Enhancement by ganglioside GT1b of annexin I phosphorylation in bovine mammary gland in the presence of phosphatidylserine and Ca2+ |
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Authors: | Norio Katoh Toru Miyamoto |
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Affiliation: | (1) Laboratory of Biochemistry, National Institute of Animal Health, 3-1-1 Kannondai, 305 Tsukuba, Ibaraki, Japan;(2) Hokkaido Branch Laboratory, National Institute of Animal Health, 062 Sapporo, Japan |
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Abstract: | Ganglioside GT1b and, to a lesser extent, GD3, enhanced phosphorylation of a 36 kDa protein (the substrate of protein kinase
C) in the particulate fraction from bovine mammary gland. Sialic acids, asialogangliosides, and GM3 were without effect, and
GD1a conversely inhibited phosphorylation of the 36 kDa protein. The enhanced phosphorylation by GT1b required the simultaneous
presence of phosphatidylserine (PS) and Ca2+. The 36 kDa protein reacted with anti-annexin I in Western blot analysis. Addition of purified annexin I to the reaction
mixture containing the particulate fraction increased the extent of phosphorylated 36 kDa protein, and the phosphorylation
was further enhanced by GT1b. The enhanced phosphorylation of annexin I by GT1b was also dependent on PS and Ca2+. When annexin I was phosphorylated by purified protein kinase C, GT1b inhibited the annexin I phosphorylation. Addition of
epidermal growth factor or insulin to the particulate fraction had little effect on the enhancement. These results suggest
that an enzyme or enzymes other than protein kinase C, epidermal growth factor receptor kinase, or insulin receptor kinase
is responsible for the GT1b- and GD3-enhanced phosphorylation of annexin I in the presence of PS and Ca2+. |
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