Inflammation, Vol. 14, No. 2, 1990

R E C O M B I N A N T INTERLEUKIN-1/3 I N T E R A C T S WITH H I G H - A F F I N I T Y RECEPTORS TO ACTIVATE NEUTROPHIL LEUKOTRIENE B 4 SYNTHESIS 1 LARRY BORISH, RAYMOND ROSENBAUM, BRIAN McDONALD, and LANNY J. ROSENWASSER Department of Medicine New England Medical Center Tufts Medical School 750 Washington St. Boston, Massachusetts 02111

Abstract--The capacity of interleukin-I O L d ) to function as a neutrophil (PMN) activator has been the subject of controversy. While IL-1 purified from mononuclear cell supernatants induced PMN activation, these observations have not been confirmed with recombinant IL-1. To document a cellular basis for a putative P M N IL-1 interaction, we investigated the presence of IL-1 receptors on the PMN. Using an [35S]methionine-labeled preparation, specific binding of IL-I to PMNs was demonstrated. Through Scatchard analysis PMNs were calculated to have a mean of 469 +_ 337 receptors per PMN with an affinity (Ka) of 0.32 _+ 0.09 nM. As IL-1 frequently activates arachidonic acid metabolism in other cell types, we investigated eicosanoid production as a putative consequence of the IL-1-PMN interaction. HPLC analysis of extracted supernatants of IL-l-treated PMNs demonstrated the release of l e u k o t r i e n e B 4 (LTB4), its oxidative products, and 5-hydroxyeicosatetraenoic acid (5-HETE). Production of LTB4 was quantified using a commercial RIA. LTB4 secretion increased from 17.2 + 1.1 to 96.7 _+ 16.4 ng, also with 10.0 ng of IL-1. In time-course studies, it was shown that maximal eicosanoid secretion required a 30rain incubation with IL-1. These observations confirm the proinflammatory activity of IL-1 on neutrophils and resolve the controversy concerning a direct effect of ILl on neutrophils. In conclusion, recombinant IL-1/3 interacts with neutrophils through the presence on the PMN of a high-affinity receptor and results in the secretion of arachidonate metabolites.

This work was presented in part at the American Federation for Clinical Research National Meeting, Washington, D.C., May 1988 (Clin. Res. 36:436A). This work was supported by USPHS NIH grants A125173 (L. J. R.), HL33961 (L. J. R.), and A124843 (L. B.). L. J. R. is the recipient of an Allergic Diseases Academic Award (A100595). L. B. is the recipient of a Burroughs Wellcome Developing Investigator Award. Address correspondence and reprint requests to: Dr. Lanny J. Rosenwasser, National Jewish Center for Immunology and Respiratory Diseases, 1400 Jackson St., Denver, Colorado 80206. 151 0360-3997/90/0400-0151 $06.00/0 9 1990 Plenum Publishing Corporation

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INTRODUCTION

Interleukin-1 (IL-1) is a proinflammatory cytokine with multiple activities mediated through its ability to interact with numerous cellular targets (1-3). The ability o f IL-1 to activate neutrophils (PMNs), however, has been the subject o f some controversy. Several studies have reported that highly purified ILl is chemotactic for neutrophils (4-6) and stimulates the respiratory burst (7) and degranulation (8-11). Recently, the molecular cloning o f human IL-1 alpha (rhlL-lot) (12) and beta ( r h l L - 1 / 3 ) ( 1 3 ) peptides has been reported. Using homogenous IL-1 obtained from molecular biological techniques, several investigators have been unable to confirm these earlier observations. Thus, it has recently been reported that rhlL-1 is not chemotactic for PMNs (14-16) nor does it stimulate the respiratory burst (14) or function as a secretagogue (14). However, it has also been reported that rhlL-1/~ is capable of generating thromboxane B 2 release from P M N s (17). To clarify whether IL-1 is capable o f activating P M N s , we investigated the presence o f IL-1 receptors on the neutrophil. In addition, given the importance o f phospholipase A= activation as a mechanism o f many o f the actions of IL-1 on other cell types, we investigated the ability o f IL-1 to activate P M N arachidonic acid metabolism.

