3.4.22.37: gingipain R
This is an abbreviated version!
For detailed information about gingipain R, go to the full flat file.
Word Map on EC 3.4.22.37
-
3.4.22.37
-
porphyromonas
-
gingivalis
-
periodontal
-
proteinases
-
adhesins
-
lysine-specific
-
hemagglutinins
-
hemagglutination
-
protease-activated
-
keystone
-
periodontopathogenic
-
fimbriae
-
crevicular
-
diagnostics
-
actinomycetemcomitans
-
biotechnology
-
molecular biology
-
forsythia
-
johnsoniae
-
periodontopathic
-
gingivalis-induced
-
black-pigmented
-
par-2
-
subgingival
-
peptidylarginine
-
tooth-supporting
-
tannerella
-
gliding
-
autoaggregation
-
medicine
-
pharmacology
-
drug development
-
lys-specific
- 3.4.22.37
- porphyromonas
- gingivalis
- periodontal
- proteinases
- adhesins
-
lysine-specific
- hemagglutinins
-
hemagglutination
-
protease-activated
-
keystone
-
periodontopathogenic
-
fimbriae
-
crevicular
- diagnostics
- actinomycetemcomitans
- biotechnology
- molecular biology
- forsythia
- johnsoniae
-
periodontopathic
-
gingivalis-induced
-
black-pigmented
- par-2
-
subgingival
-
peptidylarginine
-
tooth-supporting
-
tannerella
-
gliding
-
autoaggregation
- medicine
- pharmacology
- drug development
-
lys-specific
Reaction
hydrolysis of proteins and small molecule substrates, with a preference for Arg in P1 =
Synonyms
Arg gingipain, Arg-gingipain, Arg-gingipain A, Arg-gingipain B, Arg-gingipains B, Arg-gingivain-55 proteinase, Arg-gingivain-70 proteinase, Arg-gingivain-75 proteinase, Arg-gingivain-specific proteinase, Arg-ginigipain A, Arg-ginigipain B, Arg-specific cysteine protease, Arg-specific cysteine proteinase, Arg-specific cysteine proteinase gingipain, Arg-specific gingipain, Arg-specific gingipain protease, Arg-X proteinase, Arg-X-specific Arg gingipain, Argingipain, arginine gingipain, arginine-gingipain, Arginine-specific cysteine protease, arginine-specific cysteine proteinase, Arginine-specific gingipain, arginine-specific gingipain 2, arginine-specific gingipain B, arginine-specific gingipain proteinase, Arginine-specific gingivain, arginine-X specific cysteine proteinase, gingipain, gingipain B, gingipain R, gingipain R1, gingipain R2, Gingipain-1, gingipain-R, Gingivain, arginine-specific, high molecular mass arginine-specific gingipain A, high molecular weight gingipain A, high-molecular-mass arginine-specific gingipain, HRgpA, HrgpB, low molecular weight gingipain B, More, mt-RgpA, mt-RgpB, RgB, RGP, Rgp proteinase, RGP-1, RGP-2, RgpA, RgpA proteinase, RgpA(cat), RgpB
ECTree
3.4.22.37 gingipain RAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.22.37 - gingipain R
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-globin + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because alpha-globin is not soluble at neutral pH
-
?
alpha-thrombin + H2O
beta-thrombin B-1 and B-2 chains
-
HRgpA and RgpB, cleavage of peptide bond R383-N394
-
?
apoB-100 protein + H2O
?
-
apoB-100 degradation induces LDL-modification and contributes to the onset of atherosclerosis
-
-
?
benzoyl-Arg 4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
Benzoyl-Ile-Glu-(gamma-ornithyl)-Gly-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
benzoyl-Phe-Val-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Val-Gly-Arg-4-nitroanilide + H2O
benzoyl-Val-Gly-Arg + 4-nitroaniline
-
-
-
?
beta-globin + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because beta-globin is not soluble at neutral pH
-
?
beta-thrombin B-2 chain + H2O
?
-
HRgpA and RgpB, substrate inactivation and degradation
-
?
butoxy-carbonyl-O-benzyl-Ser-Gly-Arg-4-nitroanilide + H2O
butoxy-carbonyl-O-benzyl-Ser-Gly-Arg + 4-nitroaniline
-
best sythetic substrate
-
?
butoxy-carbonyl-Val-Leu-Gly-Arg-4-nitroanilide + H2O
butoxy-carbonyl-Val-Leu-Gly-Arg + 4-nitroaniline
-
-
-
?
CBZ-Phe-Arg-4-methyl-coumaryl-7-amide + H2O
CBZ-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
CD27 protein + H2O
?
-
involved in reduction of T-cell function, effective even in the presence of 2.5 or 5% serum
-
-
?
cell adhesion molecule + H2O
?
