Relationship between conformation and biological response for (1----3)-beta-D-glucans in the activation of coagulation factor G from limulus amebocyte lysate and host-mediated antitumor activity. Demonstration of single-helix conformation as a stimulant.
The relationship between the conformation of (1----3)-beta-D-glucans in gel or hydrated form and the stimulation of two types of biological responses, namely, activation of coagulation Factor G from limulus amebocyte lysate (LAL) and host-mediated antitumor activity was examined. Both types were activated by the single-helical conformation, as revealed by high-resolution, solid-state 13C-n.m.r. spectroscopy. The potency of activation of Factor G was increased over 100-fold by treatment with a NaOH solution which leads to a complete or partial conversion from the triple to the single helix. Such a single-helix specific response was also demonstrated for the antitumor activity of curdlan, although the distinction was less pronounced for branched (1----3)-beta-D-glucans. The presence of the single-helix conformation was observed in schizophyllan gel, even though the triple helix is the most stable form of branched glucans in aqueous media.
Saitô
H
H
Biophysics Division, National Cancer Center Research Institute, Tokyo, Japan.
Yoshioka
Y
Y
Uehara
N
N
Aketagawa
J
J
Tanaka
S
S
Shibata
Y
Y
D000818:Animals; D000970:Antineoplastic Agents / Q000737:chemistry / Q000494:pharmacology*; D001779:Blood Coagulation Factors / Q000378:metabolism*; D002236:Carbohydrate Conformation; D005260:Female; D005936:Glucans / Q000737:chemistry / Q000494:pharmacology*; D008033:Limulus Test; D051379:Mice; D008813:Mice, Inbred ICR; D012513:Sarcoma, Experimental / Q000188:drug therapy; D013329:Structure-Activity Relationship; D047071:beta-Glucans
D000970:Antineoplastic Agents; D001779:Blood Coagulation Factors; D005936:Glucans; D047071:beta-Glucans; C033363:beta-1,3-glucan