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• W2057177567 abstract "The term “peripheral node addressins” describes a set of several endothelial adhesion molecules, which collectively bind to L-selectin and react with monoclonal antibody MECA-79. They regulate lymphocyte recirculation through peripheral nodes. Their expression is thought to be restricted to a specialized vascular segment within the node, called the high endothelial venule. In certain chronic skin diseases, however, postcapillary venules of the skin may also acquire a high endothelial venule-like morphology. Employing immunohistochemistry on cryostat sections, we found these skin endothelial cells – like peripheral node high endothelial venules – to be reactive with monoclonal antibody MECA-79. Tissue lysates from the same specimens were then analyzed by immunoprecipitation using recombinant human L-selectin Fc-chimeras followed by immunoblotting using monoclonal antibody MECA-79. In contrast to peripheral node endothelium, which mainly expressed peripheral node addressin moieties of molecular sizes 90–110 kDa and 160 kDa, endothelial cells in cutaneous T cell lymphoma skin lesions expressed an additional and not yet defined 220 kDa peripheral node addressin-like molecule. Most surprisingly, even in normal skin specimens, we found a distinct subset of endothelial cells located around hair follicles constitutively expressing 90–110 kDa peripheral node addressin-like moieties. It is intriguing to speculate that – in analogy to the role of peripheral node addressins in peripheral nodes – the induced expression of peripheral node addressins in chronic T cell mediated skin diseases is responsible for a sustained lymphocyte recruitment. The constitutive expression of peripheral node addressins on perifollicular endothelium may serve for a continuous lymphocyte recirculation through normal skin. The term “peripheral node addressins” describes a set of several endothelial adhesion molecules, which collectively bind to L-selectin and react with monoclonal antibody MECA-79. They regulate lymphocyte recirculation through peripheral nodes. Their expression is thought to be restricted to a specialized vascular segment within the node, called the high endothelial venule. In certain chronic skin diseases, however, postcapillary venules of the skin may also acquire a high endothelial venule-like morphology. Employing immunohistochemistry on cryostat sections, we found these skin endothelial cells – like peripheral node high endothelial venules – to be reactive with monoclonal antibody MECA-79. Tissue lysates from the same specimens were then analyzed by immunoprecipitation using recombinant human L-selectin Fc-chimeras followed by immunoblotting using monoclonal antibody MECA-79. In contrast to peripheral node endothelium, which mainly expressed peripheral node addressin moieties of molecular sizes 90–110 kDa and 160 kDa, endothelial cells in cutaneous T cell lymphoma skin lesions expressed an additional and not yet defined 220 kDa peripheral node addressin-like molecule. Most surprisingly, even in normal skin specimens, we found a distinct subset of endothelial cells located around hair follicles constitutively expressing 90–110 kDa peripheral node addressin-like moieties. It is intriguing to speculate that – in analogy to the role of peripheral node addressins in peripheral nodes – the induced expression of peripheral node addressins in chronic T cell mediated skin diseases is responsible for a sustained lymphocyte recruitment. The constitutive expression of peripheral node addressins on perifollicular endothelium may serve for a continuous lymphocyte recirculation through normal skin. high endothelial venules peripheral node addressins In order to populate and continuously recirculate through peripheral lymph nodes, lymphocytes utilize a distinct cell adhesion molecule, L-selectin, expressed on their cell surface. The biologic importance of L-selectin was demonstrated by experiments showing that L-selectin-deficient lymphocytes are unable to enter peripheral nodes (Arbones et al., 1994Arbones M.L. Ord D.C. Ley K. et al.Lymphocyte homing and leukocyte rolling and migration are impaired in L-selectin-deficient mice.Immunity. 