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5133.Boulay F. Rabiet M.-J. Tardiff M. - fMLP (2000).pdf

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fMLP
FrancËois Boulay*, Marie-JoseÁphe Rabiet and Marianne Tardif
Department of Molecular and Structural Biology, DBMS/BBSI UMR 314 CEA-CNRS CEA,
17 Rue des Martyrs, Grenoble, Cedex 9, F 38054, France
* corresponding author tel: (33)04-76-88-31-38, fax: (33)04-76-88-51-85, e-mail: fboulay@cea.fr
DOI: 10.1006/rwcy.2000.12003.
SUMMARY
N-Formylated peptides are potent activators of phagocytic cells such as neutrophils, monocytes, and
macrophages. By interacting with a cell surface receptor (FPR) they induce chemotaxis, granule enzyme
secretion, and production of toxic oxygen metabolites. The prototypical tripeptide N formyl-Lmethionyl-L-leucyl-L-phenylalanine is referred to as
fMLP and is produced by bacteria (Escherichia coli
and Staphylococcus aureus) and may also derive from
mitochondria. The methyl ester N-formyl-L-Met-LLeu-L-Phe-OMe was crystallized and its structure was
determined. The formylated tripeptide motif is the
minimal structure for an optimal bioactivity. The
bioactivity can be increased by adding amino acids to
the tripeptide module. The action of fMLP can be
antagonized by various peptide analogs, including Nter-butoxycarbonyl-Phe-Leu-Phe-Leu-Phe-OH peptide (t-BOC-peptide), the tripeptide Met-Leu-Phe
with branched carbamates, and cyclic undecapeptide
cyclosporin H (CSH).
BACKGROUND
Discovery
The invention of the Boyden chamber in 1962
(Boyden, 1962) allowed the characterization of a set
of substances isolated from bacterial culture supernatants that promote the migration of phagocytic
cells. Supernatants of Escherichia coli cultures were
found to contain N-formylated di- and tripeptides
that chemoattract mammalian phagocytes in vitro
(Schiffmann et al., 1975a,b). From the systematic
analysis of synthetic peptides, the tripeptide Nformyl-L-methionyl-L-leucyl-L-phenylalanine emerged
as the shortest module able to activate phagocyte
functions with high potency (Showell et al., 1976;
Freer et al., 1980, 1982). A few years later, it was
shown that this peptide is the most potent neutrophil
chemotactic factor produced by Escherichia coli
(Marasco et al., 1984). N-Formylated peptides
derived from mitochondria were also found (Carp,
1982; Shawar et al., 1995).
Alternative names
The prototypical tripeptide N-formyl-L-methionyl-L(N-formyl-L-Met-L-Leu-Lleucyl-L-phenylalanine
Phe-OH) is currently referred to as fMLP. It is also
known as fMLF (using the single-letter codes for
amino acids), as N-formyl-Met-Leu-Phe, CHO-MetLeu-Phe, N-formyl-methionyl-leucyl-phenylalanine,
or as N-formyl peptide.
Structure
Structure±activity studies have allowed the determination of the structural requirements for optimal
biological activity of the tripeptide: (1) A formyl group
is essential on the -amino group of methionine or
norleucine in position 1. Removal or replacement of
the formyl group by an acetyl or an ethyl group
results in a 1000±10,000-fold loss in bioactivity. (2) An
aliphatic residue such as leucine, -aminobutyric acid,
valine, or norvaline is required in position 2 but a
glycine or an alanine results in a dramatic reduction
of the biological activity. (3) Position 3 has a strict
requirement for a phenylalanine.
A high degree of hydrophobicity appears to be a
major determinant for optimal biological activity.
Thus, the benzyl ester or the benzylamide derivatives
1310 FrancËois Boulay, Marie-JoseÁphe Rabiet and Marianne Tardif
of N-formyl-Met-Leu-Phe-OH are about 10-fold
more active than the acid form, but the methyl ester
(N-formyl-L-Met-L-Leu-L-Phe-OMe) is slightly less
active than the parent peptide (reviewed in Ye and
Boulay, 1997).
Main activities and
pathophysiological roles
fMLP is a potent activator of phagocytes such as
neutrophils, monocytes, and macrophages. By reacting with a receptor on the cell surface of these cells, it
induces not only chemotaxis, but also granule enzyme
secretion and the production of toxic oxygen metabolites. N-Formylated peptides and the fMLP receptor
are thought to be part of a system involved in inflammation and in host defense against invading bacteria.
