Japanese cedar and cypress pollinosis updated: New allergens, cross-reactivity, and treatment.

Pollen from many tree species in the Cupressaceae family is a well-known cause of seasonal allergic diseases worldwide. Japanese cedar pollinosis and Japanese cypress pollinosis, which are caused by pollen from Japanese cedar (Cryptomeria japonica) and Japanese cypress (Chamaecyparis obtusa), respectively, are the most prevalent seasonal allergic diseases in Japan. Recently, the novel major Japanese cypress allergen Cha o 3 and the homologous Japanese cedar allergen Cry j cellulase were identified, and it was shown, for the first time, that cellulase in plants is allergenic. Although the allergenic components of pollen from both species exhibit high amino acid sequence identity, their pollinosis responded differently to allergen-specific immunotherapy (ASIT) using a standardized extract of Japanese cedar pollen. Pharmacotherapy and ASIT for Japanese cedar and cypress pollinosis have advanced considerably in recent years. In particular, Japanese cedar ASIT has entered a new phase, primarily in response to the generation of updated efficacy data and the development of new formulations. In this review, we focus on both Japanese cypress and cedar pollinosis, and discuss the latest findings, newly identified causative allergens, and new treatments. To manage pollinosis symptoms during spring effectively, ASIT for both Japanese cedar and Japanese cypress pollen is considered necessary.

Differential ethylene-inducible expression of cellulase in pepper plants.

Ethylene promotes the abscission of leaves and the ripening of fruits in pepper plants, and in both events an increase in cellulase activity is observed. However, two enzyme isoforms (pI 7.2 and 8.5, respectively) are differentially involved in the two physiological phenomena. The pI 8.5 form has been purified from ripe fruits. It is a glycoprotein with an apparent molecular mass of 54 kDa. Two short peptides were sequenced and a very high homology to a tomato cellulase was observed. Polyclonal antibodies, raised against the purified enzyme, have allowed us to demonstrate that the observed ethylene-induced increase in cellulase activity is paralleled by de novo synthesis of protein. Three cDNAs (CX1, CX2 and CX3), encoding different cellulases, were obtained and characterized and their expression investigated. Accumulation of all three mRNAs is induced by ethylene treatment, though to different levels. CX1 is mainly expressed in ripe fruits while CX2 is especially found in abscission zones. CX3 accumulates at very low levels in activated abscission zones. Comparisons with other known cellulases demonstrate clear heterogeneity within the higher plant cellulases. Differences in ethylene inducibility and molecular structure suggest different physiological roles for cellulase in pepper plants.

Endo-1,4-beta-glucanase in the cell wall of stems of auxin-treated pea seedlings.

Endo-1,4-beta-glucanase induced by treatment of pea seedlings with 2,4-D was extracted from a preparation of the walls of epicotyl cells. The beta-glucanase was purified by chromatography on DEAE-cellulose, affinity chromatography on Con A-Sepharose and SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The activity of beta-glucanase was retained after removal of SDS and extraction from polyacrylamide gels. The band of a protein (46 kDa), that corresponded to the activity of endo-1,4-beta-glucanase, was injected directly into mice for preparation of antiserum and the protein was also subjected to amino acid sequencing after blotting onto a membrane. Western blot analysis showed that the antiserum obtained bound to a 46-kDa polypeptide and recognized endo-1,4-beta-glucanase. The N-terminal sequence of the 46-kDa polypeptide revealed some homology to abscission endo-1,4-beta-glucanases of bean and avocado fruit.