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1.
Cureus ; 14(2): e21909, 2022 Feb.
Article in English | MEDLINE | ID: mdl-35265430

ABSTRACT

Acquired hemophilia A (AHA) is an inhibitory coagulopathy that represents a rare variant of hemorrhagic syndromes. We present a case of idiopathic AHA in a 75-year-old male patient with a cutaneous hematoma that could be attributed to a recent COVID-19 vaccination. The aim of this report is to raise awareness of a possible association between AHA and COVID-19 vaccination and to review similar reported cases and management plans to prevent the development of possible morbidity and debilitating complications. This case illustrates an exceptionally rare side effect of the COVID-19 vaccination. The advantages of obtaining the COVID-19 vaccine outweigh the risks.

2.
Ann Rheum Dis ; 61(6): 554-8, 2002 Jun.
Article in English | MEDLINE | ID: mdl-12006334

ABSTRACT

Classification criteria for Sjögren's syndrome (SS) were developed and validated between 1989 and 1996 by the European Study Group on Classification Criteria for SS, and broadly accepted. These have been re-examined by consensus group members, who have introduced some modifications, more clearly defined the rules for classifying patients with primary or secondary SS, and provided more precise exclusion criteria.


Subject(s)
Sjogren's Syndrome/classification , Decision Making , Decision Trees , Europe , Female , Humans , Male , Middle Aged , ROC Curve , Sensitivity and Specificity
3.
Rheumatology (Oxford) ; 41(3): 338-42, 2002 Mar.
Article in English | MEDLINE | ID: mdl-11934973

ABSTRACT

OBJECTIVE: Apoptosis is an organized energy-dependent process of cellular self-destruction carried out by proteolytic enzymes such as the caspases. These enzymes may play a role in epithelial cell apoptosis in Sjögren's syndrome (SS). A classical caspase substrate is poly(ADP-ribose)polymerase (PARP), a DNA repair enzyme. To elucidate the molecular mechanisms responsible for salivary gland dysfunction in SS, we studied the expression of caspase and PARP in SS salivary gland biopsies. METHODS: The presence of activated caspases (caspases 3 and 9) and cleaved PARP (85 kDa) in SS biopsies was demonstrated by immunohistochemistry using specific polyclonal antibodies. RESULTS: Initial studies performed with an antibody reagent that recognizes both active and inactive forms of caspase 3 identified this enzyme in SS salivary ductal and acinar cells. Activated caspase 3 and cleaved PARP were strongly expressed in ductal and acinar cells in SS salivary glands (13/15). Ductal and acinar cells from normal salivary glands (n=5) stained with less intensity compared with SS tissue. Staining for activated caspase 9 was negative in all samples. Likewise, infiltrating lymphocytes were negative for caspase 3, caspase 9 and cleaved PARP. CONCLUSION: This study shows that caspase 3 is important in the salivary dysfunction of SS, while caspase 9 appears not to be involved.


Subject(s)
Caspases/metabolism , Poly(ADP-ribose) Polymerases/metabolism , Salivary Glands/enzymology , Sjogren's Syndrome/enzymology , Apoptosis/physiology , Caspase 3 , Caspase 9 , Epithelial Cells/enzymology , Epithelial Cells/pathology , Fluorescent Antibody Technique, Indirect , Humans , Immunoenzyme Techniques , Salivary Glands/pathology , Sjogren's Syndrome/pathology
4.
Cell Signal ; 13(9): 617-24, 2001 Sep.
Article in English | MEDLINE | ID: mdl-11495719

ABSTRACT

Apoptosis plays an important role in the dysfunction of exocrine glands. Fas is a death-inducing receptor found on many types of cells including epithelial acinar cells. To elucidate the intracellular mechanism of Fas-mediated cell death in exocrine glands, an epithelial acinar cell line, SMG-C6, was studied. Caspase-1, -3, -8, and -9 activities were elevated in SMG-C6 cells after the induction of apoptosis by soluble Fas ligand (FasL). The activation of caspase-1 and -8 occurred prior to caspase-3 and -9 activation. The caspase-1 inhibitor, zYVAD-fmk, was effective in preventing cell death, whereas the caspase-3 and -8 inhibitors (ac-DEVD-CHO and ac-IETD-CHO, respectively) were not. zYVAD-fmk was able to inhibit caspase-3 activation indicating that caspase-1 is upstream to caspase-3. Furthermore, kinetic studies show that caspase-1 is an early event in the Fas apoptotic pathway. This study shows that caspase-1 participates in Fas-mediated apoptosis of epithelial cells by initiating the caspase cascade.


