Toward understanding barnacle cementing by characterization of one cement protein-100kDa in Amphibalanus amphitrite
Barnacle
0301 basic medicine
Settlement
Life Cycle Stages
Evolution
Molecular Sequence Data
Thoracica
Arthropod Proteins
03 medical and health sciences
Cement protein
Organ Specificity
Adhesives
Animals
Tissue Distribution
Amino Acid Sequence
Cp100k
DOI:
10.1016/j.bbrc.2017.11.101
Publication Date:
2017-11-20T03:33:55Z
AUTHORS (5)
ABSTRACT
Barnacles, as major fouling organisms, have attracted more attentions. It is no doubt that the study on cement proteins is required to illustrate the mechanism of barnacle cementing. A cement protein defined as Aa-cp100k was characterized from Amphibalanus amphitrite in this study. The amino acid sequence of Aa-cp100k was shown a high similarity to other three barnacles including Megabalanus rosa (Mr-cp100k), Tetraclita japonica formosana (Tj-cp100k) and Pollicipes pollicipes (Pp-cp100k). Moreover, the localization of Aa-cp100k in the vacuoles of cyprid β secretory cells and the adult cement gland cells by immunofluorescence microscopy, indicating that Aa-cp100k existed in both cyprid and adult barnacle. Aa-cp100k from basal plate could be dissolved in urea buffer without high concentration of dithiothreitol (DTT), different from that in Megabalanus rosa, implying diverse possible roles of cp100k in cementing.
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