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,§,§,§,§,§
Departments of
*
Pathology and
Medicine, Harvard Medical School, Boston, MA 02115; and
Department of Pathology and the
§
Division of Rheumatology, Immunology, and Allergy, Brigham and Women’s Hospital, Boston, MA 02115
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
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Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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The ability to induce a mature rat peritoneal MC to synthesize chondroitin sulfate E within minutes after exposure to ß-D-xyloside (22, 23) led to the realization that rat peritoneal and jejunal MCs are closely related cell types. The ß-D-xyloside experiments also revealed for the first time that a mature, nontransformed MC could quickly alter its histochemistry and proteoglycan expression in vitro. Although IL-3-developed mouse bone marrow (BM)-derived MCs preferentially express chondroitin sulfate E-containing serglycin proteoglycans when cultured alone (24), these in vitro-differentiated MCs preferentially express heparin-containing proteoglycans when cocultured in the presence of fibroblasts (25). The detection of hybrid mouse BM-derived MCs in the fibroblast cocultures containing both safranin+ and safranin- granules indicated that mouse MCs also can change their granule proteoglycan phenotype in vitro when exposed to different environments. Although adoptive transfer experiments conducted by Kitamura and coworkers on MC-deficient W/Wv mice provided evidence that mouse MCs could change their histochemistry and proteoglycan expression in vivo (26, 27, 28, 29, 30), hybrid stainable granules were not routinely found in the MCs of the reconstituted animals. Thus, Kitamura and coworkers (31) speculated that MCs probably undergo "trans-differentiation," dedifferentiating into unrecognizable MCs before acquiring their new granule proteoglycan phenotype.
Besides serglycin proteoglycans, mouse MCs also store varied combinations of a carboxypeptidase and at least seven chymases (designated mouse MC protease (mMCP)-1 to mMCP-5, mMCP-8, and mMCP-9) and two tryptases (mMCP-6 and mMCP-7) in their granules (32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43). Using gene-specific probes and protease-specific Abs, at least five distinct populations of MCs have been detected in various tissues of the BALB/c mouse. For example, MCs that differ in their protease expression have been found in the peritoneal cavity (33, 34, 36, 37, 38), uterus (43), skin (44), spleen (45), and jejunal epithelium (8, 32, 35) of this mouse strain. Which chymase a MC expresses in the BALB/c mouse seems to be dictated by both the current and previous microenvironment of the cell. We recently reported that the MCs in the jejunum of Trichinella spiralis-infected BALB/c mice undergo time- and strata-dependent changes in their expression of the three chymases mMCP-1, mMCP-2, and mMCP-5 (8). Helminth-infected mice and rats experience a transient, but pronounced, T cell-dependent increase in the number of their jejunal MCs (2, 3, 4, 5, 6, 7, 8). Within 1 wk after BALB/c mice have been infected with T. spiralis larvae, increased numbers of MCs appear in the crypts at the base of the villi, and the number of MCs throughout the villi increases by >25-fold by wk 2. During the resolution phase of the helminth infection, MCs initially disappear from the tip of the villus, then from the mid-region of the villus, and finally from the lower villus. At the height of the helminth infection, only intraepithelial MCs possess stellate-shaped granules containing crystalline structures (8, 46). The retention of such granules with fragmented crystals in lamina propria MCs during resolution of the infection indicates that at least some MCs migrate through the jejunal strata during the different phases of the inflammation (8). At the height of the infection, MCs found in the muscle expressed mMCP-5 but not mMCP-1 or mMCP-2, even though most MCs in the epithelium at this time point expressed mMCP-1 and mMCP-2 but not mMCP-5. Accompanying these two MC populations were transitional forms in the submucosa that expressed mMCP-5 and mMCP-2 but not mMCP-1 and forms in the lamina propria that expressed mMCP-2 alone. In the recovery phase of the infection at wk 4, MCs sequentially cease expressing mMCP-1, express mMCP-5, and finally cease expressing mMCP-2 as they progressively move from the tip of the villus to the submucosa. BALB/c mouse BM-derived MCs that are developed in vitro with IL-3 reversibly change their chymase expression when cultured in the presence of different combinations of cytokines and glucocorticoids (47, 48, 49, 50, 51), primarily through a posttranscriptional mechanism (51, 52). Thus, it is possible that jejunal MCs alter their expression of mMCP-1, mMCP-2, and mMCP-5 in part by altering the stability of the individual chymase transcripts.