Subject(s)
Apoptosis , Caspase 1/metabolism , Membrane Glycoproteins/pharmacology , Salivary Glands/pathology , Sjogren's Syndrome/pathology , Animals , Caspase 3 , Caspase Inhibitors , Caspases/metabolism , Cell Line, Transformed , Cysteine Proteinase Inhibitors/pharmacology , Epithelial Cells/drug effects , Epithelial Cells/enzymology , Epithelial Cells/pathology , Fas Ligand Protein , Kinetics , Models, Biological , Rats , Salivary Glands/enzymology , Signal Transduction , Sjogren's Syndrome/enzymology
5.
Inflammation ; 25(2): 69-73, 2001 Apr.
Article in English | MEDLINE | ID: mdl-11321361

ABSTRACT

The TGF-beta1(-/-) mouse is a murine model for systemic autoimmune disease. The aim of this study is to elucidate the immunological mechanism that leads to multifocal tissue inflammation and autoantibody production in TGF-beta1(-/-) mice. Heart, lung, liver, and salivary gland from TGF-beta1(-/-) were assessed for CD154 expression by RT-PCR and immunohistochemistry. Compared to wild-type littermates, CD154 expression was elevated in all tissues studied. Furthermore, IL-12 mRNA was expressed in the salivary gland and heart of TGF-beta1(-/-) mice and not in wild-type littermates. This suggests that the CD154 pathway is activated in these tissues. This shows that TGF-beta1 regulates CD154 expression leading to spontaneous IL-12 production and autoimmunity.


Subject(s)
CD40 Ligand/genetics , CD40 Ligand/metabolism , Transforming Growth Factor beta/genetics , Animals , Autoimmunity , Immunohistochemistry , Inflammation/etiology , Inflammation/genetics , Inflammation/immunology , Interleukin-12/biosynthesis , Liver/immunology , Liver/metabolism , Lung/immunology , Lung/metabolism , Lymphocyte Activation , Mice , Mice, Inbred C57BL , Mice, Knockout , Myocardium/immunology , Myocardium/metabolism , RNA, Messenger/genetics , RNA, Messenger/metabolism , Salivary Glands/immunology , Salivary Glands/metabolism , T-Lymphocytes/immunology , Tissue Distribution , Transforming Growth Factor beta/metabolism , Up-Regulation
6.
Arthritis Rheum ; 44(3): 693-702, 2001 Mar.
Article in English | MEDLINE | ID: mdl-11263785

ABSTRACT

OBJECTIVE: Salivary gland epithelial cells in patients with Sjögren's syndrome (SS) and in NOD and NODscid mice express Fas and Fas ligand, and these cells die from apoptosis. To elucidate the intracellular molecular mechanisms responsible for this salivary gland epithelial cell apoptosis, expression of the Bcl-2 family of proteins (Bcl-2, Bcl-xL, Bax) and caspase (caspases 3 and 8) was studied in young (ages 8-10 weeks) and old (ages 17-28 weeks) NOD and NOD.scid mice. METHODS: Sections of frozen salivary gland tissue were obtained from NOD and NOD.scid mice and from the lip biopsy material of SS patients. Immunohistochemistry or Western blot analysis was performed to assess the apoptotic-associated proteins. RESULTS: Levels of Bax and caspase 3 were elevated in the epithelial cells of glands from old NOD mice, but not in those from young NOD mice. In contrast, epithelial cells from both young and old NOD.scid mice exhibited strong expression of Bax and caspase 3. Western blot analysis showed that the activated form of caspase 3 was increased 2-5-fold in the glands from old NOD, old NOD.scid, and young NOD.scid mice compared with those from young NOD mice. Caspase 3 was also significantly elevated (P < 0.01) in SS patients whose focus scores were grade 3 or 4. In the SS patients' biopsy tissue and in the mouse glands, cells with fragmented DNA were positive for caspase 3. CONCLUSION: These results demonstrate that salivary gland epithelial cells in NOD and NOD.scid mice overexpress the proapoptotic molecules Bax and caspase 3. Bax could be the gene responsible for initiation of caspase activation, epithelial cell destruction, and lymphocyte glandular localization in SS.


