Spermine
Spermine is a polyamine involved in cellular metabolism found in all eukaryotic cells. The precursor for synthesis of spermine is the amino acid arginine, and the enzymatic production involves the enzymes ornithine decarboxylase, S-adenosylmethionine decarboxylase, and spermidine synthase.
Etymology[edit | edit source]
The term "spermine" was first coined by the German physiologist Johannes Peter Müller. It is derived from the word "sperm," as it was first isolated from semen.
Structure and Properties[edit | edit source]
Spermine is a tetravalent cationic molecule. It has a linear structure with four amine groups, and is fully protonated at physiological pH. The molecule is highly flexible and can adopt numerous conformations due to the rotation around its single bonds.
Biological Role[edit | edit source]
Spermine plays a crucial role in the stabilization of DNA structure, regulation of ion channels, and modulation of cell growth and proliferation. It is also involved in the regulation of protein synthesis and RNA processing.
Synthesis[edit | edit source]
The synthesis of spermine from arginine involves several steps. First, arginine is converted to ornithine and then to putrescine by the action of ornithine decarboxylase. Putrescine is then converted to spermidine by spermidine synthase. Finally, spermidine is converted to spermine by spermine synthase.
Clinical Significance[edit | edit source]
Abnormal levels of spermine have been associated with various diseases, including cancer, cardiovascular disease, and neurological disorders. In cancer, increased levels of spermine have been observed, and inhibition of spermine synthesis has been proposed as a potential therapeutic strategy.
See Also[edit | edit source]
References[edit | edit source]
Spermine Resources | |
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Contributors: Prab R. Tumpati, MD