Because the v-abl-immortalized V3-MC line also changes its chymase expression following its adoptive transfer into BALB/c mice (45), it has been proposed that the chymase phenotype of a jejunal MC is the result of the dynamics of changing MC-regulatory factors. Although V3-MC can be induced to express mMCP-7 following its adoptive transfer into BALB/c mice, we and others have been unable to cytokine-regulate tryptase expression in IL-3-developed, mouse BM-derived MCs. Thus, it remained to be determined whether a mouse MC can alter its tryptase expression in vivo during an inflammatory event. We now show that jejunal MCs reversibly alter their expression of the two tryptases and the recently recognized chymase mMCP-9 (43) as these cells move through the various strata during the onset and resolution stages of T. spiralis-induced MC hyperplasia.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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Each BALB/c mouse was infected orally with 500 freshly isolated, stage 3 T. spiralis larvae, as previously described (8, 48). Mice were killed at various times after infection, and 2-cm lengths of jejunum, whole spleen, and ear were removed and fixed for analysis. Because all jejunal and splenic MCs express abundant levels of at least one chymase, these MCs are readily recognized in fixed, dehydrated, and embedded mouse tissues by their pronounced chloroacetate esterase activity (8). In a modification (53) of the enzyme cytochemistry procedure of Leder (54), fixed sections of intestine from noninfected and helminth-infected mice were incubated at 30°C for 1 h with a solution containing naphthol AS-D chloroacetate (Sigma Chemical Co., St. Louis, MO). The tissue preparations were rinsed and counterstained with hematoxylin.
MCs with tryptic activities were identified in jejunal tissue sections by the cytochemistry method of Osman and coworkers (55), using Z-Ala-Ala-Lys-4-methoxy-2-naphthylamide (AAK; Enzyme System Products, Livermore, CA) as the substrate. In control experiments conducted on serial sections of jejunum, the mMCP-6-/mMCP-7- MCs in the epithelium of BALB/c mice did not exhibit AAK activity. In contrast, all mMCP-6+/mMCP-7+ MCs in the submucosa of these control mice exhibited an intense tan reaction product in their cytoplasmic granules when incubated with the AAK substrate. The C57BL/6 mouse cannot express mMCP-7 (56) because its gene possesses a point mutation at the intron 2/exon 2 splice site (57). The observation that the mMCP-6+ MCs in the skin of this strain also contain AAK enzymatic activity (data not shown) indicates that mMCP-6 can cleave the substrate. Likewise, the discovery of an occasional AAK+ MC in the submucosa of BALB/c mice at the resolution phase of the infection that expresses mMCP-7 but not mMCP-6 (data not shown) indicates that mMCP-7 can cleave the substrate as well.
Immunohistochemistry
MCs in serial sections of jejunum from noninfected and T.
spiralis-infected mice were evaluated immunohistochemically (8, 58) for their expression of mMCP-2 (49), mMCP-6 (59), mMCP-7 (56), and
mMCP-9 (43) using previously described rabbit anti-peptide Abs.
Briefly, collected tissues were fixed for 4 h at room temperature
in 4% paraformaldehyde in 0.1 M sodium phosphate (pH 7.6).
Alternately, selected samples were fixed in Carnoy’s solution. The
preparations were washed twice with PBS containing 2% DMSO and then
suspended in 50 mM NH4Cl overnight at 4°C. The specimens
were dehydrated and embedded in accordance with the JB-4 kit from
Polysciences (Warrington, PA). Sections were cut on a Reichert-Jung
Supracut microtome (Leica, Deerfield, IL) with glass knives and picked
up on glass slides. The slides were incubated sequentially for 15 min
at 37°C in 2 mM CaCl2 containing 0.025% trypsin, for 15
min at room temperature in PBS containing 0.05% Tween-20 and 0.1%
BSA, for 30 min at 37°C in PBS containing 0.05% Tween-20 and 4%
normal goat serum, and then overnight at 4°C in 4% normal goat serum
containing purified rabbit anti-mMCP-2 Ig (49), anti-mMCP-6 Ig
(59), anti-mMCP-7 Ig (56), or anti-mMCP-9 Ig (43). Each section
was evaluated immunohistochemically for the presence of just one mMCP.