1994; 1: 247-260Abstract Full Text PDF PubMed Scopus (728) Google Scholar;Steeber et al., 1996Steeber D.A. Green N.E. Sato S. Tedder T.F. Lymphocyte migration in L-selectin-deficient mice.J Immunol. 1996; 157: 1096-1106PubMed Google Scholar;Tang et al., 1998Tang M.L.K. Steeber D.A. Zhang X.Q. Tedder T.F. Intrinsic differences in L-selectin expression levels affect T and B lymphocyte subset-specific recirculation pathways.J Immunol. 1998; 160: 5113-5121PubMed Google Scholar). As a functional consequence, lymphocytes cannot “see” antigens presented by antigen-presenting cells within the regional nodes, which results in impaired sensitization (Catalina et al., 1996Catalina M.D. Carroll M.C. Arizpe H. Takashima A. Estess P. Siegelman M.H. The route of antigen entry determines the requirement for L-selectin during immune responses.J Exp Med. 1996; 184: 2341-2351Crossref PubMed Scopus (89) Google Scholar). L-selectin exerts this function by binding to ligands expressed on a specialized vascular segment within the node, called the high endothelial venule (HEV). Most of the current knowledge about these “node-specific L-selectin ligands” is derived from studies using monoclonal antibody (MoAb) MECA-79. This antibody reacts with sialylated, fucosylated, and sulfated carbohydrates (sulfo-sLex) coupled to a diverse set of glycoproteins and blocks lymphocyte homing to peripheral nodes (Streeter et al., 1988Streeter P.R. Rouse B.T. Butcher E.C. Immunohistologic and functional characterization of a vascular addressin involved in lymphocyte homing into peripheral lymph nodes.J Cell Biol. 1988; 107: 1853-1862Crossref PubMed Scopus (513) Google Scholar;Hemmerich et al., 1994Hemmerich S. Butcher E.C. Rosen S.D. Sulfation-dependent recognition of high endothelial venules (HEV) -ligands by L-selectin and MECA 79, and adhesion-blocking monoclonal antibody.J Exp Med. 1994; 180: 2219-2226Crossref PubMed Scopus (245) Google Scholar). Therefore, these MECA-79-reactive L-selectin ligands expressed on HEV have been collectively called peripheral node addressins (PNAd). PNAd isolated from human lymph nodes and tonsils encompasses several glycoproteins of molecular weights 50–60, 90–110, 160, and 200 kDa (Berg et al., 1991Berg E.L. Robinson M.K. Warnock R.A. Butcher E.C. The human peripheral node vascular addressin is a ligand for a lymphocyte homing receptor.J Cell Biol. 1991; 114: 343-349Crossref PubMed Scopus (260) Google Scholar;Suzuki et al., 1996Suzuki A. Andrew D.P. Gonzalo J.A. et al.CD34-deficient mice have reduced eosinophil accumulation after allergen exposure and show a novel crossreactive 90-kD protein.Blood. 1996; 87: 3550-3562Crossref PubMed Google Scholar;Sassetti et al., 1998Sassetti C. Tangemann K. Singer M.S. Kershaw D.B. Rosen S.D. Identification of podocalyxin-like protein as a high endothelial venule ligand for L-selectin: parallels to CD34.J Exp Med. 1998; 187: 1965-1975Crossref PubMed Scopus (213) Google Scholar). CD34 represents a part of the 90–110 kDa component and the 160 kDa molecule is a podocalyxin-like protein, whereas the identities of the remaining proteins of the “PNAd complex” in humans are as yet unknown (Berg et al., 1991Berg E.L. Robinson M.K. Warnock R.A. Butcher E.C. The human peripheral node vascular addressin is a ligand for a lymphocyte homing receptor.J Cell Biol. 1991; 114: 343-349Crossref PubMed Scopus (260) Google Scholar;Baumhueter et al., 1993Baumhueter S. Singer M.S. Henzel W. Hemmerich S. Renz M. Rosen S.D. Lasky L.A. Binding of L-selectin to the vascular sialomucin CD34.Science. 1993; 262: 436-438Crossref PubMed Scopus (578) Google Scholar;Puri et al., 1995Puri K.D. Finger E.B. Gaudernack G. Springer T.A. Sialomucin CD34 is the major L-selectin ligand in human tonsil high endothelial venules.J Cell Biol. 1995; 131: 261-270Crossref PubMed Scopus (139) Google Scholar;Sassetti et al., 1998Sassetti C. Tangemann K. Singer M.S. Kershaw D.B. Rosen S.D. Identification of podocalyxin-like protein as a high endothelial venule ligand for L-selectin: parallels to CD34.J Exp Med. 1998; 187: 1965-1975Crossref PubMed Scopus (213) Google Scholar). PNAd has to be separated from MECA-79-nonreactive L-selectin ligands, such as PSGL-1 or ELAM-1, which do not function as lymph node homing receptors and have an altered tissue distribution (Imai et al., 1993Imai Y. Lasky L.A. Rosen S.D. Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin.Nature. 1993; 361: 555-557Crossref PubMed Scopus (326) Google Scholar;Kogelberg and Rutherford, 1994Kogelberg H. Rutherford T.J. Studies on the three-dimensional behaviour of the selectin ligands Lewis (a) and sulphated Lewis (a) using NMR spectroscopy and molecular dynamics simulations.Glycobiology. 1994; 4: 49-57Crossref PubMed Scopus (43) Google Scholar;Tu et al., 1996Tu L. Chen A. Delahunty M.D. Moore K.L. Watson S.R. McEver R.P. Tedder T.F. L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes: interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity.J Immunol. 1996; 157: 3995-4004PubMed Google Scholar;Sackstein et al., 1997Sackstein R. Fu L. Allen K.L. A hematopoietic cell L-selectin ligand exhibits sulfate-independent binding activity.Blood. 1997; 89: 2773-2781Crossref PubMed Google Scholar;Zöllner et al., 1997Zöllner O. Lentner M.C. Blanks J.E. Borges E. steegmaier M. Zerwes H.G. Vestweber D. L-selectin from human, but not from mouse neutrophils binds directly to E-selectin.J Cell Biol. 1997; 136: 707-716Crossref PubMed Scopus (119) Google Scholar;Berg et al., 1998Berg E.L. Mullowney A.T. Andrew D.P. Goldberg J.E. Butcher E.C. Complexity and differential expression of carbohydrate epitopes associated with L-selectin recognition of high endothelial venules.Am J Pathol. 1998; 152: 469-477PubMed Google Scholar;Clark et al., 1998Clark R.A. Fuhlbrigge R.C. Springer T.A. L-selectin ligands that are O-glycoprotease resistant and distinct from MECA-79 antigen are sufficient for tethering and rolling of lymphocytes on human high endothelial venules.J Cell Biol. 1998; 140: 721-731Crossref PubMed Scopus (54) Google Scholar;Snapp et al., 1998Snapp K.R. Ding H. Atkins K. Warnke R. Luscinskas F.W. Kansas G.S. A novel P-selectin glycoprotein ligand-1 monoclonal antibody recognizes an epitope within the tyrosine sulfate motif of human PSGL-1 and blocks recognition of both P- and L-selectin.Blood. 1998; 91: 154-164Crossref PubMed Google Scholar). Based on the observation that postcapillary venules in certain chronic skin diseases such as psoriasis, pseudolymphoma, and T cell lymphoma acquire a HEV-like morphology, similar to that seen in peripheral nodes (Streilein, 1990Streilein J.W. Speculations on the immunopathogenesis of psoriasis: T cell violation of a keratinocyte sphere of influence.J Invest Dermatol. 1990; 95: 20s-21sAbstract Full Text PDF PubMed Google Scholar), we set out to explore, whether these skin endothelial cells also acquire a HEV-like phenotype, namely the expression of L-selectin ligands of the PNAd complex. Human lymph nodes from the axillary and inguinal region and normal human skin from the thighs, limbs, and trunk were obtained from cadaveric donors through the Department of Pathology, University of Vienna, according to an approved protocol of the University of Vienna Ethical Committee. Biopsies from cutaneous T cell lymphoma skin lesions (plaque and tumor stage of mycosis fungoides) were obtained from five different patients after informed consent. After removing the subcutaneous tissue, all samples were immediately snap frozen and stored in liquid nitrogen. For selected experiments, dermal microvascular endothelial cells were isolated from 100 cm2 normal cadaveric thigh skin by dispase digestion followed by mechanical expression of cells into phosphate-buffered saline as described previously (Petzelbauer et al., 1995Petzelbauer P. Watson C.A. Pfau S.E. Pober J.S. IL-8 and angiogenesis: evidence that human endothelial cells lack IL-8 receptors and do not respond in vitro.Cytokine. 