocytesSemantic proximity Read ↗

Proteolytic processing of the serine protease matriptase-2: identification of the cleavage sites required for its autocatalytic release from the cell surface.Semantic proximity Read ↗

The epidermal barrier function is dependent on the serine protease CAP1/<i>Prss8 </i>Semantic proximity Read ↗

Aberrant mucosal wound repair in the absence of secretory leukocyte protease inhibitor.Semantic proximity Read ↗

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