-
involved in the detachment of endothelial cells
-
-
?
denatured alpha1-proteinase inhibitor + H2O
?
-
-
?
factor IX proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
factor X proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
fibrinogen A alpha-chain + H2O
28 kDa fragment + ?
-
major cleavage site at position 22, all isoforms
the 28 kDa fragment is the major product of isoform HRgpA
?
fibrinogen B beta-chain + H2O
?
-
high activity of isoform HRgpA, which performs cleavage at 2 positions: 42 and 44
-
?
Fibronectin + H2O
?
-
the enzyme isoforms HRgpA and RgpB effectively destroy the cell-binding domain of fibronectin
-
-
?
haemoglobin + H2O
?
-
complete digestion, enzyme form RGP-B shows high activity, not RGP-A, human substrate
-
?
Leu-Tyr-Arg-4-nitroanilide + H2O
Leu-Tyr-Arg + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Lysozyme + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds
-
?
N-alpha-benzoyl-D,L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine 4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
N-alpha-benzoyl-DL-Lys-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Lys + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-benzoyl-L-arginine-4-nitroanilide + H2O
N-benzoyl-L-arginine + 4-nitroaniline
-
-
-
?
N-cadherin + H2O
?
-
in BCAEC cells, cleavage by HRgpA but not RgpB
-
-
?
Nalpha-benzoyl-D,L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-D,L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-D,L-arginine 4 nitroanilide + H2O
Nalpha-benzoyl-D,L-arginine + 4 nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
prefimbrillin + H2O
fimbrilline + ?
-
-
mature form of the protein
-
?
protease-activated receptor-1 + H2O
?
-
specific substrate for Arg-gingipain
-
-
?
prothrombin + H2O
alpha-thrombin + 2 peptide fragments
-
major cleavage sites of HRgpA are R271-T272, R320-I321, and R155-S156, activation of human substrate, HRgpA possesses adhesion domains and is about 20fold more active than the single chain RgpB
high amount od alpha-thrombin
?
prothrombin + H2O
alpha-thrombin + prethrombin 1 + prethrombin 2 + 1 peptide fragments
-
major cleavage sites of RgpB are R155-S156 and R271-T272, while the peptide bond R320-I321 is not efficiently cleaved resulting in about 20fold slower reaction, activation of human substrate, less active than HRgpA
low amount of alpha-thrombin
?
prothrombin + H2O
thrombin + ?
-
HRgpA, involved in fibrinogen clotting
-
?
RgpA-HagA polyprotein + H2O
?
-
processing of the precursor by Rgp
-
-
?
ribonuclease A + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds
-
?
t-butyloxycarbonyl-L-leucylglycyl-L-arginine-4-metylcoumaryl-7-amide + H2O
?
-
-
-
-
?
thrombomodulin + H2O
?
-
Lys-gingipain and Arg-gingipain cleave thrombomodulin in vitro
-
-
?
toluenesulfonyl-glycyl-L-prolyl-L-arginine-4-nitroanilide + H2O
toluenesulfonyl-glycyl-L-prolyl-L-arginine + 4-nitroaniline
-
-
-
?
tosyl-Gly-L-Pro-L-Arg 4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg 4-nitroaniline
-
-
-
-
?
tosyl-GPR-4-nitroanilide + H2O
tosyl-GPR + 4-nitroaniline
other substrates with a Ps proline are very poor substrates, synthetic fluorogenic substrate
-
?
transferring receptor + H2O
?
-
Rgp is responsible for transferring receptor degradation
-
-
?
Z-Arg-Arg-4-nitroanilide + H2O
Z-Arg-Arg + 4-nitroaniline
synthetic fluorogenic substrate
-
?
alpha chains of haptoglobin + H2O
?
-
low activity, hemoglobin protects
-
?
alpha chains of haptoglobin + H2O
?
-
low activity, hemoglobin protects
-
?
alpha1-Antichymotrypsin + H2O
?
inactivation of the substrate
-
?
alpha1-Antichymotrypsin + H2O
?
inactivation of the substrate
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O
AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
-
-
-
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O
AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
-
-
-
-
?
azocasein + H2O
?
synthetic chromogenic substrate
-
?
azocasein + H2O
?
synthetic chromogenic substrate
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells) with RgpB being far more efficient than other gingipains. RgpB efficiently inactivates the inhibitory activity of elafin at subnanomolar concentrations through proteolysis limited to the Arg22-Cys23 peptide bond within the surface loop harboring the inhibitor active site
-
-
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 47 kDa, products of 23 kDa and 40 kDa in serum
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 47 kDa, products of 23 kDa and 40 kDa in serum
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
PAR-2 activation on epithelial cells
-
-
?
interferon gamma + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin 12 + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain, EC 3.4.22.47
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O
methaemoglobin + ?