1995; 7: 267-272Crossref PubMed Scopus (94) Google Scholar). The expressed cells contained approximately 5 × 105 endothelial cells per sample. After pelleting they were immediately snap frozen and stored in liquid nitrogen. Five micrometer cryostat sections were prepared and three step immunohistochemistry using the avidin–biotin system (peroxidase ABC-Elite kit; Vector Laboratories, Burlingame, CA) was performed as described previously (Kunstfeld et al., 1997Kunstfeld R. Lechleitner S. Gröger M. Wolff K. Petzelbauer P. HECA-452+ T Cells migrate through superficial vascular plexus but not through deep vascular plexus endothelium.J Invest Dermatol. 1997; 108: 343-348Abstract Full Text PDF PubMed Scopus (29) Google Scholar). As first step reagents, we used MoAb MECA-79 (rat anti-mouse antibody, IgM; Pharmingen, San Diego, CA) or an isotype control antibody diluted 1:1000 in phosphate-buffered saline containing 3% rabbit serum. The second step antibody was a biotin-conjugated rabbit anti-rat IgM from Jackson (West Grove, PA). Frozen tissues (≈200 mg per experiment) were cut into pieces, submersed in 1 ml lysis buffer containing 50 mM Tris, 2 mM CaCl2, 2 mM MnCl, 2 mM MgCl, 2% NP-40, and 1 mM phenylmethylsulfonyl fluoride, 10 μg per ml aprotinin, 15 μg per ml leupeptin, pH 7.5, and homogenized using the Dispersing-Tool from IKA (Stauffen, Germany). Following 1 h incubation on ice, centrifugation at 13,000 × g for 20 min at 4°C, the supernatants were collected and precleared with protein G Sepharose beads (GammaBind G; Pharmacia, Uppsala, Sweden). For selective experiments, endothelial cells were isolated from cadaveric thigh skin by dispase digestion as described above. Endothelial cells were submersed in lysis buffer as described for full skin samples. For immunoprecipitation of L-selectin ligands, 50 μg protein G Sepharose beads (Sigma, St Louis, MO) were loaded with 25 μg L-selectin–Fc protein (gift from Ray Camphausen, Genetics Institute, Cambridge, MA). Alternatively, 50 μg protein G Sepharose beads were loaded with 10 μg anti-rat IgM antibody (Jackson) followed by incubation with 20 μg MECA-79. As a negative control, beads were loaded with 25 μg L-selectin–Fc chimeric protein in the presence of 10 M ethylenediamine tetraacetic acid, as it has been shown previously that the L-selectin/L-selectin ligand interaction is Ca2+ sensitive (Sassetti et al., 1998Sassetti C. Tangemann K. Singer M.S. Kershaw D.B. Rosen S.D. Identification of podocalyxin-like protein as a high endothelial venule ligand for L-selectin: parallels to CD34.J Exp Med. 1998; 187: 1965-1975Crossref PubMed Scopus (213) Google Scholar). To control for the precipitation with MoAb MECA-79, the specific MoAb was replaced by an irrelevant rat IgM. The respective beads were incubated with lysates derived from ≈200 mg tissue for 2 h at 4°C under continuous rotation. Beads were then pelleted by centrifugation at 3000 × g, washed in 50 mM Tris buffer, pH 7.5, containing 2 mM CaCl2, 2 mM MnCl, 2 mM MgCl, and immunoprecipitates were eluted using a 2 × sample buffer (62.5 mM Tris/HCl, pH 6.8, 10% glycerol, 1% sodium dodecyl sulfate, 10 μg bromophenol blue per ml, 2% β-mercaptoethanol) for 5 min at 95°C. Precipitated proteins were separated by polyacrylamide gel electrophoresis under reducing conditions according to the method described byLaemmli, 1970Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature. 1970; 227: 680-685Crossref PubMed Scopus (202564) Google Scholar. After electrotransfer on to nitrocellulose membranes (BioRad, Richmond, CA), incubation with MECA-79 (5 μg per ml) in 50 mM Tris-buffered saline, pH 7.5, containing 1% low-fat milk, rinsing, incubation with a horseradish peroxidase-conjugated second step antibody (Pierce, Rockford, IL), peroxidase was visualized by chemiluminescence (Amersham Corporation, Buckinghamshire, U.K.) and recorded on film. Appropriate isotype controls were run in parallel. Screening lesional skin from chronic eczema (n = 3), psoriasis (n = 4), parapsoriasis (n = 8), and cutaneous T cell lymphoma (n = 5) by immunohistochemistry for the expression of MECA-79-reactive epitopes revealed that both, the numbers of positively stained vessels within the superficial vascular plexus as well as their relative staining intensity was most abundant in patch and tumor stages of cutaneous T cell lymphoma lesions (data shown for T cell lymphoma only; Figure 1a–c). This has been reported previously (Mackay et al., 1992Mackay C.R. Marston W. Dudler L. Altered patterns of T cell migration through lymph nodes and skin following antigen challenge.Eur J Immunol. 