TY - JOUR
T1 - Participation of the C-type hemolymph lectin in mineralization of the acorn barnacle Megabalanus rosa
AU - Kamiya, H.
AU - Jimbo, M.
AU - Yako, H.
AU - Muramoto, K.
AU - Nakamura, O.
AU - Kado, R.
AU - Watanabe, T.
N1 - Funding Information:
Acknowledgements The study was funded in part by a grant-in-aid for scientific research from the Ministry of Education, Culture, Sport, Science, and Technology, Japan, to K.M. (13556031), by a Yumekendo-Iwate research and promotion project to H.K., and by a grant from New Energy and Industrial Technology Development Organization to H.K. (1994).
PY - 2002
Y1 - 2002
N2 - BRA-2, a major C-type lectin in the hemolymph of the acorn barnacle Megabalanus rosa was detected in shell-associated proteins. Immobilized BRA-2 promoted CaCO3 crystallization as determined by an in vitro pH-drift mineralization assay. In nature, calcification occurs as wound repair in M. rosa after breakage of the shell plate. To observe this phenomenon, we inserted a rubber cube inside the mantle cavity of M. rosa through the basal plate, and kept the organisms in a tank for several weeks. The rubber cube was covered first with brownish-colored material, probably a melanin, and then with CaCO3 5 weeks after the insertion. In the CaCO3-associated proteins, BRA-3, a minor component of M. rosa hemolymph lectins, was present in addition to BRA-2. The presence of both the lectins and their ligands on the hemocyte was also observed. These results suggest that the C-type lectins of the M. rosa hemolymph participate in mineralization as well as defense in these organisms.
AB - BRA-2, a major C-type lectin in the hemolymph of the acorn barnacle Megabalanus rosa was detected in shell-associated proteins. Immobilized BRA-2 promoted CaCO3 crystallization as determined by an in vitro pH-drift mineralization assay. In nature, calcification occurs as wound repair in M. rosa after breakage of the shell plate. To observe this phenomenon, we inserted a rubber cube inside the mantle cavity of M. rosa through the basal plate, and kept the organisms in a tank for several weeks. The rubber cube was covered first with brownish-colored material, probably a melanin, and then with CaCO3 5 weeks after the insertion. In the CaCO3-associated proteins, BRA-3, a minor component of M. rosa hemolymph lectins, was present in addition to BRA-2. The presence of both the lectins and their ligands on the hemocyte was also observed. These results suggest that the C-type lectins of the M. rosa hemolymph participate in mineralization as well as defense in these organisms.
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U2 - 10.1007/s00227-002-0789-6
DO - 10.1007/s00227-002-0789-6
M3 - Article
AN - SCOPUS:0036940645
VL - 140
SP - 1235
EP - 1240
JO - Marine Biology
JF - Marine Biology
SN - 0025-3162
IS - 6
ER -