Subject(s)
Caspases/metabolism , Proto-Oncogene Proteins/metabolism , Sjogren's Syndrome/metabolism , Animals , Apoptosis/physiology , Caspase 3 , Disease Models, Animal , Enzyme Activation/physiology , Mice , Mice, Inbred BALB C , Mice, Inbred NOD , Mice, SCID , Proto-Oncogene Proteins c-bcl-2/metabolism , bcl-2-Associated X Protein
8.
Cell Death Differ ; 7(11): 1119-26, 2000 Nov.
Article in English | MEDLINE | ID: mdl-11139286

ABSTRACT

Salivary epithelial cells from patients with primary Sjögren's syndrome (SS) undergo Fas-mediated apoptosis. Bcl-2 and Bcl-xL are apoptosis suppressing oncogenes. Very little is known about the role of these oncogene molecules in salivary epithelial cells. To investigate the possible prevention of salivary glandular destruction in SS by Bcl-2 and Bcl-xL, stable transfectants expressing these molecules were made from HSY cells, a human salivary epithelial cell line. HSY cells were transfected with an expression vector for human Bcl-2 or Bcl-xL. Stable transfectants were selected and apoptosis was induced by anti-Fas antibody. Apoptosis was quantified by propidium iodide staining followed by flow cytometry. Caspase activity was detected by immunohistochemical analysis and enzyme cleavage of DEVD-AMC, a fluorescent substrate. Response to carbachol, a muscarinic receptor agonist, and EGF was measured by Ca2+ mobilization and influx. Fas-mediated apoptosis was significantly inhibited in Bcl-2 and Bcl-xL transfectants compared to wild-type and control transfectants (empty vector). Surprisingly, caspase activity was not inhibited in Bcl-2 and Bcl-xL transfectants. Activation of the Fas pathway in the Bcl-2 and Bcl-xL transfectants by antibody also inhibited carbachol and EGF responsiveness (i.e., Ca2+ mobilization and/or influx) by 50-60%. This Fas-mediated inhibition of cell activation was partially or completely restored by specific peptide interference of caspase enzyme activity. The prevention of Fas-mediated apoptosis by the overexpression of Bcl-2 and Bcl-xL in salivary gland epithelial cells results in injured cells expressing caspase activity and unable to respond normally to receptor agonists. Such damaged cells may exist in SS patients and could explain the severe dryness out of proportion to the actual number of apoptotic cells seen on salivary gland biopsy.


Subject(s)
Apoptosis , Epithelial Cells/metabolism , Proto-Oncogene Proteins c-bcl-2/metabolism , Salivary Glands/cytology , Sjogren's Syndrome/physiopathology , fas Receptor/metabolism , Calcium/metabolism , Carbachol/pharmacology , Cardiotonic Agents/pharmacology , Caspases/metabolism , Ceramides/metabolism , Epidermal Growth Factor/pharmacology , Epithelial Cells/cytology , Epithelial Cells/drug effects , Flow Cytometry , GTP-Binding Proteins/metabolism , Humans , Immunohistochemistry , Proto-Oncogene Proteins/metabolism , Proto-Oncogene Proteins c-bcl-2/genetics , Salivary Glands/metabolism , Signal Transduction/physiology , Transfection , Tumor Cells, Cultured , bcl-2-Associated X Protein , bcl-X Protein
9.
Scand J Immunol ; 50(5): 479-84, 1999 Nov.
Article in English | MEDLINE | ID: mdl-10564550

ABSTRACT

The induction of T-cell apoptosis is regulated in part by monocytes (CD14+ cells). Human peripheral blood monocytes inhibited the spontaneous cell death of activated T cells in vitro. The inhibition of T-cell apoptosis did not require autologous monocytes. Inhibition required direct contact with monocytes and was not due to a soluble factor. Furthermore, treatment of monocytes with actinomycin D, cycloheximide and paraformaldehyde abrogated the anti-apoptotic activity of these cells. Blocking antibody to CD40 and CD154 (CD40 ligand) decreased the ability of monocytes to aid in T-cell survival, whereas, blocking LFA-1/I-CAM-1, Fas ligand and the CD4/major histocompatibility complex class II interaction did not affect the influence of monocytes on T-cell survival. This shows that monocytes rescue of activated T cells from apoptosis is dependent upon CD40/CD154 interaction.


