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A human axillary odorant is carried by apolipoprotein D
C Zeng1, A I Spielman, B R Vowels
1Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA.
Summary
Human axillary odor is linked to E-3-methyl-2-hexenoic acid (E-3M2H) bound to apolipoprotein D (apoD). This protein, synthesized in apocrine glands, plays a role in body odor formation and potentially pheromonal communication.
Area of Science:
- Biochemistry
- Human Physiology
- Olfactory Communication
Background:
- Human axillary odor is biologically significant, influencing menstrual cycles and originating from apocrine secretions.
- The primary odor component, E-3-methyl-2-hexenoic acid (E-3M2H), is bound to specific proteins in apocrine secretions.
- Two odor-binding proteins, ASOB1 and ASOB2, were identified in apocrine secretions.
Purpose of the Study:
- To elucidate the structural relationship between E-3M2H and its carrier protein.
- To determine the amino acid sequence and glycosylation pattern of ASOB2.
- To understand the role of apolipoprotein D (apoD) in human axillary odor formation.
Main Methods:
- Mass spectrometry was used to determine the amino acid sequence and glycosylation of ASOB2.
- In situ hybridization was employed to localize apoD mRNA synthesis in axillary tissue.
- Comparison of axillary apoD glycosylation with plasma apoD.
Main Results:
- ASOB2 was identified as apolipoprotein D (apoD), a lipocalin family member.
- The glycosylation pattern of axillary apoD differs from plasma apoD.
- ApoD mRNA synthesis is specific to the apocrine glands in the axillary region.
Conclusions:
- Human axillary apoD is synthesized in apocrine glands and differs from plasma apoD.
- Lipocalins, like apoD, are involved in carrying odor signals in human axillary secretions.
- This mechanism mirrors pheromonal communication systems found in other mammals.