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The Journal of Immunology, 1998, 161: 1594-1597.
Copyright © 1998 by The American Association of Immunologists

CUTTING EDGE

Cutting Edge: Identification of an Additional Isoform of STAT5 Expressed in Immature Macrophages1

Mary A. Lokuta2,3, Mary Ann McDowell2,4 and Donna M. Paulnock5

Department of Medical Microbiology and Immunology, University of Wisconsin Medical School, Madison, WI 53706


   Abstract
Top
 Abstract
Introduction
 Materials and Methods
 Results
 Discussion
 References
 
We are interested in understanding the molecular basis of macrophage (M{phi}) differentiation and activation by cytokines. Recent reports have suggested that the transcription factor STAT5 may play a role in M{phi} differentiation. In the experiments described here, we assessed the expression of STAT5-related molecules in three M{phi} cell lines, RAW 264.7, WEHI-3, and WEHI-3D+, which represent different stages of M{phi} maturation, and also in primary peritoneal and bone marrow M{phi} from BALB/c mice. The studies revealed that the previously characterized STAT5a and STAT5b isoforms are detectable at both the mRNA and protein levels in these M{phi} populations. Additional STAT5-related proteins were detected by immunoblot analysis and were preferentially expressed in both the immature WEHI-3 cell population and the adherent bone marrow population containing immature M{phi}. These results identify new isoforms of STAT5 and demonstrate that distinct patterns of expression of STAT5-related proteins are observed in M{phi} at different stages of maturation.


   Introduction
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 Abstract
 Introduction
Materials and Methods
 Results
 Discussion
 References
 
The importance of the Janus kinase-STAT signaling pathway in the initiation of the response to IFN-{gamma} and other cytokines has been recognized for several years (1). This pathway includes a network of latent cytoplasmic factors, which are termed STAT proteins. STAT proteins are activated through specific phosphorylation events following ligand-receptor interaction and ultimately function as the transcriptional activators of target genes through the use of specific DNA regulatory elements. Currently, at least seven mouse and human STAT proteins have been identified. An analysis of hemopoietic receptor signaling actions has indicated that the specificity of cytokine signaling involves the recruitment of specific subsets of kinases and STATs. Thus, characterization of the pathway components involved in cytokine responses in specific cell types is critical for a complete understanding of the transcriptional control of cytokine stimulation.

Typically, STAT proteins activate target genes through the use of a DNA element called the {gamma}-activated site. Recent reports have demonstrated that the transcription factor STAT5, which was originally identified as a ß-casein promoter-binding factor in sheep mammary gland tissue (2), can interact with the {gamma}-activated site element to stimulate gene transcription (3, 4, 5). The expression of several STAT5-related proteins has been identified in myeloid cells, including the isoforms STAT5a and STAT5b (3, 6) and a differentiation-induced factor (7, 8). These results suggest that members of the STAT5 family may play a role in myeloid cell differentiation and/or activation.

In the experiments described here, we assessed the expression of STAT5-related molecules in three macrophage (M{phi})6 cell lines, RAW 264.7, WEHI-3, and WEHI-3D+, which is cell line derived from WEHI-3, as well as in primary peritoneal and bone marrow (BM) M{phi}. Studies by us and others have determined that the three cell lines represent different stages of M{phi} maturation (8, 9). While all primary M{phi} tissue populations are heterogenous, elicited peritoneal M{phi} largely are representative of mature tissue M{phi}; BM populations contain a heterogeneous mixture of M{phi} populations that includes immature cells. Our results with the cell lines demonstrate that the previously characterized isoforms of STAT5a and STAT5b were detectable at both the mRNA and protein levels in these M{phi} populations. However, the relative levels of expression of the STAT5a and STAT5b proteins differed dramatically in the three cell populations, with the more mature RAW 264.7 and WEHI-3D+ cell lines expressing the higher molecular mass (or full-length) proteins and the less mature WEHI-3 cells expressing the smaller isoforms (3, 6). Two previously undescribed STAT5-related proteins were also detected in these studies and were preferentially expressed in the immature WEHI-3 cell population. A similar analysis of adherent peritoneal and BM cells that had been isolated from BALB/c mice revealed that the less mature BM population also expressed the novel isoforms of STAT5. These results identify new members of the STAT5 transcription factor family and demonstrate that distinct patterns of expression of STAT5-related proteins can be observed in M{phi} at different stages of maturation.