PROTEIN
Description of protein
The most potent neutrophil chemoattractant recovered from E. coli culture supernatants is the tripeptide
N-formyl-L-methionyl-L-leucyl-L-phenylalanine. Its
methyl ester form has a bioactivity similar to that of
the acid form.
Discussion of crystal structure
The crystal structure of the ionic form of N-formylL-Met-L-Leu-L-Phe-OH has not been established but
the methyl ester N-formyl-L-Met-L-Leu-L-Phe-OMe
has been crystallized and its structure determined
(Gavuzzo et al., 1989). The backbone of the methylated peptide is folded at the Leu residue without
intramolecular hydrogen bonds and is extended at the
two external residues. In the solid state, the Leu sidechain is oriented on the same side as the benzene ring
of Phe and on the opposite side of the Met side-chain
(Figure 1).
Although the folded structure found in the solid
state is consistent with molecular modeling studies,
suggesting that folded conformations of fMLP may
be energetically favored, several lines of evidence
indicate that the folded conformation may not be the
preferred conformation recognized by the receptor.
Early studies have tried to define the nature of the
biologically active analogs of the tripeptide N-formylL-Met-L-Leu-L-Phe-OH. From studies using NMR
spectroscopy, it was concluded that the backbone
Figure 1 Perspective view of N-formyl-L-Met-L-Leu-LPhe-OMe. The structure was drawn with the software
INSIGHT using the coordinates determined by Gavuzzo
et al. (1989). Hydrogen atoms in the amide bonds are shown
in gray; carbon atoms are in green; nitrogen atoms are in
blue; oxygen atoms are in red; sulfur is in yellow. (Full
colour figure may be viewed online.)
fMLP 1311
conformation of fMLP in dimethylsulfoxide solution
was an extended and semi-rigid sheet conformation
(Becker et al., 1979). However, the preference of the
fMLP receptor for a -extended conformation was
debated since other studies using circular dichroism
and infrared spectroscopy demonstrated that the
conformation was solvent-dependent. The role of
peptide backbone conformation on the biological
activity of the tripeptide fMLP has been examined
with structurally constrained analogs. The replacement of Leu by 1-aminocyclohexanecarboxylic acid
(Ac6c) at position 2 in the methyl ester of fMLP yields
an analog with a rigid folded type II turn
conformation
(N-formyl-L-Met-Ac6c-L-Phe-OMe)
(Sukumar et al., 1985), whereas incorporation of
dipropylglycine (Dpg) in place of Leu gives an analog
(N-formyl-L-Met-Dpg-L-Phe-OMe) adopting an extended sheet like structure with a slight conformational flexibility both in solution and in the solid
state (Dentino et al., 1991). N-Formyl-L-Met-Dpg-LPhe-OMe was found to be 8-fold more potent than
the methylated parent peptide and 16-fold more
potent than N-formyl-L-Met-Ac6c-L-Phe-OMe to induce the release of -glucuronidase from human
neutrophils. Thus, it appears that the fMLP receptor
has a preference for the extended sheet rather than
for the stereochemically constrained type II turn
folded analog and the unconstrained parent peptide.
CELLULAR SOURCES AND
TISSUE EXPRESSION
Cellular sources that produce
The prototypical N-formyl peptide, CHO-L-Met-LLeu-L-Phe-OH, has been purified from natural
sources. It is the major neutrophil chemoattractant
produced by Escherichia coli (Marasco et al., 1984). A
potent chemoattractant for human monocytes which
contains equimolar amount of methionine, leucine,
isoleucine, and phenylalanine was also purified from
Staphylococcus aureus (Rot et al., 1987). This chemoattractant is likely to begin with a N-formylmethionine since it competes with the prototypical
tripeptide for binding to human monocytes. The
synthetic N-formyl tetrapeptide N-formyl-L-methionyl-L-isoleucyl-L-phenylalanyl-L-leucine emerged as
the most potent activator of human monocytes (Rot
et al., 1987).