Subject(s)
Apoptosis/immunology , CD40 Antigens/metabolism , Membrane Glycoproteins/metabolism , Monocytes/immunology , T-Lymphocytes/cytology , T-Lymphocytes/immunology , Antibodies, Blocking/pharmacology , CD40 Ligand , Cycloheximide/pharmacology , Dactinomycin/pharmacology , Formaldehyde/pharmacology , Humans , In Vitro Techniques , Ligands , Lipopolysaccharide Receptors/metabolism , Lupus Erythematosus, Systemic/immunology , Lupus Erythematosus, Systemic/pathology , Lymphocyte Activation , Monocytes/drug effects , Polymers/pharmacology
12.
Cytokine ; 11(3): 187-91, 1999 Mar.
Article in English | MEDLINE | ID: mdl-10209065

ABSTRACT

T lymphocytes from several autoimmune diseases including rheumatoid arthritis (RA) and systemic lupus erythematosus (SLE) exhibit deficient mitogenic response in terms of proliferation and IL-2 production. The expression of the IL-2 gene is regulated by various transcription factors. One of these factors suppresses IL-2 expression and binds to the negative responsive element in the IL-2 gene 5' flanking region (NRE-A). The authors hypothesized that the decreased production of IL-2 by T cells from RA and SLE patients is at least partially caused by high expression of the NRE-A binding protein. To test this hypothesis T cells from healthy donors and patients with RA and SLE were stimulated. Using the electrophoretic mobility shift assay we detected NRE-A DNA-binding proteins in the nuclei of the stimulated cells. No difference was found between NRE-A DNA binding in nuclear extracts of T cells taken from healthy donors and those taken from patients. The specificity of the DNA-protein interactions was ascertained through the use of unlabeled DNA competitors. No correlation was found between DNA-binding and the patients' disease duration or medication. In conclusion, decreased IL-2 biosynthesis by T lymphocytes from RA and SLE patients can not be explained by abnormal expression of the NRE-A DNA-binding protein.


Subject(s)
DNA-Binding Proteins/metabolism , Interleukin-2/genetics , Nuclear Proteins/metabolism , Adult , Aged , Arthritis, Rheumatoid/genetics , Arthritis, Rheumatoid/immunology , Arthritis, Rheumatoid/metabolism , Binding Sites/genetics , Case-Control Studies , Female , Humans , In Vitro Techniques , Interleukin-2/biosynthesis , Lupus Erythematosus, Systemic/genetics , Lupus Erythematosus, Systemic/immunology , Lupus Erythematosus, Systemic/metabolism , Lymphocyte Activation , Male , Middle Aged , T-Lymphocytes/immunology , T-Lymphocytes/metabolism
13.
Clin Exp Rheumatol ; 16(6): 675-81, 1998.
Article in English | MEDLINE | ID: mdl-9844759

ABSTRACT

OBJECTIVE: The lesion is Sjögren's syndrome consists of lymphocytic infiltration and has a pathology characteristic of the potential apoptotic death of salivary gland secretory epithelial cells. To examine the role of the glandular epithelial cells in the pathogenesis of autoimmune exocrinopathy, we studied Fas and Fas ligand (FasL) expression and quantitated the levels of apoptosis in salivary and lacrimal glands from NOD and NOD-scid mice, an animal model that develops a Sjögren's syndrome-like pathology. METHODS: The parotid, submandibular and lacrimal tissues of NOD, NOD-scid, and BALB/c mice were evaluated by immunohistochemical analysis for the expression of Fas and FasL. Nuclear fragmentation of DNA from the epithelial cells of exocrine tissues was evaluated by the terminal UTP nucleotide end labeling method (TUNEL). Messenger RNA was isolated from 8 and 18 week old mice and was analyzed by the reverse transcription-polymerase chain reaction (RT-PCR) for the expression of Fas and FasL. RESULTS: We found suggestive evidence that apoptosis of the secretory epithelial cells occurs in both NOD and NOD-scid mice despite the lack of T- and B-lymphocytes in the latter. FasL mRNA and cell surface protein were expressed in salivary and lacrimal gland epithelial cells from 8 and 18 week old NOD, NOD-scid, and BALB/c mice. Fas protein and mRNA were expressed only in the exocrine glands from 18 week old NOD and NOD-scid mice. Glandular secretory epithelial cell apoptosis was elevated in both NOD and NOD-scid mice, however; there was little evidence of apoptosis in the control strain of BALB/c mice. CONCLUSION: These results suggest a potential apoptotic process dependent on Fas:FasL interactions occurring in NOD-scid glandular secretory epithelial cells in the absence of lymphocytic infiltration.


