Systemic lupus erythematosus (SLE) is an autoimmune disease characterized by the production of several autoantibodies. Among the multiple factors involved in SLE development, apoptotic defects and impaired clearance of cellular debris have gained considerable interest, as they contribute to autoantigen overload. Several molecules of the innate immunity, also participate in the removal of damaged and apoptotic cells. Among them are C1q, C-reactive protein (CRP), serum amyloid P protein (SAP), mannose-binding lectin (MBL), and apolipoprotein A1 (APO A1). To evaluate the prevalence of autoantibodies against CRP, SAP, MBL, APO A1, and C1q among SLE patients, and their relationship with disease activity, a total of 150 SLE patients were screened for the presence of elevated antibody titers against C1q, CRP, SAP, MBL, and APO A1, utilizing the enzyme-linked immunosorbent assay (ELISA) method. Disease activity was assessed using the ECLAM or SLEDAI scores. The study population comprised two groups of patients: 100 patients with quiescent disease (median ECLAM score 2) comprised the first group, and 50 patients with active disease (median SLEDAI score 16) comprised group 2. Elevated titers of anti-CRP antibodies were significantly elevated only in group 1 (10% versus 4% of controls). Antibodies against SAP were evaluated only among patients in group 1, and were found at a significant high prevalence (20%). Elevated titers of anti-MBL antibodies were significantly elevated only in group 1 (15% versus 3.6%); and antibodies directed against APO A1 were significantly elevated in 21% of group 1, and 50% of group 2 patients. Elevated titers of anti-C1q were evaluated only in group 2, and were found at a significant prevalence of 66%. Significant correlation with disease activity was found only for anti-APO A1 antibodies, and only in group 1. Several patients harbored more than one of the autoantibodies tested. In patients with SLE, autoantibodies directed against protective molecules, that is, acute-phase proteins involved in the disposal of cellular and nuclear debris, can be detected. These autoantibodies may play a pathogenic role in the development or perpetuation of autoimmunity in SLE.

Atopic dermatitis (AD) is a chronic, recurrent pruritic skin disease with repeated remissions and exacerbations. Various factors, such as allergies, skin conditions and lifestyle, combine to cause AD, making it difficult to cure completely. Although AD symptoms are suppressed with medications, this is a long-term effort and burden on patients. Thus, safer drugs and alternatives are needed. We previously found that consumption of tea prepared from fig (Ficus carica L.) leaves alleviated allergy and AD symptoms in cultured cells and animals. Therefore, here, we conducted a double-blind, randomized, controlled study in patients with mild AD to evaluate the safety and AD-relieving effects of prolonged consumption of fig leaf tea. Positive effects of fig leaf tea consumption were confirmed in 14 of 15 participants. Eczema Area and Severity Index values were significantly lowered in the fig leaf tea-treated group than in the placebo-treated group. The effect weakened 4 weeks after the end of the intervention, suggesting that continued intake of fig leaf tea was effective. Further assessments confirmed the safety of fig leaf tea consumption and revealed no variations that might pose a health hazard. Therefore, we postulate that fig leaf tea is a natural and safe therapeutic option for AD.

In this study, I investigated the allergy suppressive effect of tea made from fig (Ficus carica L.) leaves. In the rat basophil cell line RBL-2H3, degranulation was significantly suppressed by treatment with fig tea at the same time as addition of IgE antibodies (sensitization). IgE bound to the cell surface was liberated in the medium depending on the treatment time with fig tea. Therefore, it was suggested that the mechanism of action of fig tea is promotion of dissociation of IgE from FcεRI receptors. Such a mechanism is novel in food materials. On oral administration to mice, fig tea showed an inhibitory effect on allergic dermatitis. Furthermore, in tests using an atopic dermatitis model in NC/Nga mice, continued administration of fig tea suppressed symptom exacerbation after antigen administration. Abbreviations AD: atopic dermatitis; β-Hex: β-hexosaminidase; FCM: flow cytometory; OA: oral administration; TA: transdermal administration

In this study, we characterized protease activities of 23 Ficus carica cultivars. Extracts of fruit, branch, and leaf of Masui Dauphine, one of the most representative F. carica cultivars in Japan, exhibited gelatin‐hydrolyzing activity, both in the absence and presence of a cysteine protease‐specific inhibitor, E‐64, suggesting that not only ficin (classified as cysteine protease) but also collagenase (classified as serine protease) were involved in the digestion of gelatin. In the hydrolysis of (7‐methoxycoumarin‐4‐yl)acetyl‐l‐Lys‐l‐Pro‐l‐Leu‐Gly‐l‐Leu‐[N3‐(2,4‐dinitrophenyl)‐l‐2,3‐diaminopropionyl]‐l‐Ala‐l‐Arg‐NH2, all branch extracts of 23 F. carica cultivars exhibited the activity both in the absence and presence of cysteine protease‐specific inhibitor E‐64, indicating that they contain ficin and collagenase. During digestion of acid‐solubilized type I collagen by the branch extract of Masui Dauphine at 40–55 °C, collagen was completely digested in the absence of E‐64, while it was partially digested in the presence of the inhibitor, indicating that the manner of digestion differed between ficin and collagenase contained in the extract. These results suggest that F. carica is attractive for industrial use to digest collagen. Practical Application The industrial use of F. carica might be enhanced by efficiently utilizing these proteases and/or selecting the appropriate F. carica cultivar. Collagen is one of the targets to which our results might be applied. It is widely accepted today that collagen and its digestion products could be useful as functional food. F. carica is a potential candidate for use in not only complete but also partial digestion of collagen.