Trimble W S
Department of Physiology, University of Toronto, Ontario, Canada.
J Physiol Paris. 1993;87(2):107-15. doi: 10.1016/0928-4257(93)90004-d.
VAMP/synaptobrevin proteins were first discovered as small integral membrane proteins in synaptic vesicles of vertebrates and invertebrates. At least two isoforms are expressed in the central nervous system of mammals in non-overlapping patterns. Biochemical studies have revealed that the VAMP synaptic vesicle proteins are the specific target in the presynaptic nerve terminal of botulinum B neurotoxin and tetanus toxin metalloendoprotease activities. The fact that these toxins rapidly and completely abrogate neurotransmission suggests that VAMP proteins play an essential role in this process. More recently, immunologically related proteins have been identified in non-neuronal cells such as adipocytes. In addition, molecular genetic studies of yeast secretion have identified VAMP-related proteins as playing important roles in vesicular transport between the endoreticulum and Golgi. Taken together, these results suggest that the VAMP proteins found on synaptic vesicles might represent specialized forms of proteins which participate in general aspects of cell membrane trafficking.
VAMP/突触小泡蛋白最初是在脊椎动物和无脊椎动物的突触小泡中作为小的整合膜蛋白被发现的。至少两种亚型以不重叠的模式在哺乳动物的中枢神经系统中表达。生化研究表明，VAMP突触小泡蛋白是肉毒杆菌B型神经毒素和破伤风毒素金属内蛋白酶活性在突触前神经末梢的特异性靶点。这些毒素能迅速且完全消除神经传递这一事实表明，VAMP蛋白在这一过程中起重要作用。最近，在非神经元细胞如脂肪细胞中发现了免疫相关蛋白。此外，酵母分泌的分子遗传学研究已确定VAMP相关蛋白在内质网和高尔基体之间的囊泡运输中起重要作用。综上所述，这些结果表明，在突触小泡上发现的VAMP蛋白可能代表参与细胞膜运输一般过程的蛋白质的特殊形式。