Subject(s)
Apoptosis , Lacrimal Apparatus/metabolism , Membrane Glycoproteins/metabolism , Salivary Glands/metabolism , Sjogren's Syndrome/metabolism , fas Receptor/metabolism , Animals , Cell Count , DNA Primers/chemistry , Epithelial Cells/metabolism , Epithelial Cells/pathology , Fas Ligand Protein , Immunoenzyme Techniques , In Situ Nick-End Labeling , Lacrimal Apparatus/pathology , Membrane Glycoproteins/genetics , Mice , Mice, Inbred BALB C , Mice, Inbred NOD , Mice, SCID , RNA, Messenger/biosynthesis , Salivary Glands/pathology , Sjogren's Syndrome/pathology , fas Receptor/genetics
14.
Eur J Immunol ; 28(9): 2648-60, 1998 Sep.
Article in English | MEDLINE | ID: mdl-9754553

ABSTRACT

Fas (CD95) is a cell surface receptor whose biological function in circulating peripheral T cells is not well understood. To address the question of abnormal T cell sensitivity to Fas stimulation in systemic lupus erythematosus (SLE), we studied Fas-transduced stimulation and apoptosis in peripheral blood T cells from patients with SLE and normal control. Immobilized anti-Fas monoclonal antibodies (mAb) (imCH-11; IgM type) significantly stimulated SLE T cell proliferation compared to T cells from normal donors and patients with rheumatoid arthritis (p < 0.003 and p < 0.005, respectively). The soluble form of CH-11 and other immobilized anti-Fas mAb (UB-2, ZB-4; IgG type) failed to stimulate lupus T cells while immobilized human Fas ligand did. Furthermore, imCH-11 induced IL-2 and IL-6 mRNA expression. However, imCH-11 activation failed to induce expression of the T cell activation surface molecules CD25 and CD69. Addition of exogenous ceramide, a second messenger for Fas-mediated apoptosis signaling, also induced T cell proliferation in SLE and normal controls. Moreover, fumonisin B1, a specific ceramide synthase inhibitor, and caspase inhibitors markedly suppressed imCH-11 induced T cell proliferation, suggesting that the ceramide pathway may be involved in Fas-transduced stimulation signals in SLE T cells. These results show that SLE T cells have an alteration in the Fas signal transduction pathway leading to cell proliferation. This defect may be important in Fas-mediated peripheral immune homeostasis.


Subject(s)
Lupus Erythematosus, Systemic/immunology , Lymphocyte Activation/immunology , Signal Transduction/immunology , T-Lymphocytes/immunology , fas Receptor/immunology , Adult , Antigens, CD/immunology , Antigens, Differentiation, T-Lymphocyte/immunology , Cell Division/immunology , Cells, Cultured , Female , Humans , Lectins, C-Type , Male , Middle Aged , Receptors, Interleukin-2/immunology
15.
Clin Immunol Immunopathol ; 88(2): 133-41, 1998 Aug.
Article in English | MEDLINE | ID: mdl-9714690

ABSTRACT

To investigate the molecular mechanism of glandular parenchyma destruction in Sjögren's syndrome (SS), Bcl-2, Bax, Bcl-X, and Bak expression were studied. SS (n = 18) and control salivary glands (n = 6) were examined by immunohistochemistry. Apoptosis was assessed by in situ DNA nick end labeling. Infiltrating mononuclear cells in the SS salivary gland showed elevated Bcl-2. These mononuclear cells expressed increased Bax but did not undergo apoptosis. Both SS and control salivary gland ductal epithelial cells expressed Bcl-2, Bax, and Bcl-X. SS, but not normal, salivary gland acinar cells expressed Bax and underwent apoptosis. These results suggest that elevated Bax expression in SS salivary gland acinar cells may play an important role in the apoptotic pathway. In contrast, Bcl-2 expression in SS infiltrating mononuclear cells and ductal cells may contribute to their survival.