Like the bacteria, the mitochondria present in
eukaryotic cells use a N-formylmethionine to initiate
the biosynthesis of several proteins of the mitochondrial respiratory chain. Several lines of evidence
suggest that mitochondria represent a potential
source of chemoattractants. Carp (1982) has shown
that disrupted mitochondria are able to chemoattract
neutrophils and that the chemotactic activity is
mediated by mitochondrial N-formylmethioninecontaining proteins but not by the nonformylated
proteins. More recently, it has been found that Nformylated peptides that derive from the murine
mitochondrially encoded NADP dehydrogenase subunit 1 are potent activators of the release of elastase
from rabbit neutrophils (Shawar et al., 1995). Thus,
at sites of inflammation or tissue damage, cells that
are disrupted may become potential sources of
phagocyte activators through the release of mitochondrial N-formylmethionine-containing proteins.
It has been recently shown that the bronchial secretions of cystic fibrosis patients contain chemoattractants which activate neutrophil chemotaxis, most
likely via the fMLP receptor since the effect is inhibited by the fMLP antagonist N-ter-butoxycarbonylPhe-Leu-Phe-Leu-Phe-OH peptide (Dayer et al.,
1998). However, the nature of the chemotactic factor
has not been formally characterized.
All these findings do not exclude the possibility that
N-formylated peptides are only peptidomimetics for
an as yet undiscovered natural agonist, for instance a
neuropeptide or a lipid. Of interest is the observation
that lipoxin A4 binds with high affinity to a receptor
highly homologous to the N-formyl peptide receptor
also known as FPRL1 (Fiore et al., 1994).
RECEPTOR UTILIZATION
N-Formylated peptides mediate their effects through
a high-affinity plasma membrane receptor known as
FMLP-R and FPR.
IN VITRO ACTIVITIES
In vitro findings
The motif CHO-Met-Leu-Phe-OH is the minimal
structure for an optimal bioactivity but longer peptides built on this module also proved to be highly
potent and not necessarily dependent on the presence
of a formyl group at the N-terminus (Table 1). Recent
studies on the structure±activity of various synthetic
peptides have indicated that the bioactivity can be
increased by adding amino acid residues to the tripeptide module. Positions 4, 5, and 6 can accommodate
various residues and substituents. The tetrapeptide
1312 FrancËois Boulay, Marie-JoseÁphe Rabiet and Marianne Tardif
Table 1 Affinity and bioactivity of N-formylated peptides and derivatives
Peptides
Kd (nM)a
IC50 (nM)b
EC50 (nM)c
CHO-Met-Leu-Phe-OH
0.3±1
0.3
Freer et al., 1982
CHO-Met-Leu-Phe-NHBzl
0.9
Freer et al., 1982
CHO-Met-Nva-Phe-OH
2.8
Freer et al., 1982
CHO-Nle-Leu-Phe-OH
3.4
Freer et al., 1982
CHO-Met-Gly-Phe-OH
400
Freer et al., 1982
References
CHO-Met-Ile-Phe-Leu-OH
0.05
Rot et al., 1987
CHO-Met-Nle-Leu-Phe-Phe-OH
0.1
Gao et al., 1994
Ac-Met-Nle-Leu-Phe-Phe-OH
0.1
Gao et al., 1994
H-Met-Nle-Leu-Phe-Phe-OH
10
Gao et al., 1994
CHO-Met-Leu-Phe-Lys-OH
10
CHO-Nle-Leu-Phe-Nle-Tyr-Lys-OH
"
CHO-Met-Leu-Phe-N -(Pep12)-Lys-OH
d
Freer et al., 1980
1.9
Niedel et al., 1980
1
Boulay et al., 1990b
CHO-Met-Leu-Phe-N"-(2-( p-azidosalicylamido)ethyl-1,30 -dithiopropionyl)Lys-OH
0.28
Allen et al., 1986
CHO-Met-p-benzoyl-L-phenylalaninePhe-Tyr-N"-(fluorescein)-Lys-OH
39
Mills et al., 1998
CHO-Met-Leu-Phe-Phe-N"-(fluorescein)-Lys
0.03
Fay et al., 1993
a
Dissociation constant measured by direct binding of radiolabeled ligands, for instance CHO-Met-Leu-[3H]Phe-OH.