The mMCP-2-, mMCP-6-, mMCP-7-, and mMCP-9-specific Abs were obtained
previously against synthetic peptides that correspond to residues 56 to
71, 160 to 178, 160 to 178, and 144 to 152 in the respective serine
protease. Although the brush borders of the villus exhibit a
nonspecific reaction in the immunohistochemistry procedure due to the
endogenous intestinal alkaline phosphatase (AP), the Abs are
mMCP-specific. The specificities of these rabbit anti-peptide Abs
have been described in earlier publications using recombinant proteases
and select MC populations. As assessed by the OD of the stock solutions
at 280 nm, the affinity-purified Abs were generally used at a
concentration of 
4 µg/ml with 0.2 µg/slide. Samples were
washed, incubated for 40 min at room temperature in buffer containing
biotin-labeled goat anti-rabbit IgG, washed twice in 0.1% BSA and
0.05% Tween-20 in PBS, incubated for 40 min at room temperature in
Vectastain avidin-biotin complex-AP reagent (Vector Laboratories,
Burlingame, CA), and then incubated for 15 min in the dark at room
temperature in an AP substrate solution. Tissue sections were
counterstained with Gill’s hematoxylin in 20% ethylene glycol, and
then coverslips with Immu-Mount (Shandon, Pittsburgh, PA) were
applied.
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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As assessed by immunohistochemical analysis of serial sections of
jejunum, the MCs in the submucosa of noninfected BALB/c mice expressed
mMCP-6 and mMCP-7 but not mMCP-2 or mMCP-9 (Fig. 1
and Table I). At 1 wk after helminth infection, MCs
increased in number in the lower portion of the lamina propria, the
lower portion of the villus epithelium, and between the epithelial
cells in the crypts. Most of the MCs in the submucosa at this time
point continued to express mMCP-6, but some MCs were found in this
location that expressed all combinations of mMCP-2, mMCP-6, and mMCP-7,
with the exception of mMCP-7 alone (Table I). MCs that expressed mMCP-9
were found in the submucosa at the height of the intestinal MC
hyperplasia at wk 2, but mMCP-9+ MCs were rarely found
in the upper villus, mid-villus, lower villus, or crypts at this time
point (Fig. 2). Nevertheless, the MCs in
the submucosa at wk 2 did resemble those in the submucosa at wk 1 in
terms of the diversity of their expression of the other three granule
proteases (Table I). Most submucosa MCs continued to coexpress mMCP-6
and mMCP-7. While only a few submucosa MCs expressed mMCP-2 alone or
mMCP-7 alone, numerous MCs could be found in the submucosa at this
point that coexpressed mMCP-2 and mMCP-6 with (Fig. 3) or without mMCP-7. Many of the MCs in
the lamina propria region of the crypts and lower villus at wk 2 also
coexpressed mMCP-6 and mMCP-7, but a greater percentage of the MCs in
these locations just expressed mMCP-2 at that point. In addition, more
MCs with a
mMCP-2-/mMCP-6+/mMCP-7- phenotype
were found in the crypt lamina propria than in the villus lamina
propria, whereas more MCs having a
mMCP-2+/mMCP-6+/mMCP-7-
phenotypewere found in the villus lamina propria than in the
crypt lamina propria (Table I). While MCs could be found in the upper
villus that expressed nearly every combination of mMCP-2, mMCP-6, and
mMCP-7, most of the MCs in this location and in the crypt
epithelium expressed mMCP-2 alone (Fig. 3). In agreement with the
immunohistochemistry data, the MCs in the submucosa of
helminth-infected mice, but not those MCs in the crypt epithelium,
contained tryptic proteases that cleaved the AAK substrate (Fig. 4). The MCs in the crypt epithelium that
expressed mMCP-1 and mMCP-2, but not mMCP-6 or mMCP-7, did not exhibit
AAK enzymatic activity.
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As previously determined (8), the number of jejunal MCs steadily
decreased during the resolution phase of the helminth infection (Table I
) and was near baseline by wk 8 (data not shown). MCs were rarely
found in the tips of the upper villi at wk 4 (Fig. 5). During the recovery phase of the
helminth infection, MCs could be found in the villus lamina propria
that had nearly every combination of mMCP-2, mMCP-6, and mMCP-7 (Table I). However, most of the lamina propria MCs in the upper villus
expressed either mMCP-2 alone or both mMCP-2 and mMCP-6, whereas
most lamina propria MCs in the lower villus expressed either mMCP-6
alone or both mMCP-6 and mMCP-7 (Fig. 5). Although the MCs in the
lamina propria of the crypts expressed every combination of
mMCP-2, mMCP-6, and mMCP-7, a higher percentage of the cells in
the crypt lamina propria and submucosa now expressed mMCP-7 relative to
those cells in the villus lamina propria. At this time point, any MC
that contained immunoreactive mMCP-6 or mMCP-7 in its granules cleaved
the AAK substrate (data not shown). As illustrated in Figure 6 for one tissue section, 119 of the 122
analyzed MCs in the submucosa of three mice (40 submucosa MCs
analyzed in each mouse) and 37 of the 41 analyzed MCs in the crypt
lamina propria of the same three mice expressed mMCP-9.