MATERIALS

AND METHODS

Neutrophils. PMNs were obtained from volunteer heparinized venous blood through the sequential application of Ficoll-Hypaque centrifugation and 3 % dextran sedimentation. This final preparation is > 97 % pure. Staining with a fluorescein-conjugatedanti-gpIIb/IIIa antibody (obtained courtesy of Dr. Barry S. Coller, SUNY, Stony Brook, New York) demonstrated contamination with fewer than three platelets per PMN. Interleukin-1 Beta. IL-lfl was obtained from Cistron Biotechnology (Pine Brook, New Jersey). This material was purified to homogeneity and contains < 50 pg endotoxin by the Limulus assay. Generation of [35S]Methionine-Labeled IL-I (18). Binding assays were performed with [3SS]methionine-labeled-IL-1/3(35S-IL-1/3)(17.5 kDa molecular weight corresponding to positions 117-269 of the prolL-1/3 sequence), as this internally labeled material has been shown to have all of the biological activity as unlabeled IL-1 (19). SP64 IL-1 (Ml17-269) with an AMV-4, 5' untranslated leader plasmid DNA was linearized by BamHI digestion and transcribed as described (19). Labeled IL-I~ protein was generated via in vitro rabbit reticulocyte lysate translation of plasmid directed transcribed mRNA in the presence of [3~S]methionine(1155 Ci/mmol; ICN Radiochemicals, Irvine, California). The 35S-IL-1 bad a specific activity of 660 Ci/mmol. Binding Assay. PMNs (5 N 106) and a range of concentrations of 3SS-IL-1(0.1-2 nM) were allowed to interact in HBSS supplemented with 0.1% bovine serum albumin, 0.01% sodium azide, and 20 mM HEPES buffer (pH 7.20). Incubations were carried out in quadruplicate for a minimum