Concentration of peptide required to displace 50% of the specifically bound CHO-Met-Leu-[3H]Phe-OH, or fluorescein-labeled
CHO-Met-Leu-Phe-Lys-OH.
c
Concentration of peptide required to produce 50% of the maximum biological response (lysozyme or -glucuronidase release,
or Ca2+ mobilization).
d
Pep12 refers to the hydrophilic dodecapeptide N-acetyl-SDQALSFLKDYC-OH branched to the cysteine residue via the N"
amino group of lysine with m-maleimido-N hydroxysuccinimide ester.
b
CHO-Met-Leu-Phe-Phe-OH is more active than the
parent tripeptide (Freer et al., 1982). Insertion of a
norleucine between the methionine and the leucine
in the latter tetrapeptide yields a pentapeptide (CHOMet-Nle-Leu-Phe-Phe-OH) with a potency in the
subnanomolar range (Gao et al., 1994). In this pentapeptide the N-formylation of methionine is no longer
a prerequisite. Its N-acetylated form is as active as
the N-formylated counterpart and the unacetylated
H-Met-Nle-Leu-Phe-Phe-OH pentapeptide retains a
high potency, indicating that the bioactivity is not
entirely dependent on the presence of a formyl at the
N-terminus but can be modulated by the side-chain of
internal amino acid residues.
The tetrapeptide CHO-Met-Leu-Phe-Lys-OH, the
pentapeptide CHO-Met-Leu-Phe-Phe-Lys-OH, and
the hexapeptide CHO-Nle-Leu-Phe-Nle-Tyr-Lys-OH
are as active as the prototypical tripeptide fMLP. This
feature proved to be very useful for studying FPR
because the lysine residue could be derivatized either
with a hydrophilic dodecapeptide which renders the
entire molecule highly water soluble (Boulay et al.,
1990b), with bulky hydrophobic photoactivatable
moieties (Niedel et al., 1980; Schmitt et al., 1983;
Allen et al., 1986; Boulay et al., 1990a), or with fluorescent chromophores (Fay et al., 1991, 1993) without
loss of specificity and biological activity.
Regulatory molecules: Inhibitors
and enhancers
The leukocyte responses to fMLP are modulated by
a surface membrane endopeptidase that cleaves the
N-formylated peptide. The neutral endopeptidase
known as CD10/NEP (EC 3.4.24.11) is a cell surface
enzyme that hydrolyzes fMLP and, thereby, reduces
its local concentration and availability for receptor
binding and signal transduction as illustrated in
fMLP 1313
Figure 2 Downregulation of fMLP by CD10/NEP on
leukocyte plasma membrane.
Table 2 Bioassays used to determine the bioactivity of Nformyl peptides
Bioassays
Sensitivity to fMLP
IC50 (nM)
EC50 (nM)
Chemotaxis
0.1±1
Enzyme release
0.3
Lysozyme, -glucuronidase,
N-acetyl--D-glucosaminidase
GTPase activity
5±10
Superoxide production
20±50
Calcium mobilization
1±10
Binding inhibition
(CHO-Met-Leu-(3H)Phe-OH)
10±30
Bioassays used
Figure 2 (Connelly et al., 1985; Yuli and Lelkes, 1991;
Painter and Aiken, 1995). Cell surface CD10/NEP
enzymatic activity is increased by fMLP and other
inflammatory mediators such as TNF, GM-CSF,
and C5a (Shipp et al., 1991; Werfel et al., 1991). Thus,
fMLP appears to regulate its proinflammatory
potential by controlling its own degradation. More
information on CD10/NEP can be obtained in a
review by Shipp and Look (1993).
In vitro, the action of fMLP can be antagonized by
various peptide analogs. For years, the N-ter-butoxycarbonyl-Phe-Leu-Phe-Leu-Phe-OH peptide (t-BOC
peptide) was known as the most potent competitive
antagonist commercially available. It inhibits lysozyme release with an IC50 in the range of 0.2±0.3 mM
(Freer et al., 1980). Specific antagonists with IC50
values ranging between 0.25 and 2 mM were engineered by substituting the N-terminus of the tripeptide Met-Leu-Phe with branched carbamates, such as
iso- and ter-butyloxycarbonyl (Derian et al., 1996).
Unbranched carbamates, such as methoxycarbonyl
and ethoxycarbonyl, resulted in agonist activity.
A completely unrelated peptide, the cyclic undecapeptide cyclosporin H (CSH), an analog of cyclosporin A, has been described as a very selective
antagonist that is about 5-fold more potent than the
t-BOC peptides in inhibiting fMLP-induced cellular
responses (Wenzel-Seifert and Seifert, 1993). CSH
inhibits fMLP-induced calcium mobilization, superoxide production, and -glucuronidase release in
differentiated HL-60 cells with EC50 values of 80 nM,
240 nM, and 450 nM, respectively.