1992; 22: 2205-2210Crossref PubMed Scopus (124) Google Scholar;Michie et al., 1993Michie S.A. Streeter P.R. Bolt P.A. Butcher E.C. Picker L.J. The human peripheral lymph node vascular addressin. An inducible endothelial antigen involved in lymphocyte homing.Am J Pathol. 1993; 143: 1688-1698PubMed Google Scholar), but we wish to draw attention to the fact that all endothelial cells reactive with MECA-79 had acquired morphologic features of HEV, being of a cuboidal shape with large and prominent nuclei (Figure 1b, c). In normal skin samples, endothelial cells within the superficial vascular plexus were reproducibly negative for MECA-79 (Figure 1d). Most interestingly, screening normal skin samples from 10 different donors by serial sectioning revealed 20%–60% of hair follicles being surrounded by MECA-79-positive vessels (Figure 1e). It should be noted that endothelial cells from the perifollicular vascular segment differ by morphology from the superficial vascular plexus endothelium by having bridged fenestrations (Braverman and Keh, 1981Braverman I.M. Keh Y.A. Ultastructure of the human dermal microcirculation. III. The vessels in the mid- and lower dermis and subcutaneous fat.J Invest Dermatol. 1981; 77: 297-304Abstract Full Text PDF PubMed Scopus (59) Google Scholar). HEV in peripheral nodes, investigated as a positive control, showed a staining pattern with MoAb MECA-79 very similar to that observed in tumor stages of cutaneous T cell lymphoma lesions (Figure 1). Moreover, immunohistochemistry revealed a striking specificity of MoAb MECA-79 for endothelium, hematopoietic cells always being nonreactive for MECA-79 (Figure 1). As an additional control for the specificity of MECA-79, peripheral blood nuclear cells were tested for MECA-79 expression by fluorescence-activated cell sorter and this also resulted in a negative staining (data not shown). We next addressed the question whether these MECA-79-reactive epitopes found on skin endothelium are indeed L-selectin ligands or even resemble PNAd molecules. For these experiments we chose cutaneous T cell lymphoma lesions, because of the abundance of endothelial MECA-79 reactivity. Detergent lysates of lesional skin from five different patients were analyzed. Lysates from four patients gave reproducible results in at least two independent experiments each, material from the fifth patient was not sufficient for an independent repeat and was therefore excluded from this study. From each of the four lysates, L-selectin precipitated a pattern of MECA-79-reactive proteins of molecular weights of 90–110 kDa, 160 kDa, 200 kDa, and 220 kDa (Figure 2). Fifty to 60 kDa proteins were only found in one patient (HK; Figure 2). With the exception of the 220 kDa component, the pattern of these skin-derived MECA-79-reactive L-selectin ligands exactly matched the PNAd complex isolated from peripheral nodes, which were examined as a positive control (Figure 2). In peripheral nodes, the 220 kDa component was either absent or not clearly separable from the 200 kDa protein (Figure 2). As a negative control, precipitation with the L-selectin–Fc chimeric protein in the presence of Ca2+ was performed, the subsequent immunoblot of these precipitates did not reveal any MECA-79-reactive proteins (data not shown). To control for the possibility that the MECA-79-reactive L-selectin ligands detected in our skin samples were expressed by infiltrating white blood cells, peripheral blood nuclear cells were analyzed for comparison. In these cells, L-selectin precipitated the 240 kDa dimeric protein PSGL-1, a MECA-79 nonreactive L-selectin ligand expressed on lymphocytes, but no MECA-79-reactive proteins (data not shown). This experiment confirmed our immunohistochemical observation that MoAb MECA-79 reacts exclusively with endothelial epitopes and not with leukocytes. We next subjected skin lysates to MECA-79 immunoprecipitation followed