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of 4 h at 4~ with constant agitation. Nonspecific binding of 35S-IL-l~ was determined from incubations performed in the additional presence of 100-fold excess of unlabeled ligand. Background binding was determined from PMNs which were interacted with samples prepared by performing translations as above but in the absence of the IL-1 mRNA. At the end of the incubation, the mixture was layered over 0.5 ml silicone oil (General Electric, Waterford, New York) in 1.5 ml Eppendorf tubes. Samples were centrifuged at 15,000g for 2 rain and cell-associated radioactivity counted in an LKB 1219 beta counter (Turku, Finland). The cpm in the mRNA-negative samples were subtracted from both the total and nonspecific bound samples, and Scatchard analysis was performed by the beta counter using a "Fraction Plot" software program. IL-l-lnduced PMN Arachidonate Metabolism. PMNs (5 X 106/m]) were resuspended in HBSS and allowed to incubate with a range of concentrations of rhIL-l~ (0.1-1000 ng) at 37~ in the additional presence of cytochalasin b (5 tzg/ml; Sigma Chemical Co., St. Louis, Missouri). After 1 h, samples were centrifuged and the cell-free supematants were collected. The supematants were either immediately assayed or were stored at - 7 0 ~ under nitrogen for later analysis. Lipid Extraction. Samples were acidified with 2 M citric acid (pH 3.50). Lipid extractions (20, 21) were performed with the addition of 1.5 volumes of chloroform followed by centrifugation at 600g for 5 rain. The chloroform extraction was repeated, and the combined organic fractions were evaporated under nitrogen gas. PgB2 (10 ng) was applied to selected samples to assess the efficiency of the lipid extractions. HPLC Analysis. The extracted lipid was resuspended in 0.1 ml methanol-water (1 : 1; HPLC grade; Fisher Scientific; Boston, Massachusetts) and injected into a Rainin HPLC system. Reversephase HPLC analysis was performed with a 10-cm C 18 Microsorb fatty acid column (Rainin Instrument Co., Woburn, Massachusetts) on a binary gradient HPLC system with a dynamic high-pressure mixer (Rainin) linked to a Macintosh SE computer (22). The eicosanoids were separated using an isocratic solvent system of HPLC grade methanol-water-acetate (75:25:0.1) at a flow rate of 1 ml/min for 15 rain. Elutions were monitored at 270 nm and 237 nm on a variable wavelength UV detector (Gilson Medical Electronics, Wobum, Massachusetts). Integrations and data analysis were performed on a Macintosh SE Computer. Retention times were compared to those of known standards: 5- and 12-hydroxyeicosatetraenoic acid (HETE), leukotriene B 4 (LTB4), 20-hydroxyLTB 4 (20-OH-LTB4), and 20-earboxy-LTB4 (LTB4) (Seragen Inc., Boston, Massachusetts). Peak identification for putative LTB4-containing samples was confirmed by radioimmunoassay. Radioimmunoassays. Samples obtained as above were assayed for LTB4 using a commercially obtained radioimmunoassay (RIA) kit (New England Nuclear, Boston, Massachusetts). The calcium ionophore A23187 (2 • 10 -6 M; Sigma) was applied as a positive control. In subsequent experiments, PMNs were exposed to IL-1 (0.1-10 ng) for varying time intervals (0-60 rain) and cell-free supernatants were collected and assayed for LTB4 as before. Specificity for PMNs. To assess a putative role for platelet contamination, PMNs were stimulated with thrombin (40 units; Sigma) and secreted LTB4, assayed by RIA. In additional studies, platelet-rich plasma was prepared from citrated blood (3.8% sodium citrate; 0.5 ml/4.5 ml blood) and stimulated with rhIL-1/3 (10 ng) and thrombin (40 U). Lipid extractions and HPLC analyses were performed as before and data analyzed in comparison to authentic thromboxane B2 and 12HETE standards (Seragen, Inc.). In further experiments, peripheral blood mononuctear cells (PBMCs) were obtained from the Ficoll-Hypaque centrifugation of heparinized blood and washed. IL-II3 (10 ng) was allowed to interact with cytochalasin b-treated PBMC at a concentration corresponding to the number contaminating our PMN population (1.5 • 105) for 30 min at 37~ LTB4 production was assayed by RIA. Statistics. The mean + SD of replicate experiments is given. Statistical analyses were performed using Student's paired t tests on a Macintosh SE computer with a "Stats View" software program.

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RESULTS

Neutrophil IL-1 Receptors. PMNs were allowed to interact with varying concentrations of [35S]methionine-labeled IL-1 (35S-IL-1) with or without the additional presence of 100-fold excess unlabeled rhlL-1/3. Specific binding of the 35S-IL-1 to PMNs was demonstrated (a representative experiment of five similar results is shown in Figure 1). Scatchard analysis was subsequently performed (inset, Figure 1). PMNs were demonstrated to have a mean of 469 + 337 IL-1 receptors with a binding coefficient (Kd) of 0.32 + 0.09 nM. HPLC Analysis of IL-l-Induced PMN Arachidonate Products. PMNs were exposed to a range of concentrations of IL- 1 for 1 h. Lipids were extracted from the supernatants and arachidonate products analyzed by H P L C in comparison to known standards. Analysis of lipids obtained from resting PMNs revealed small peaks representing LTB4 and 5-HETE, consistent with the artifactual activation of PMNs during the purification process (data not shown) (23, 24). Stimulation with 10 ng IL-1 was associated with substantially larger peaks of LTB 4 and 5-HETE as well as omega oxidation products of LTB4 (a representative experiment of five similar results is shown in Figure 2). Peak areas were integrated, and the data are presented in Table 1. Peak identification for LTB4 was confirmed via RIA (not shown). 6000 -~

Non-specific 9 Specific 9 Total

5000

,~176176 aooom

2000lOOO 100

1000 Concentration IL-1 (pmol)

Fig. 1. Binding of 35S-IL-1 to PMNs. PMNs were allowed to interact with a range of concentrations of 35S-IL-1/3(0.1-2.0 nmol) with or without the additional presence of 100-foldexcess unlabeled IL-1 for 4 h at 4~ Cell-associated 35S-IL-1 was determined after centrifuging samples through silicone oil. Specificbinding was calculated as the difference in cpm between samples with and without the unlabeled IL-1. Scatchard analysis was performed as shown in the insert. A representative experiment is displayed.