The bioactivity of N-formylated peptides can be measured by several means, as summarized in Table 2.
Neutrophil or monocyte chemotaxis and granule
enzyme release are by far the most sensitive assays to
estimate the potency of N-formylated peptides, most
likely because the triggering of these two responses
requires a low level of receptor occupancy. The
release of N-acetyl--D-glucosaminidase from rabbit
neutrophils is a particularly reproducible method that
is about 100-fold more sensitive than the binding
competition assay (Kermode et al., 1988). Superoxide
anion release is assayed by monitoring the superoxide
dismutase-inhibitable reduction of ferricytochrome C
at 550 nm (Cohen and Chovaniec, 1978). The main
advantage of this assay is its simplicity, but it requires
a maximal level of receptor occupancy and it is less
sensitive than the release of N-acetyl--D-glucosaminidase. Transient increases of intracellular calcium
can be determined after loading FPR-expressing cells
with the fluorescent dye Fura 2. As with the superoxide assay, the N-formylpeptide-mediated calcium
transients are monitored continuously. The determination of GTPase activity in membrane preparation
has been widely used for many agonists. Several variations of the method have recently been described and
discussed (Gierschik et al., 1994). Measurement of
binding inhibition is a reliable approach which is very
useful when the specificity of a new peptide chemoattractant and its relative affinity for FPR have to be
determined. However, this approach is inappropriate
when minute amounts of peptide chemoattractants are
isolated from biological fluids.
1314 FrancËois Boulay, Marie-JoseÁphe Rabiet and Marianne Tardif
IN VIVO BIOLOGICAL
ACTIVITIES OF LIGANDS IN
ANIMAL MODELS
Normal physiological roles
The prevailing model is that N-formylated peptides
initiate neutrophil responses to bacterial invasion of
the host. At sites of tissue necrosis, N-formyl peptides
may be liberated by mitochondria and may trigger the
accumulation of phagocytic cells at these sites.
Pharmacological effects
The effects of the chemotactic factor fMLP have been
mainly examined in rabbits. Early studies suggested
that inhalation of fMLP by rabbits causes a bronchoconstriction and airway inflammation most likely
mediated via the activation of inflammatory cells
(Berend et al., 1986; Peters et al., 1991). In guinea pigs,
aerosol inhalation or intratracheal injection of fMLP
causes a significant infiltration of eosinophils in tracheal mucosa, which is not prevented by PAF antagonists and 5-lipoxygenase inhibitors (Amagai et al.,
1992). In rabbit trachea, fMLP has been shown to
increase microvascular leakage (Matheson et al.,
1997). This effect appears to be mediated by PAF and
leukotrienes C4 and D4 produced upon fMLP
inhalation. Intravenous administration of fMLP in
normal rabbits induces transient and dose-dependent
hypotension, neutropenia, and thrombocytopenia
(Jonsson et al., 1997). It is unclear, however, whether
these effects result simply from neutrophil activation
or from the activation of other cell types that express
FPR or the FPR homolog FPRL1.
Interactions with cytokine network
fMLP triggers the production of a variety of
proinflammatory cytokines and chemokines, including IL-1, IL-6, GM-CSF, and IL-8.
Endogenous inhibitors and
enhancers
Cytokines such as TNF and GM-CSF render
granulocytes more responsive to fMLP, resulting in
increased superoxide production in vitro. This
phenomenon is known as `priming', but the underlying mechanisms are still unclear (Hallett and
Lloyds, 1995). This priming phenomenon is observed
in mice challenged with staphylococcal enterotoxin B.
The treated animals present an acute inflammatory
lung injury, a high level of TNF in serum, and their
peripheral blood granulocytes respond with an
increased production of toxic oxygen metabolites
upon fMLP exposure. This priming effect may
increase the tissue-damaging potential of granulocytes when recruited in lungs of staphylococcal
enterotoxin B-treated mice (Neumann et al., 1997).
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LICENSED PRODUCTS
N-Formyl peptides can be purchased from Sigma;
Cyclosporin H can be obtained from Novartis
Pharmacia AG, Research, CH 4002 Basel,
Switzerland
(contact
Anna
Maria
Suter,
Anna_Maria.Suter@pharma.novartis.com).
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