-
data indicate direct product formation without the occurrence of intermediates
-
-
?
oxyhaemoglobin + H2O
methaemoglobin + ?
-
data indicate direct product formation without the occurrence of intermediates
-
-
?
RgpA-Hgp polyprotein + H2O
?
-
processing of the precursor by Rgp
-
-
?
RgpA-Hgp polyprotein + H2O
?
-
processing of the precursor by Rgp, Porphyromonas gingivalis-induced platelet aggregation in platelet-rich plasma depends on processed Hgp44 adhesin but not directly on Rgp proteinase, the adhesin is also processed by Lys-gingipain Kgp, EC 3.4.22.47
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
reduction of the protective effect of SLPIon neutrophil proteases and bacterial proinflammatory compounds
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
recombinant protein, reaction catalyzed by RgpA and RgpB
-
-
?
TNFalpha + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
TNFalpha + H2O
?
-
inactivation by degradation of human TNFalpha on host cell surface and recombinant fibroblast cell surface, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
TNFalpha + H2O
?
-
degradation, high activity with HRgpA, moderate activity with RgpB
-
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
-
hydrolysis of synthetic chromogenic substrates with arginine in the P1 position
-
-
?
additional information
?
-
-
no activity of both enzyme forms with toluenesulfonyl-glycyl-L-prolyl-L-lysine-4-nitroanilide, Val-Leu-Lys-4-nitroanilide, benzoyl-Lys-4-nitroanilide, succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, glutaryl-Phe-4-nitroanilide, benzoyl-Tyr-4-nitroanilide, and Lys-4-nitroanilide, activity with chromogenic synthetic substrates is limited to those with arginine in the P1-position
-
?
additional information
?
-
-
substrate specificity for the C-terminal position next to the cleavage site of the different enzyme forms, overview
-
?
additional information
?
-
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
-
the enzyme makes a significant contribution to the virulence of Porphyromonas gingivalis
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains R are potent permeability enhancement factors by prekallikrein activation and bradykinin induction, the enzyme degrades proteins of connective tissue, cell surface proteins and receptors, cytokines and plasma proteins, including components of the coagulation and complement cascades, heme- and iron-binding proteins, immunoglobulins and proteinase inhibitors
-
-
?
additional information
?
-
-
gingipains R mediate coaggregation of Porphyromonas gingivalis with other bacteria, overview
-
-
?
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages
-
-
?
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases cleaving a broad range of in-host proteins
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is specific for peptide substrate with Arg at P1 position, gingipain R performs autoprocessing and activation
-
-
?
additional information
?
-
-
implicated in a wide range of both pathological and physiological processes of Porphyromonas gingivalis, including destruction of periodontal tissue, disruption of host defense mechanisms, processing of bacterial cell surface and secretory proteins, and acquisition of heme and amino acids, involved in atherosclerotic processes
-
-
?
additional information
?
-
-
important for the provision of nutrients for the bacterium in the host organism, destruction of host tissue, modulation of host immune response
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, activation of the C1 complex in serum, degradation of multiple complement components, important factor for the resistance to the bacteriolytic activity of serum
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, involved in the perturbation of host defense and the destruction and invasion of host tissues, degradation of hosts proteins such as ICAM-1m VCAM-1, catenins, and cadherins, involved in the shedding of syndecan-1
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, probably involved in the reduction of T-cell function at periodontal lesion sites, induction of PAR-1 and PAR-2 receptor expression, up-regulation of PAR-4 expression, little effect on PAR-3 expression, increases expression of CD69 and CD25 on T-cells
-
-
?
additional information
?
-
-
involved in the deregulation of the hosts inflammatory response
-
-
?
additional information
?
-
-
involved in the induction of apoptosis in caspase dependent and caspase independent pathway
-
-
?
additional information
?
-
-
involved in the regulation of mRNA expression for the receptor activator of NF-kappaB ligand (RANKL) protein
-
-
?
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
?
additional information
?
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gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs, overview
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gingipains are involved in bacterial adherence to host cells, RgpA binds to adhesin via its adhesin binding domain. Peptide A44 derived from the adhesin domain of RgpA plays a role in binding of Porphyromonas gingivalis to HEP-2 epithelial cells via cell surface receptors, e.g. clathrin, nocodazole and paclitaxel, which disrupt microtubule formation, block the interaction, while genistein does not
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gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
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gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
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HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
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RgpA and RgpB cleave proteins after arginine residues
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enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
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gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
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gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
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gingipains are cysteine proteinases cleaving a broad range of in-host proteins
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gingipains are essential for bacterial virulence and survival
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role of the Sn binding pocket, molecular basis for substrate specificity, overview
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HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
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substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
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substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
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