Binding and Activation of PMNs by rhlL-lp

155

I

1

'

l

270nm

h2

g

237nm

5

o .Q


97 % PMNs). These PMNs contain fewer than three "satellite" platelets per PMN (35, 36). While a platelet-PMN interaction has been reported (37, 38) and may promote eicosanoid metabolism, we do not believe this mechanism to be relevant for several reasons. Stimulation of our PMN preparation with thrombin, a stimulus of platelet arachidonate metabolism, failed to stimulate LTB4 secretion. Furthermore, exposure of platelet rich plasma to IL-1 did not generate arachidonate products including thromboxane B2 or 12-HETE. While the remaining 3 % of our PMN preparation represented mononuclear cells, stimulation of a comparable concentration of PMN-free mononuclear cells with IL-1 failed to stimulate significant LTB4 production (data not shown). These results are consistent with the observations of Conti et al. (17) that recombinant IL-1 is able to activate PMNs. More recently, however, it has been reported that recombinant IL-1 is unable to mediate PMN secretion or activation of the respiratory burst (14-16). In vivo, recombinant IL-1 in animals is associated with neutrophil accumulation at intradermal sites of injection (39, 40). Intravenous infusion of IL-1 is associated with the development of neutrophilia (41, 42). IL-1 has been shown to be a stimulus of expression of adherence molecules on endothelial cells. Thus, IL-1 may promote PMN accumulation through its ability to stimulate both PMN adherence to EC and diapedesis across EC monolayers (43-46) and not necessarily through a direct effect on the PMNs. However, LTB 4 is a potent stimulus of PMN chemotaxis (47). Thus, our data suggest that LTB4 produced by IL-l-stimulated PMNs will promote the further local accumulation of PMNs. Such "secondary" stimulation of chemotaxis by IL-1 would not have been recognized by traditional chemotaxis assay techniques (14-16).

Binding and Activation of PMNs by rhIL-1l~

159

The numerous studies showing that IL-1 is chemotactic for PMNs and is able to stimulate secretion and respiratory burst activity used IL-1 preparations of various degrees of purification. IL-1 purified from stimulated mononuclear cell supematants, however, may still contain measurable TNF activity (C. A. Dinarello, personal communication). TNF contaminating these preparations may have been sufficient to induce PMN secretion and chemotaxis (16, 48-50). IL6 may also have contaminated an "ultrapure" IL-1 preparation and produced PMN activation (51). More recently, a number of additional monocyte products that activate PMNs have been described, including monocyte-derived neutrophil chemotactic factor (interleukin-8) (52) and a series of peptides termed macrophage-derived inflammatory proteins (MIP) (53, 54). These conflicting observations demonstrate the importance of using molecularly defined reagents in investigations with cytokines. In summary, we have demonstrated the presence of a high-affinity receptor for IL-1 on neutrophils. These receptors were demonstrated to activate PMNs to secrete several eicosanoid products including leukotriene B 4. These observations further demonstrate the inflammatory potential of IL-1 and confirm that the range of activities of this cytokine extends to the neutrophil. Acknowledgments--The authors wish to thank Drs. S. Jobling, P. Auron, and L. Gehrke for the use of the SP64 IL-1 (M,117-269) plasmid with the AMV-4 5' UTL and the technique for producing 35S-labeled mature IL-1. We also thank Dr. G. Gurka for helping with the binding assays and J. Newtown and A. Gonzales for technical assistance with the HPLC. The secretarial assistance of Ms. Julie Irwin is gratefully acknowledged.

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Recombinant interleukin-1 beta interacts with high-affinity receptors to activate neutrophil leukotriene B4 synthesis.

The capacity of interleukin-1 (IL-1) to function as a neutrophil (PMN) activator has been the subject of controversy. While IL-1 purified from mononuc...
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