# Hedione increases one night stands and sex behavior in women

**URL:** <https://pheromonetalk.com/t/hedione-increases-one-night-stands-and-sex-behavior-in-women/67685>\
**Category:** Pheromone Theory & Molecules\
**Created:** [April 19, 2018, 9:45pm UTC](https://pheromonetalk.com/t/hedione-increases-one-night-stands-and-sex-behavior-in-women/67685 "2018-04-19T21:45:18Z")\
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**Author:** ![datadragon](https://sea2.discourse-cdn.com/flex016/user_avatar/pheromonetalk.com/datadragon/32/1252_2.png) [@datadragon](https://pheromonetalk.com/u/datadragon)\
**Post date:** [May 23, 2018, 5:10pm UTC](https://pheromonetalk.com/t/hedione-increases-one-night-stands-and-sex-behavior-in-women/67685/8 "2018-05-23T17:10:13Z")

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Another method of Pheromone transport: (Lipocalin - wikipedia)  
The lipocalin family has been connected with the transport of mammalian pheromones due to easily observable protein-pheromone interactions. Lipocalins have been detected as carrier proteins of important pheromones in the nasal mucus of rodents. Major urinary proteins, a lipocalin subfamily, are found in mouse and rat urine and may act as protein pheromones themselves.

[https://onlinelibrary.wiley.com/doi/full/10.1002/ar.a.20125](https://onlinelibrary.wiley.com/doi/full/10.1002/ar.a.20125)

They further demonstrate the similarity between human axillary secretions and nonhuman mammalian odor sources where lipocalins carry chemical signals used in pheromonal communication. In rodents (Novotny, 2003), pigs (Spinelli et al., 2002), and hamsters (Singer et al., 1989), volatile molecules appear to be bound to lipocalin proteins that transport them and are in part responsible for some of the activity. Hence, the chemistry of human axillary secretions appears to be analogous to other mammalian pheromone systems, an interesting and thought‐provoking analogy.

Humans also have lipocalin protein transporters:  
[http://www.pnas.org/content/pnas/93/13/6626.full.pdf](http://www.pnas.org/content/pnas/93/13/6626.full.pdf)

A human lipocalin protein transporter, apolipoprotein D, was recently found expressed in apocrine sweat glands, and was shown to bind the axillary odorant, E-3-methyl-2-hexenoic acid (E-3M2H). These results further suggest a remarkable similarity between human axillary secretions and nonhuman mammalian odor sources, where lipocalins have been shown to carry the odor signals used in pheromonal communication.

In pigs pheromones such as androstenol and androstenone are first bound to a lipocalin transporter:  
[https://pdfs.semanticscholar.org/6ce3/9d8255be785e67c406435ab45ca06a08e429.pdf](https://pdfs.semanticscholar.org/6ce3/9d8255be785e67c406435ab45ca06a08e429.pdf)

Low molecular mass proteins are implicated in chemical communication throughout mammalian species, and are involved in both perception and delivery of pheromonal  
compounds. The submaxillary glands of the male pig secrete large quantities of saliva when aroused by female pigs. The presence of pheromones within the saliva cause oestrous sows to take up the mating stance. These pheromones are the 16-androstene steroids, 5a-androsten-3a-ol (Androstenol) and 5a-androsten-3-one (Androstenone). Biochemical studies have shown that the submaxillary glands of pigs, particularly Gottingen boars, contain a low molecular mass protein, pheromaxein, which is capable of binding these 16-androstene steroids. When the binding affinities of various steroids to pheromaxein were assessed relative to 5a-androsten-3-one (100%) at 50% binding of 5a-[3 H]androsten-3-one, all 16-androstenes tested had strong affinities for pheromaxein, with 4,16-androstadienone the highest at 176%. Other steroids, which had poor binding affinities, were saturated at the C16 position and reduced at C5. In general, 5a-androstanes bound better than 5b-androstanes.

[https://pheromonetalk.com/t/human-lipocalin-protein-patents/4353](https://pheromonetalk.com/t/human-lipocalin-protein-patents/4353)

Booth and White reported a partially characterized porcine extracellular protein, pheromaxein, that binds androstenol and related steroids in boar submaxillary gland saliva (Booth and White, J. Endrocr. 118:47 (1988)). A salivary gland lipocalin, which binds 16-androstrenes, was later isolated from boar submaxillary gland (Marchese et al., Eur. J. Biochem. 252:563 (1998)). A cDNA encoding this protein, termed sex-specific salivary lipocalin (SAL), was recently reported, and shown to encode a polypeptide with high homology to the murine MUPs (Loebel et al., Biochem. J. 350:369 (2000)). It is not known whether boar SAL or pheromaxein has phermone activity itself, or only contributes to the phermone activity of cognate androstene ligands. Human homologs of boar pheromaxein or SAL have not been characterized.

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