Transglutaminase forms midkine homodimers in cerebellar neurons and modulates the neurite-outgrowth response.
Transglutaminase forms midkine homodimers in cerebellar neurons and modulates the neurite-outgrowth response.
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转谷氨酰胺酶在小脑神经元中形成中期因子同型二聚体并调节神经突生长反应。
DOI:
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发表时间:
1996
期刊:
影响因子:
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通讯作者:
L. Haynes
中科院分区:
文献类型:
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作者:
S. Mahoney;M. Perry;A. Seddon;P. Bőhlen;L. Haynes
Midkine is a prominent acyl donor substrate for the protein cross-linking enzyme transglutaminase type 2 in rat brain neurons. Transglutaminase type 2 and midkine immunoreactivity are regionally colocalized in developing cerebellar cortex. Monomeric midkine is present in the embryonic dorsal rhombic lip which gives rise to the cerebellar cortex. A high-molecular weight (29-30 kDa) midkine appears during postnatal cerebellar development. The presence of the high-molecular weight midkine in cultured cerebellar cortical interneurons is dependent upon culture conditions. Transglutaminase catalyzes the calcium-dependent cross-linking of midkine predominantly into 29-30 kDa dimers. Dimer-formation of midkine in vitro and in cultured neurons is reduced in the presence of a transglutaminase inactivator. Neurons plated onto previously cross-linked midkine exhibit larger growth cones and enhanced neurite outgrowth compared to those plated onto monomeric midkine alone.