by immunoblotting using MoAb MECA-79 for detection. The molecular sizes of proteins detected by this procedure matched those precipitated by L-selectin and detected by MECA-79 immunoblotting (Figure 3). These experiments do not prove but strongly suggest that virtually all MECA-79-reactive epitopes detected in our skin samples stand for L-selectin ligands “of the PNAd type”. In seeming contrast with our immunohistochemical observation that MoAb MECA-79 reacted with perifollicular endothelial cells, we were unable to precipitate L-selectin ligands from normal skin samples when lysing 200 mg of tissue for one experiment (Figure 2). We attributed this to the fact that L-selectin ligands were below the detection limit and tried to enrich for L-selectin ligands. For this purpose, L-selectin-Fc-protein G Sepharose beads were incubated with lysates from normal skin, centrifuged and reincubated with another fresh lysate. This procedure was repeated up to five times. In the following blot, MoAb MECA-79 now detected a faint band of ≈110 kDa (Figure 2). As this result was still unsatisfactory, we isolated microvascular endothelial cells by dispase digestion, a technique, which is routinely used for generating microvascular endothelial cell cultures. The resulting cell suspension was lysed and subjected to precipitation with L-selectin, electrophoresed, and blotted. Now MoAb MECA-79 clearly detected a 110 kDa protein band and two other low molecular weight bands (most likely artifacts due to dispase treatment). We next analyzed MECA-79 expression on dermal microvascular endothelial cells placed in cell culture and passaged as described previously (Petzelbauer et al., 1995Petzelbauer P. Watson C.A. Pfau S.E. Pober J.S. IL-8 and angiogenesis: evidence that human endothelial cells lack IL-8 receptors and do not respond in vitro.Cytokine. 1995; 7: 267-272Crossref PubMed Scopus (94) Google Scholar). Unfortunately, neither cultured human foreskin-derived nor cultured adult human thigh skin-derived endothelium reacted with MoAb MECA-79 (data not shown). This indicated that cell culture either selected for MECA-79 negative cells or resulted in a downregulation of these moieties, which prevented further characterization of the nature of the 110 kDa L-selectin ligand expressed on perifollicular endothelium seen in situ. For comparison, human umbilical vein endothelial cells were also subjected to the same procedure and did not reveal any MECA-79 reactivity. These experiments show that L-selectin ligands of the “PNAd type” are not a specific feature of peripheral node HEV, but are also expressed on skin endothelial cells. By size, these MECA-79-reactive L-selectin ligands detected in T cell lymphoma skin largely corresponded to proteins of the PNAd complex expressed on peripheral lymph node HEV. We want to emphasize, however, that skin endothelial cells expressed an additional PNAd-like 220 kDa protein, which has yet not been identified and extents the list of proteins capable of holding PNAd moieties. This 220 kDa protein appears to be preferentially expressed by skin endothelium and is absent or expressed in very low levels on peripheral node HEV. It should be noted thatSassetti et al., 1998Sassetti C. Tangemann K. Singer M.S. Kershaw D.B. Rosen S.D. Identification of podocalyxin-like protein as a high endothelial venule ligand for L-selectin: parallels to CD34.J Exp Med. 1998; 187: 1965-1975Crossref PubMed Scopus (213) Google Scholar were able to identify a >200 kDa protein in human tonsils, which they postulated to represent a multimer of the 160 kDa podocalyxin-like protein. Whether the herein described 220 kDa protein represents a podocalyxin multimer remains to be determined. For obvious reasons, the availability of sufficiently large samples of diseased human skin is limited and we thus have not yet succeeded in characterizing the protein backbone of this 220 kDa L-selectin ligand." @default.
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• W2057177567 title "Peripheral Lymph Node Addressins are Expressed on Skin Endothelial Cells" @default.
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