Little was known about biological activities of compounds from the medicinal mushroom of the genus Pholiota. A lectin from the Pholiota adiposa has now been isolated and its properties tested. The isolation procedure included ion exchange chromatography on DEAE-cellulose and CM-cellulose, and fast protein liquid chromatography-gel filtration (FPLC) on Superdex 75. The lectin was composed of two identical subunits, each with a molecular mass of 16 kDa. Its N-terminal amino-acid sequence showed little similarity to sequences of other Agaricales lectins. The hemagglutinating activity of the lectin was stable at temperatures up to 50 degrees C, and in NaOH and HCl solutions with concentrations less than 25 mM. It was inhibited by inulin (12.5-200 mM), but enhanced by Cu(2+) (6.25-25 mM), Fe(2+) (12.5-25 mM), and Al(3+) (6.25-25 mM) ions. The lectin showed antiproliferative activity toward hepatoma Hep G2 cells and breast cancer MCF7 cells with an IC(50) of 2.1 microM and approximately 3.2 microM, respectively. It exhibited HIV-1 reverse transcriptase inhibitory activity with an IC(50) of 1.9 microM. When compared with P. aurivella lectin, the only Pholiota lectin published to date, P. adiposa lectin differs in chromatographic behavior, molecular mass, N-terminal sequence, and effect of cations on hemagglutinating activity. In the case of the lectin from P. aurivella, its antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities have not been determined.

Mushrooms are famous for their nutritional and medicinal values and also for the diversity of bioactive compounds they contain including lectins. The present review is an attempt to summarize and discuss data available on molecular weights, structures, biological properties, N-terminal sequences and possible applications of lectins from edible mushrooms. It further aims to update and discuss/examine the recent advancements in the study of these lectins regarding their structures, functions, and exploitable properties. A detailed tabling of all the available data for N-terminal sequences of these lectins is also presented here.

Hypertension is a major risk factor for cardiovascular disease. A crude water extract of the fruiting bodies of a highly prized mushroom Tricholoma matsutakei exerted an antihypertensive action on spontaneously hypertensive rats (SHRs) at a dosage of 400 mg/kg. An angiotensin converting enzyme (ACE) inhibitory peptide with an IC₅₀ of 0.40 μM was purified from the extract and designated as TMP. Its amino acid sequence was elucidated to be WALKGYK through LC-MS/MS analysis. The Lineweaver-Burk plot suggested that TMP was a non-competitive inhibitor of ACE. A short-term assay of antihypertensive activity demonstrated that TMP at the dosage of 25 mg/kg could significantly lower the systolic blood pressure (SBP) of SHRs. TMP exhibited remarkable stability over a wide range of temperatures and pH values. It also demonstrated 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity. The aforementioned activities of TMP were corroborated by utilizing the synthetic peptide. Hence T. matsutake can be used as a functional food to help prevent hypertension- associated diseases.