Subject(s)
Proto-Oncogene Proteins c-bcl-2/biosynthesis , Salivary Glands/metabolism , Sjogren's Syndrome/metabolism , Apoptosis/physiology , Epithelium/metabolism , Epithelium/physiology , Female , Humans , Leukocytes, Mononuclear/metabolism , Membrane Proteins/biosynthesis , Middle Aged , Proto-Oncogene Proteins/biosynthesis , Proto-Oncogene Proteins/physiology , Proto-Oncogene Proteins c-bcl-2/physiology , Salivary Ducts/chemistry , Salivary Ducts/cytology , Salivary Ducts/metabolism , Salivary Glands/chemistry , Salivary Glands/pathology , bcl-2 Homologous Antagonist-Killer Protein , bcl-2-Associated X Protein , bcl-X Protein
16.
J Rheumatol ; 25(6): 1226-31, 1998 Jun.
Article in English | MEDLINE | ID: mdl-9632092

ABSTRACT

We describe a 49-year-old patient with lip biopsy proven Sjögren's syndrome (SS) and keratoconjunctivitis sicca, who had dental caries, xerostomia, recurrent upper respiratory tract infections, arthritis in her hands, elbows and knees, and recurrent parotid inflammation. She developed bilateral breast nodules in 1988. Right breast nodules were excised in 1993 and 1995, but reappeared in 1996, requiring 2 more excisions. Breast tissue samples showed remarkable intralobular and perilobular mononuclear cell infiltrates that were predominantly CD4+ T cells and expressed bcl-2. A few cells stained CD20+ and CD8+. SS breast glandular epithelial cells stained more intensely for Fas compared to normal cells. CD4+ T cells and Fas mediated cell death may be involved in the mammary gland lesions in SS.


Subject(s)
Breast Diseases/pathology , CD4-Positive T-Lymphocytes/pathology , Membrane Glycoproteins/metabolism , Sjogren's Syndrome/pathology , fas Receptor/metabolism , Breast/metabolism , Breast/pathology , Breast Diseases/metabolism , CD4-Positive T-Lymphocytes/metabolism , Epithelium/metabolism , Epithelium/pathology , Fas Ligand Protein , Female , Humans , Immunoenzyme Techniques , Keratoconjunctivitis Sicca/pathology , Middle Aged , Proto-Oncogene Proteins c-bcl-2/metabolism , Sjogren's Syndrome/metabolism , Xerostomia/pathology
20.
J Immunol ; 158(11): 5527-35, 1997 Jun 01.
Article in English | MEDLINE | ID: mdl-9164977

ABSTRACT

Mice homozygous for a disrupted TGF-beta1 allele develop multiple lymphoproliferative disorders similar to those seen in the pseudolymphoma of Sjögren's syndrome. At 2 wk of age, these TGF-beta1 mutant mice begin to develop wasting syndrome and die at around 4 to 5 wk of age. We studied salivary glands from symptomatic mutant mice >14 days of age. Reverse transcriptase-PCR analysis showed up-regulation of proinflammatory cytokine genes such as IL-1alpha, IL-1beta, IL-2, IL-4, IL-6, IL-10, and IFN-gamma in these mutant mice. Enhanced expression of intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule (VCAM-1), and MHC class II as well as CD4-positive T lymphocyte infiltration was detected by immunostaining. To elucidate the role of MHC class II, salivary glands from TGF-beta1/MHC class II double knockout mice were used to investigate the expression of adhesion molecules and MHC class II. In spite of the existence of basal intercellular adhesion molecule-1 expression on vessels, there was neither MHC class II expression, enhanced vascular cell adhesion molecule-1 expression, nor lymphocytic infiltration in the salivary glands. These results suggest that MHC class II plays a significant role in the pathogenesis of TGF-beta1 mutant mice. Although the mechanism that initiates multiple inflammatory diseases in these mice remains unclear, the context reported here would provide insight into the immunopathology of Sjögren's syndrome.


Subject(s)
Cell Adhesion Molecules/immunology , Cytokines/immunology , Histocompatibility Antigens Class II/immunology , Salivary Glands/immunology , Transforming Growth Factor beta/immunology , Animals , Cell Adhesion Molecules/biosynthesis , Cytokines/biosynthesis , Histocompatibility Antigens Class II/biosynthesis , Mice , Mice, Knockout , RNA, Messenger/biosynthesis , Transforming Growth Factor beta/deficiency , Transforming Growth Factor beta/genetics , Up-Regulation
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