Enzyme Inhibition Studies

Kanagewa et al. (2000) reported telomerase inhibition by a methanolic extract of C. sertularioides on a MOLT-4 cell culture at a level of 1.25% (v/v).

A comprehensive screening for phospholipase A2 (PLA2) inhibitors from marine seaweeds revealed that CYN and structurally related metabolites from C. prolifera, C. bikinensis and C. racemosa are highly active (Mayer et al., 1993). CYN isolated from C. prolifera in 4.2 mM concentration lead to a 92% inhibition of PLA2 activity. An esterase-based cleavage product (CYN lacking one acetyl group)

isolated from C. racemosa showed 26% inhibition at 3.9 mM concentration for PLA2. 12-Lipoxygenase inhibitory activity of C. taxifolia extracts was reported by Nimoniya et al. (1998).

Bitou et al. (1999) showed complete inhibition of lipase by purified CYN. According to their research, 50% inhibition was observed against triolein and 4-methylumbelliferyl oleate hydrolysis in 2 mM and 13 mM concentrations, respectively. Ben Rebah et al. (2008) showed that C. prolifera extract significantly decreased both dog gastric and human pancreatic lipase activities. Therefore, they proposed C. prolifera extract for the development of anti-obesity drugs.

Mao et al. (2006) discovered the two novel sesquiterpenoids, caulerpal A and B, from C. taxifolia. These two compounds have inhibitory property on the human protein tyrosine kinase. This enzyme is a target enzyme in the treatments of type-2 diabetes and obesity.

Inhibition of a-amylase by acetone extract of C. racemosa with an IC50 0.09 mg/mL value has been shown by Teixeira et al. (2007).

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