   Materials and Methods
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 Abstract
 Introduction
 Materials and Methods
Results
 Discussion
 References
 
Cells and cell culture

The murine M{phi} cell lines RAW 264.7 and WEHI-3 were obtained from American Type Culture Collection (Manassas, VA). The WEHI-3D+ cells were a kind gift of Dr. Malcolm Moore (Columbia University, New York, NY) (10). Cells were maintained and activated as described previously (9). Primary M{phi} were obtained from the peritoneal cavity and BM of BALB/c mice. Peritoneal M{phi} were obtained after mice had been injected i.p. with 1.0 ml of a sterile 10% (w/v) solution of thioglycolate (Difco, Detroit, MI), as described previously (11). Harvested cells were plated at a density of 12 to 14 x 106 cells/ml in complete medium in 100-mm tissue culture plates (Costar, Cambridge, MA) and were allowed to adhere for 1 h at 37°C. Nonadherent cells were removed by vigorous washing of the monolayer, and the remaining adherent M{phi} were lysed as described below. BM M{phi} were obtained by flushing BALB/c femurs with RPMI 1640 medium containing 5% FBS as described previously (12). The marrow plugs were made into a single-cell suspension, gravity sedimented for 5 min, and plated at a density of 1.0 x 106 cells/ml in 100-mm tissue culture dishes (Costar). Following 2 h of adherence at 37°C, the nonadherent cells were removed, and the remaining adherent M{phi} were lysed as described below.

Reagents

STAT5-reactive proteins were detected using a pan-STAT5-reactive mAb that was generated in mice against amino acids 451–649 of the sheep STAT5 molecule (Transduction Laboratories, Lexington, KY). This mAb was used at a dilution of 1:250 as recommended by the manufacturer. Polyclonal Ab to mouse ß-actin (Sigma, St. Louis, MO) was used at 1:500. Horseradish peroxidase (HRP)-conjugated anti-mouse IgG (Transduction Laboratories) and HRP-conjugated anti-rabbit IgG (Bio-Rad, Hercules, CA) were used as secondary Abs at dilutions of 1:5,000 and 1:10,000, respectively.

Immunoblot analysis

Cell lysates were prepared using a standard Nonidet P-40 lysis buffer containing 1 µg/ml leupeptin, 1 µg/ml aprotinin, and 10 µg/ml pepstatin A (all from Sigma) as protease inhibitors or were directly lysed and boiled in SDS sample buffer. Subsequently, proteins were separated by SDS-PAGE, transferred electrophoretically to nitrocellulose membranes (Micron Separations, Westborough, MA), and analyzed by immunoblot assay. Bound Ab was detected by autoradiography of chemiluminescent signals using the Lumi-glo system according to the manufacturer’s instructions (Kirkegaard & Perry Laboratories, Gaithersburg, MD). m.w. determinations were performed using SigmaGel for Windows 95 (version 1.05, Jandel Scientific, San Rafael, CA) and were calibrated to the migration of biotinylated m.w. standards (Bio-Rad).

RT-PCR analysis

Total RNA was harvested from stimulated cells using RNA STAT-60 (Tel-Test, Friendswood, TX) according to the manufacturer’s instructions. To ensure that the preparation was free of genomic DNA, the RNA was treated with RNase-free DNase I (Sigma) and repurified with RNA STAT-60 before RT-PCR amplification, as described previously (9). RT-PCR was performed as described previously (9) using an MJ Research thermocycler (Watertown, MA); primers were annealed at 55°C and subjected to 30 rounds of amplification. PCR-amplified products were separated by electrophoresis in a 4% acrylamide gel in 1x TBE (Tris-borate EDTA; 0.09 M Tris-borate, 2 mM EDTA, pH 8.0) and visualized by ethidium bromide staining. The glyceraldehyde-3-phosphate dehydrogenase primers were purchased from Clontech Laboratories (Palo Alto, CA). The STAT5a and STAT5b primers were designed in our laboratory using Oligo 4.0 software for Macintosh (National Biosciences, Plymouth, MN). The primer sequences used for STAT5a were: sense: 5'-CTT GCG AAA GCA GTT GAC GGA-3'; antisense: 5'-GGA CAG GGA GCT TCT AGC GGA-3'. The primer sequences used for STAT5b were: sense: 5'-CCC TGT GAG CCC GCA ACT GCG-3'; antisense: 5'-TGA CTG TGC GTG AGG GAT CCA-3'.