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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). The fact that submucosa MCs fixed with paraformaldehyde still
cleaved the AAK substrate (Fig. 4) established the Ags recognized by
anti-mMCP-6 Ig and anti-mMCP-7 Ig as enzymatically active
tryptases. Like the chloroacetate esterase cytochemistry
procedure (53, 54) used to quantitate all chymase-expressing MCs in
the jejunum (7, 8), skin (60), and spleen (8), the AAK enzyme
cytochemistry procedure (55) can be used to quantitate MCs in the
jejunum that express mMCP-6 and/or mMCP-7.
At the height of the T. spiralis-induced intestinal MC
hyperplasia, most of the MCs in the submucosa expressed mMCP-9 and the
two tryptases (Table I and Figs. 2 and 3). However, transitional forms
were present in the lamina propria of the crypts and lower villus that
expressed mMCP-2 alone, mMCP-6 alone, mMCP-2 and mMCP-6, and even the
combination of mMCP-2, mMCP-6, and mMCP-7. In an earlier study (8), we
noted that at the height of the infection at wk 2, some of the MCs in
the muscle and submucosa express mMCP-5 but not mMCP-1 or mMCP-2,
whereas most intraepithelial MCs express mMCP-1 and mMCP-2 but not
mMCP-5. Accompanying these two MC populations were transitional forms
in the submucosa that expressed mMCP-2 and mMCP-5 but not mMCP-1 and
forms in the lamina propria that expressed mMCP-2 alone. Because of the
thickness of serially sectioned tissue, the practical evaluation of
protease expression in a single MC is limited to three mMCPs.
Nevertheless, the cumulative findings of current and previous studies
now suggest that BALB/c mouse jejunal MCs that initially have a
mMCP-1-/mMCP-2-/mMCP-5+/mMCP-6+/mMCP-7+/mMCP-9-
granule protease phenotype sequentially express mMCP-2 and mMCP-9;
cease expressing mMCP-5, mMCP-6, mMCP-7, and mMCP-9; and finally
express mMCP-1 as they progressively move from the submucosa to the
mucosal lamina propria.
Essentially no intraepithelial MCs were present in the upper villus in
the resolution phase of the MC hyperplasia at wk 4 (Fig. 5). We and
others have previously showed that the MCs in the villus and crypt
epithelium at the height of infection are the only population of MCs
that contain stellate-shaped granules with crystalline structures (8, 46). The presence of granules with fragmented crystals in lamina
propria MCs during resolution of the infection indicates that at least
some MCs migrate through the thickness of the jejunum during this phase
of inflammation (8). During the resolution phase of the reactive MC
hyperplasia, the MCs in the lamina propria were able to express any
combination of mMCP-2, mMCP-6, and mMCP-7 (Fig. 5). However, virtually
all of the lamina propria MCs from the mid-villus to submucosa levels
of the jejunum expressed mMCP-9 (Fig. 6). Based on earlier (8) and
current studies, wk 4 is the point at which MCs stop expressing mMCP-1
and mMCP-2 and begin to express mMCP-5, mMCP-9, and various
combinations of the two tryptases as they progressively move from
the upper villus to the submucosa. Figure 7 shows a schematic representation of the
expression of the four chymases and the two tryptases in the MCs
that reside at different locations in the jejunum of noninfected and
helminth-infected BALB/c mice.
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Footnotes |
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2 Address correspondence and reprint requests to Dr. Daniel S. Friend or Dr. Richard L. Stevens, Brigham and Women’s Hospital, Smith Building, Rm. 616B, 75 Francis St., Boston, MA 02115. E-mail address:
3 Abbreviations used in this paper: MC, mast cell; BM, bone marrow; AAK, Z-Ala-Ala-Lys-4-methoxy-2-naphthylamide; mMCP, mouse mast cell protease; AP, alkaline phosphatase.
Received for publication July 29, 1997. Accepted for publication January 14, 1998.
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References |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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ali, N. Huang, S. Ghildyal, K. F. Austen Stechschulte, R. L. Stevens. 1997. Mouse mast cell protease 9, a novel member of the chromosome 14 family of serine proteases that is selectively expressed in uterine mast cells. J. Biol. Chem. 272:29158.
