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Proprotein convertase subtilisin/kexin type 6

PACE4, SPC4
The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can cleave precursor protein at their paired basic amino acid processing sites. Some of its substrates are - transforming growth factor beta related proteins, proalbumin, and von Willebrand factor. This gene is thought to play a role in tumor progression. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PC6, PC1, PC2, PCS, ACID
Papers on PACE4
Novel Insights into Structure-Activity Relationships of N-Terminally Modified PACE4 Inhibitors.
New
Day et al., Sherbrooke, Canada. In Chemmedchem, Feb 2016
UNASSIGNED: PACE4 plays important roles in prostate cancer cell proliferation.
Neuroinflammation-Induced Interactions between Protease-Activated Receptor 1 and Proprotein Convertases in HIV-Associated Neurocognitive Disorder.
New
Seidah et al., Montréal, Canada. In Mol Cell Biol, Nov 2015
The proprotein convertases (PCs) furin, PC5, PACE4, and PC7 cleave secretory proteins after basic residues, including the HIV envelope glycoprotein (gp160) and Vpr.
PC7 and the related proteases Furin and Pace4 regulate E-cadherin function during blastocyst formation.
New
Constam et al., Lausanne, Switzerland. In J Cell Biol, Oct 2015
We show that morula compaction and ICM formation depend on PC7 and the related proprotein convertases (PCs) Furin and Pace4 and that these proteases jointly regulate cell-cell adhesion mediated by E-cadherin processing.
PCSK6-mediated corin activation is essential for normal blood pressure.
New
Impact
Wu et al., Cleveland, United States. In Nat Med, Sep 2015
Here we show that proprotein convertase subtilisin/kexin-6 (PCSK6, also named PACE4; ref. 10) cleaves and activates corin.
Expression of paired basic amino acid-cleaving enzyme 4 (PACE4) correlated with prognosis in non-small cell lung cancer (NSCLC) patients.
New
Zhang et al., Guangzhou, China. In J Thorac Dis, May 2015
BACKGROUND: Paired basic amino acid-cleaving enzyme 4 (PACE4) was shown to enhance tumor cells proliferation and invasive.
PACE4 inhibitors and their peptidomimetic analogs block prostate cancer tumor progression through quiescence induction, increased apoptosis and impaired neovascularisation.
New
Day et al., Sherbrooke, Canada. In Oncotarget, Mar 2015
As a fundamentally new approach, we propose the inhibition of PACE4, a member of the proprotein convertases family of enzymes, as a therapeutic target in prostate cancer.
Liver-Specific Inactivation of the Proprotein Convertase FURIN Leads to Increased Hepatocellular Carcinoma Growth.
Creemers et al., Leuven, Belgium. In Biomed Res Int, 2014
In a mouse model for HCC expression of Furin was not altered in the tumors, while those of PC7, PC5/6, and PACE4 significantly decreased, at least at some time points.
Multi-Leu PACE4 Inhibitor Retention within Cells Is PACE4 Dependent and a Prerequisite for Antiproliferative Activity.
Day et al., Sherbrooke, Canada. In Biomed Res Int, 2014
The overexpression as well as the critical implication of the proprotein convertase PACE4 in prostate cancer progression has been previously reported and supported the development of peptide inhibitors.
PACE4 regulates apoptosis in human prostate cancer cells via endoplasmic reticulum stress and mitochondrial signaling pathways.
Guo et al., Beijing, China. In Drug Des Devel Ther, 2014
BACKGROUND: PACE4 is a proprotein convertase capable of processing numerous substrates involved in tumor growth, invasion, and metastasis.
The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions.
Review
Mbikay et al., Montréal, Canada. In J Biol Chem, 2013
The secretory proprotein convertase (PC) family comprises nine members: PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9.
A role for PACE4 in osteoarthritis pain: evidence from human genetic association and null mutant phenotype.
GeneRIF
Mogil et al., Chicago, United States. In Ann Rheum Dis, 2012
A variant in PCSK6 is strongly associated with protection against pain in knee osteoarthritis.
The biology and therapeutic targeting of the proprotein convertases.
Review
Impact
Prat et al., Montréal, Canada. In Nat Rev Drug Discov, 2012
Seven of these (proprotein convertase 1 (PC1), PC2, furin, PC4, PC5, paired basic amino acid cleaving enzyme 4 (PACE4) and PC7) activate cellular and pathogenic precursor proteins by cleavage at single or paired basic residues, whereas subtilisin kexin isozyme 1 (SKI-1) and proprotein convertase subtilisin kexin 9 (PCSK9) regulate cholesterol and/or lipid homeostasis via cleavage at non-basic residues or through induced degradation of receptors.
Identification and functional validation of CDH11, PCSK6 and SH3GL3 as novel glioma invasion-associated candidate genes.
GeneRIF
Riemenschneider et al., Düsseldorf, Germany. In Neuropathol Appl Neurobiol, 2012
PCSK6 as a novel glioma invasion-associated candidate gene that likely contribute to the invasive phenotype of malignant gliomas.
The microenvironment patterns the pluripotent mouse epiblast through paracrine Furin and Pace4 proteolytic activities.
GeneRIF
Constam et al., Lausanne, Switzerland. In Genes Dev, 2011
Furin and Pace4 are released by the extraembryonic microenvironment, and that they cleave a membrane-bound reporter substrate in adjacent epiblast cells and activate Nodal to maintain pluripotency
Pcsk6 mutant mice exhibit progressive loss of ovarian function, altered gene expression, and formation of ovarian pathology.
GeneRIF
Nachtigal et al., Halifax, Canada. In Reproduction, 2011
PCSK6 activity plays a role in maintaining normal cellular and tissue homeostasis in the ovary.
What lies ahead for the proprotein convertases?
Review
Seidah, Montréal, Canada. In Ann N Y Acad Sci, 2011
Limited proteolysis of secretory proteins is performed by one or more of the nine-membered proprotein convertase (PC) family: PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9.
PCSK6 is associated with handedness in individuals with dyslexia.
GeneRIF
Monaco et al., Oxford, United Kingdom. In Hum Mol Genet, 2011
In a genome-wide association study of handedness in patients with dyslexia, PCSK6 was the most highly associated marker.
The proprotein convertases, 20 years later.
Review
Seidah, Montréal, Canada. In Methods Mol Biol, 2010
The family of PCs comprises nine members, PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9 (Fig. 3.1).
Salivary gland development: its mediation by a subtilisin-like proprotein convertase, PACE4.
Review
Hosoi et al., Tokushima, Japan. In J Med Invest, 2008
Here, we focused upon the physiological role of PACE4 (SPC4), a member of SPC family, in the SMG development.
Extraembryonic proteases regulate Nodal signalling during gastrulation.
Impact
GeneRIF
Constam et al., China. In Nat Cell Biol, 2002
Spc4 regulates Nodal signalling during gastrulation
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