The primers listed above for STAT5a amplify the region between nucleotides 2152 and 2473, generating a PCR product of 321 bp; the primers for STAT5b amplify the region between nucleotides 2156 and 2456, generating a 300-bp product. The regions amplified are at the C terminus of both STAT5a and STAT5b and flank the tyrosine phosphorylation sites. The size difference of the PCR products was determined using SigmaGel for Windows 95 (version 1.05) and were calibrated with a 20-bp DNA standard (Bio-Rad).


   Results
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 Abstract
 Introduction
 Materials and Methods
 Results
Discussion
 References
 
Initial experiments documented that both the RAW 264.7 and WEHI-3 M{phi} cell lines expressed STAT5a and STAT5b proteins (Fig. 1Go). Immunoblot analysis using the pan-STAT5 Ab revealed the presence of both STAT5a and STAT5b isoforms, which were present as 94-kDa and 77-kDa components and as 96-kDa and 80-kDa components, respectively. There was a dramatic difference in the levels of expression seen in the two cell populations. RAW 264.7 cells clearly expressed high levels of the p96 and p94 full-length isoforms and low levels of the p80 and p77 truncated isoforms. WEHI-3 cells exhibited the reverse pattern, expressing high levels of p80/p77 in the absence of readily detectable levels of p96/p94 (Fig. 1Go). Different methods of cell lysate preparation did not change the pattern of isoform expression (data not shown). Under the conditions of lysate preparation and immunoblot analysis used for these studies, there was no detection of a STAT5-reactive band with the molecular mass previously described for the differentiation-induced factor molecule (112 kDa) (8).



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  		FIGURE 1. Expression of STAT5 protein isoforms in WEHI-3 and RAW 264.7 cells. Cell lysates from WEHI-3 or RAW 264.7 cells (60 µg/lane) were separated on a 10% SDS-PAGE gel and transferred to nitrocellulose for immunoblot analysis. Membranes were incubated with appropriate Abs to STAT5 or ß-actin, followed by the appropriate secondary Ab that had been conjugated to HRP. Bound Ab was detected by autoradiography following incubation of the membrane with a luminol substrate.

 
In addition to the presence of the known isoforms of STAT5, further analysis of the immunoblots revealed the presence of a previously undetected STAT5-reactive protein that was expressed specifically in WEHI-3 cells (Fig. 1Go). This isoform was detected as a protein doublet with molecular masses of 63 and 61 kDa (Fig. 1Go).

The presence of the mRNA products of the STAT5a and STAT5b genes was assessed in both RAW 264.7 and WEHI-3 cells using primers specific for STAT5a and STAT5b. RT-PCR analysis of mRNA that had been prepared from RAW 264.7 and WEHI-3 cells revealed an amplification of the appropriate fragment for both genes (Fig. 2Go). Careful sizing of the fragments that had been amplified using the STAT5a primers revealed that the band that had been amplified using mRNA from the RAW 264.7 cells was ~3 bp larger than the band obtained using WEHI-3 mRNA (Fig. 2Go).



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  		FIGURE 2. Expression of mRNA for the STAT5a and STAT5b genes in WEHI-3, RAW 264.7, and WEHI-3D+ cells. Total RNA was isolated from RAW 264.7, WEHI-3, and WEHI-3D+ cells, and 10 µg was used for RT-PCR with primers to STAT5a, STAT5b, or glyceraldehyde-3-phosphate dehydrogenase (G3PDH). PCR-amplified products were separated by electrophoresis in acrylamide and were visualized by ethidium bromide staining. PCR product size determinations were performed as described in Materials and Methods.