, and the IL-10-induced expression of chymases. J. Immunol. 158:4373.[Abstract]
ali, M. F. Gurish. 1996. Fate of two mast cell tryptases in V3 mastocytosis and normal BALB/c mice undergoing passive systemic anaphylaxis: prolonged retention of exocytosed mMCP-6 in connective tissues and rapid accumulation of enzymatically active mMCP-7 in the blood. J. Exp. Med. 184:1061.ali, N. Ghildyal, M. Karplus, R. L. Stevens. 1995. Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans. J. Biol. Chem. 270:19524.ali, W.-T. Qiu Matsumoto, R. L. Stevens. 1997. The tryptase, mouse mast cell protease 7, exhibits anticoagulant activity in vivo and in vitro due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma. J. Biol. Chem. 272:31885.This article has been cited by other articles:
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Y. Li, L. Li, R. Wadley, S. W. Reddel, J. C. Qi, C. Archis, A. Collins, E. Clark, M. Cooley, S. Kouts, et al. Mast cells/basophils in the peripheral blood of allergic individuals who are HIV-1 susceptible due to their surface expression of CD4 and the chemokine receptors CCR3, CCR5, and CXCR4 Blood, June 1, 2001; 97(11): 3484 - 3490. [Abstract] [Full Text] [PDF]
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D. S. Friend, M. F. Gurish, K. F. Austen, J. Hunt, and R. L. Stevens Senescent Jejunal Mast Cells and Eosinophils in the Mouse Preferentially Translocate to the Spleen and Draining Lymph Node, Respectively, During the Recovery Phase of Helminth Infection J. Immunol., July 1, 2000; 165(1): 344 - 352. [Abstract] [Full Text] [PDF]
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C. Huang, G. Morales, A. Vagi, K. Chanasyk, M. Ferrazzi, C. Burklow, W.-T. Qiu, E. Feyfant, A. Sali, and R. L. Stevens Formation of Enzymatically Active, Homotypic, and Heterotypic Tetramers of Mouse Mast Cell Tryptases. DEPENDENCE ON A CONSERVED Trp-RICH DOMAIN ON THE SURFACE J. Biol. Chem., January 7, 2000; 275(1): 351 - 358. [Abstract] [Full Text] [PDF]
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E. Razin, Z. C. Zhang, H. Nechushtan, S. Frenkel, Y.-N. Lee, R. Arudchandran, and J. Rivera Suppression of Microphthalmia Transcriptional Activity by Its Association with Protein Kinase C-interacting Protein 1 in Mast Cells J. Biol. Chem., November 26, 1999; 274(48): 34272 - 34276. [Abstract] [Full Text] [PDF]
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G. W. Wong, Y. Tang, E. Feyfant, L. Li, Y. Li, C. Huang, D. S. Friend, S. A. Krilis, and R. L. Stevens Identification of a New Member of the Tryptase Family of Mouse and Human Mast Cell Proteases Which Possesses a Novel COOH-terminal Hydrophobic Extension J. Biol. Chem., October 22, 1999; 274(43): 30784 - 30793. [Abstract] [Full Text] [PDF]
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H. R.P. Miller, S. H. Wright, P. A. Knight, and E. M. Thornton A Novel Function for Transforming Growth Factor-{beta}1: Upregulation of the Expression and the IgE-Independent Extracellular Release of a Mucosal Mast Cell Granule-Specific {beta}-Chymase, Mouse Mast Cell Protease-1 Blood, May 15, 1999; 93(10): 3473 - 3486. [Abstract] [Full Text] [PDF]
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 K. P. Valchanov and G. B. Proctor Enzyme Histochemistry of Tryptase in Stomach Mucosal Mast Cells of the Mouse J. Histochem. Cytochem., May 1, 1999; 47(5): 617 - 622. [Abstract] [Full Text]
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A. R. Rosenkranz, A. Coxon, M. Maurer, M. F. Gurish, K. F. Austen, D. S. Friend, S. J. Galli, and T. N. Mayadas Cutting Edge: Impaired Mast Cell Development and Innate Immunity in Mac-1 (CD11b/CD18, CR3)-Deficient Mice J. Immunol., December 15, 1998; 161(12): 6463 - 6467. [Abstract] [Full Text] [PDF]
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L. Li, Y. Li, S. W. Reddel, M. Cherrian, D. S. Friend, R. L. Stevens, and S. A. Krilis Identification of Basophilic Cells that Express Mast Cell Granule Proteases in the Peripheral Blood of Asthma, Allergy, and Drug-Reactive Patients J. Immunol., November 1, 1998; 161(9): 5079 - 5086. [Abstract] [Full Text] [PDF]
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G. W. Wong, S. Yasuda, M. S. Madhusudhan, L. Li, Y. Yang, S. A. Krilis, A. Sali, and R. L. Stevens Human Tryptase epsilon (PRSS22), a New Member of the Chromosome 16p13.3 Family of Human Serine Proteases Expressed in Airway Epithelial Cells J. Biol. Chem., December 28, 2001; 276(52): 49169 - 49182. [Abstract] [Full Text] [PDF]
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