Cell-surface expression of a new splice variant of the mouse signal peptide peptidase

2006 ◽  
Vol 1759 (3-4) ◽  
pp. 159-165 ◽  
Author(s):  
Jens Urny ◽  
Irm Hermans-Borgmeyer ◽  
H. Chica Schaller
Keyword(s):  
Cell Surface ◽  
Signal Peptide ◽  
Splice Variant ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Signal Peptide Peptidase

scholarly journals The PAR2 signal peptide prevents premature receptor cleavage and activation

2019 ◽  
Author(s):  
Belinda Liu ◽  
Grace Lee ◽  
Jiejun Wu ◽  
Janise Deming ◽  
Chester Kuei ◽  
...  
Keyword(s):  
Cell Surface ◽  
Signal Peptide ◽  
Synthetic Peptide ◽  
Surface Expression ◽  
Receptor Expression ◽  
Cell Surface Receptor ◽  
Cell Surface Expression ◽  
Peptide Ligand ◽  
Protease Activated Receptors ◽  
N Terminus

AbstractUnlike closely related GPCRs, protease-activated receptors (PAR1, PAR2, PAR3, and PAR4) have a predicted signal peptide at their N-terminus, which is encoded by a separate exon, suggesting that the signal peptides of PARs may serve an important and unique function, specific for PARs. In this report, we show that the PAR2 signal peptide, when fused to the N-terminus of IgG-Fc, effectively induced IgG-Fc secretion into culture medium, thus behaving like a classical signal peptide. The presence of PAR2 signal peptide has a strong effect on PAR2 cell surface expression, as deletion of the signal peptide (PAR2ΔSP) led to dramatic reduction of the cell surface expression and decreased responses to trypsin or the synthetic peptide ligand (SLIGKV). However, further deletion of the tethered ligand region (SLIGKV) at the N-terminus rescued the cell surface receptor expression and the response to the synthetic peptide ligand, suggesting that the signal peptide of PAR2 may be involved in preventing PAR2 from intracellular protease activation before reaching the cell surface. Supporting this hypothesis, an Arg36Ala mutation on PAR2ΔSP, which disabled the trypsin activation site, increased the receptor cell surface expression and the response to ligand stimulation. Similar effects were observed when PAR2ΔSP expressing cells were treated with protease inhibitors. Our findings indicated that these is a role of the PAR2 signal peptide in preventing the premature activation of PAR2 from intracellular protease cleavage before reaching the cells surface. The same mechanism may also apply to PAR1, PAR3, and PAR4.

scholarly journals Microbial Disease Spectrum Linked to a Novel IL-12Rβ1 N-Terminal Signal Peptide Stop-Gain Homozygous Mutation with Paradoxical Receptor Cell-Surface Expression

2017 ◽  
Vol 8 ◽  
Author(s):  
Thais Louvain de Souza ◽  
Regina C. de Souza Campos Fernandes ◽  
Juliana Azevedo da Silva ◽  
Vladimir Gomes Alves Júnior ◽  
Adelia Gomes Coelho ◽  
...  
Keyword(s):  
Cell Surface ◽  
Signal Peptide ◽  
Receptor Cell ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Homozygous Mutation ◽  
Disease Spectrum ◽  
Microbial Disease

scholarly journals Human Cytomegalovirus UL40 Signal Peptide Regulates Cell Surface Expression of the NK Cell Ligands HLA-E and gpUL18

2012 ◽  
Vol 188 (6) ◽  
pp. 2794-2804 ◽  
Author(s):  
Virginie Prod’homme ◽  
Peter Tomasec ◽  
Charles Cunningham ◽  
Marius K. Lemberg ◽  
Richard J. Stanton ◽  
...  
Keyword(s):  
Cell Surface ◽  
Human Cytomegalovirus ◽  
Signal Peptide ◽  
Nk Cell ◽  
Surface Expression ◽  
Cell Surface Expression

Partial expression defect for the SCN5A missense mutation G1406R depends on splice variant background Q1077 and rescue by mexiletine

2006 ◽  
Vol 291 (4) ◽  
pp. H1822-H1828 ◽  
Author(s):  
Bi-Hua Tan ◽  
Carmen R. Valdivia ◽  
Chunhua Song ◽  
Jonathan C. Makielski
Keyword(s):  
Cell Surface ◽  
Current Density ◽  
Splice Variant ◽  
Splice Variants ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Loss Of Function ◽  
Mutant Channel ◽  
Hek 293 ◽  
293 Cells

Mutations in the cardiac Na+ channel gene SCN5A cause loss of function and underlie arrhythmia syndromes. SCN5A in humans has two splice variants, one lacking a glutamine at position 1077 (Q1077del) and one containing Q1077. We investigated the effect of splice variant background on loss of function and rescue for G1406R, a mutation reported to cause Brugada syndrome. Mutant and wild-type (WT) channels in both backgrounds were transfected into HEK-293 cells and incubated for up to 72 h with and without mexiletine. At 8 h, neither current nor cell surface expression was observed for the mutant in either background, but both were present in WT channels. At 24 h, small (<10% compared with WT) currents were noted and accompanied by cell surface expression. At 48 h, current density was ∼40% of WT channels for the mutant in the Q1077del variant background but remained at <10% of WT channels in Q1077. Current levels were stable by 72 h. Coexpression with β1- or β3-subunits or insertion of the polymorphism H558R in the background did not significantly affect current expression. Mexiletine restored current density of the mutant channel in both backgrounds to nearly WT levels. The mutant channels also showed a negative shift in inactivation, slower recovery, and enhanced slow inactivation, consistent with a loss of function phenotype. These data show that a trafficking defect may be partial and time dependent and may differ with the splice variant background. Also, expression defects and gating abnormalities may contribute to loss of function for the same mutation.

Persistent HIV Transcription Induces Sialyl-Lewis-X Glyco-Antigen Cell-Surface Expression

2020 ◽  
Author(s):  
Florent Colomb ◽  
Leila B. Giron ◽  
Leticia Kuri Cervantes ◽  
Tongcui Ma ◽  
Samson Adeniji ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Expression ◽  
Sialyl Lewis X ◽  
Cell Surface Expression ◽  
Lewis X ◽  
Hiv Transcription ◽  
Sialyl Lewis
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