 
The expression of the various STAT5 isoforms then was assessed in WEHI-3D+ cells; WEHI-3D+ cells, which are a differentiated variant of parental WEHI-3 cells, were developed in the laboratory of Dr. Moore (10). An immunoblot analysis revealed that WEHI-3D+ cells did not express detectable levels of the novel p63 and p61 kDa proteins that were present in the immature WEHI-3 cells (Fig. 3Go). Instead, these differentiated cells expressed a STAT5 isoform pattern that was similar to that of the mature RAW 264.7 cell line, with a strong expression of the p96 and p94 components (Fig. 3Go). Similarly, the size of the mRNA that was amplified by RT-PCR was the same size as that seen in RAW 264.7 cells (Fig. 2Go).



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  		FIGURE 3. Comparison of STAT5 isoform expression in WEHI-3 and WEHI-3D+ cells. STAT5 protein isoform expression was analyzed in RAW 264.7, WEHI-3, and WEHI-3D+ cells as described in the legend to Figure 1Go.

 
Finally, the pattern of isoform expression was evaluated in primary M{phi} that had been isolated by adherence from elicited peritoneal and BM cell populations. Adherent peritoneal cells expressed the STAT5 isoform pattern of RAW 264.7 cells, with a strong expression of the p96 and p94 components (Fig. 4Go). In contrast, adherent cells that had been isolated from BM demonstrated marked expression of the p80/77 doublet and modest but detectable expression of the novel p63 and p61 kDa proteins.



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  		FIGURE 4. STAT5 isoform expression in primary M{phi} populations. STAT5 protein expression was analyzed in elicited peritoneal cavity (PEC) or bone marrow (BM) M{phi} that had been isolated by adherence. An immunoblot analysis was performed as described in the legend to Figure 1Go.

 

   Discussion
Top
 Abstract
 Introduction
 Materials and Methods
 Results
 Discussion
References
 
It is now clear from the work of a number of laboratories that the STAT5 transcription factor family is composed of at least four naturally occurring, antigenically related isoforms that are encoded by two highly homologous genes. Naturally occurring isoforms of STAT proteins have been identified for STAT1 and STAT3 molecules in addition to STAT5; however, the function of these molecules remains unclear. Much emphasis has been placed on exploring the potential role(s) of the STAT5 family in the proliferation, differentiation, and/or activation of hemopoietic cells. Thus, the short and long isoforms of STAT5a and STAT5b have been shown to be activated in distinct populations of cells in response to IL-3 (13). Other studies have suggested that the truncated STAT5 isoforms fail to induce several IL-3 target genes (14). Finally, Meinke et al. have demonstrated that STAT5 isoform-specific activity may be part of the regulation of myeloid cell differentiation (15). These studies suggest that the isoforms of a given STAT molecule comprise a family of factors with diverse effects or transcriptional activities.

The work described here reveals that the STAT5 family contains at least two previously unidentified isoforms, p63 and p61, that appear to be preferentially expressed in immature M{phi}. Additional experiments will be required to determine the origin of these isoforms and to assess their potential role in M{phi} activities. Recent studies by Azam et al. provide evidence that the truncated p80/p77 isoforms of STAT5 are generated by the action of a STAT5-cleaving protease, with the expression of the protease limited to specific populations of IL-3-responsive cells (14). Experiments are in progress in our laboratory to determine whether the p63/p61 isoforms detected here represent further truncations of the larger STAT5 isoforms. Regardless of the mechanism of isoform production, however, the preferential expression of certain STAT5 isoforms in immature M{phi} is consistent with the hypothesis that the isoform-specific activity of this transcription factor family contributes to M{phi} differentiation. The observations reported here set the stage for a thorough testing of this hypothesis with respect to all members of the STAT5 family.


   Footnotes
 
1 This work was supported by U.S. Public Health Service Grant CA59010 and by a National Research Service Award (AI09379) to M.A.L. Back

2 These authors made an equal contribution to this work. Back

3 Current address: Department of Neurology, University of Wisconsin Medical School, 1300 University Avenue, Madison, WI 53706. Back

4 Current address: Laboratory of Parasitic Diseases, National Institutes of Health/National Institute of Allergy and Infectious Diseases, Building 4, Room B1-12, Bethesda, MD 20892. Back

5 Address correspondence and reprint requests to Dr. Donna M. Paulnock, Department of Medical Microbiology and Immunology, University of Wisconsin Medical School, 1300 University Avenue, Madison, WI 53706-1532. E-mail address: Back

6 Abbreviations used in this paper: M{phi}, macrophage(s); BM, bone marrow; HRP, horseradish peroxidase. Back

Received for publication March 11, 1998. Accepted for publication June 19, 1998.


