Identification and immunohistochemical localization of protein precursors to human axillary odors in apocrine glands and secretions

Andrew I. Spielman, Gulshan Sunavala, Judith A.K. Harmony, William D. Stuart, James J. Leyden, Gloria Turner, Benjamin R. Vowels, Wan C. Lam, Shinjun Yang, George Preti

Research output: Contribution to journalArticle

Abstract

Objectives: To determine the cellular localization in male and female axillary tissue for apocrine secretion odor-binding proteins 1 (ASOB1) and 2 (ASOB2) and the electrophoretic pattern of female apocrine proteins and to begin characterization of the ASOB1 protein. Design: Immunohistochemical techniques were used with biopsy samples from axillary tissue of male and female subjects. Immunological techniques and microsequencing were used to characterize several of the proteins in male and female apocrine secretions. Setting: A university medical center. Participants: Healthy male and female volunteers who donated apocrine secretions and/or axillary tissue. Results: Specific immunoreactivity was localized only to the apocrine glands in both sexes. Furthermore, only preabsorption with a mixed apocrine secretion sample eliminated all immunoreactivity. The electrophoretic pattern of proteins in female apocrine secretions is similar to that in male secretions. Western blotting of the separated proteins from female samples using serum samples containing antibodies to ASOB1 and ASOB2 yielded identical results to those found with separated proteins from male samples. Partial sequence data obtained from the N-terminus of ASOB1 suggested that it shares homology with the el-chain of apolipoprotein J (Apo J). Apocrine secretion odor-binding protein 1 is not immunologically similar to Apo J, but 2 other apocrine secretion proteins are. Conclusions: Male and female subjects appear to have the same glycoprotein carriers for (E)-3-methyl-2-hexenoic acid localized to the apocrine glands. The N-terminal sequence for ASOB1 may be homologous to Apo J, but it is not immunologically similar to it. However, 2 other proteins in the apocrine secretion appear to be the monomer and dimer forms of Apo J.

Original languageEnglish (US)
Pages (from-to)813-818
Number of pages6
JournalArchives of Dermatology
Volume134
Issue number7
DOIs
StatePublished - 1998

ASJC Scopus subject areas

  • Dermatology

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