   References
Top
 Abstract
 Introduction
 Materials and Methods
 Results
 Discussion
 References
 

  1. Darnell, J. E., I. M. Kerr, G. R. Stark. 1994. Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science 264:1415.[Abstract/Free Full Text]
  2. Groner, B., S. Altiok, V. Meier. 1994. Hormonal regulation of transcription factor activity in mammary epithelial cells. Mol. Cell. Endocrinol. 100:109.[Medline]
  3. Liu, X., G. W. Robinson, F. Gouilleux, B. Groner, L. Hennighausen. 1995. Cloning and expression of Stat5 and an additional homologue (Stat5b) involved in prolactin signal transduction in mouse mammary tissue. Proc. Natl. Acad. Sci. USA 92:8831.[Abstract/Free Full Text]
  4. Tourkine, N., C. Schindler, M. Larose, L.-M. Houdebine. 1995. Activation of STAT factors by prolactin, interferon-{gamma}, growth hormones, and a tyrosine phosphatase inhibitor in rabbit primary mammary epithelial cells. J. Biol. Chem. 270:20952.[Abstract/Free Full Text]
  5. Gouilleux, F., C. Pallard, I. Dusanter-Fourt, H. Wakao, L.-A. Haldosen, G. Norstedt, D. Levy, B. Groner. 1995. Prolactin, growth hormone, erythropoietin, and granulocyte-macrophage colony-stimulating factor induce MGF-Stat5 DNA binding activity. EMBO J. 14:2005.[Medline]
  6. Azam, M., H. Erdjument-Bromage, B. L. Kreider, M. Xia, F. Quelle, R. Basu, C. Saris, P. Tempst, J. N. Ihle, C. Schindler. 1995. Interleukin-3 signals through multiple isoforms of Stat5. EMBO J. 14:1402.[Medline]
  7. Eilers, A., M. Baccarini, F. Horn, R. A. Hipskind, C. Schindler, T. Decker. 1994. A factor induced by differentiating signals in cells of the macrophage lineage binds to the {gamma} interferon activation site. Mol. Cell. Biol. 14:1364.[Abstract/Free Full Text]
  8. Barahmand-Pour, F., A. Meinke, A. Eilers, F. Gouilleux, B. Groner, T. Decker. 1995. Colony-stimulating factors and interferon-{gamma} activate a protein related to MGF-Stat5 to cause formation of the differentiation-induced factor in myeloid cells. FEBS Lett. 360:29.[Medline]
  9. McDowell, M. A., D. M. Lucas, C. M. Nicolet, D. M. Paulnock. 1995. Differential utilization of IFN-{gamma}-responsive elements in two maturationally distinct macrophage cell lines. J. Immunol. 155:4933.[Abstract]
  10. Metcalf, D., N. A. Nicola. 1982. Autoinduction of differentiation in WEHI-3B leukemia cells. Int. J. Cancer 30:773.[Medline]
  11. Lambert, L. E., D. M. Paulnock. 1989. Differential induction of activation markers in macrophage cell lines by interferon-{gamma}. Cell. Immunol. 120:401.[Medline]
  12. Myers, M. J., J. K. Pullen, N. Ghildyal, E. Eustis-Turf, L. B. Schook. 1989. Regulation of IL-1 and TNF-{alpha} expression during the differentiation of bone marrow-derived macrophage. J. Immunol. 142:153.[Abstract]
  13. Rothman, P., B. Kreider, M. Azam, D. Levy, U. Wegenka, A. Eilers, T. Decker, F. Horn, H. Kashleva, J. Ihle, C. Schindler. 1994. Cytokines and growth factors signal through tyrosine phosphorylation of a family of related transcription factors. Immunity 1:457.[Medline]
  14. Azam, M., C. Lee, I. Strehlow, C. Schindler. 1997. Functionally distinct isoforms of STAT5 are generated by protein processing. Immunity 6:691.[Medline]
  15. Meinke, A., F. Barahmand-Pour, S. Wohrl, D. Stoiber, T. Decker. 1996. Activation of different Stat5 isoforms contributes to cell-type-restricted signaling in response to interferons. Mol. Cell. Biol. 16:6937.[Abstract]



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