Abstract
Introduction: In order to clarify the mechanism of hair growth induced by biotin, we compared the serum proteins before and after the oral biotin administration. Materials and methods: The serum of three biotin-deficient children with alopecia were studied. Oral biotin administration was performed. Component proteins of serum were studied by using unique quantitative proteinmicrosequencing- deciphering method. Results: Hydrophobic membrane-proteins of ultra-high-sulphur keratin-associated protein was detected in the serum of biotin-deficient children with alopecia. This membrane protein in the serum disappeared after the biotin administration. This phenomenon is significant (p<0.05; Mann-Whitney’s U test). Conclusion: Biotin deficiency in children induced the excretion of membrane proteins into the blood, and biotin administration prevented this phenomenon. Therefore, biotin was expected to regulate the expression of membrane proteins.
Highlights
In order to clarify the mechanism of hair growth induced by biotin, we compared the serum proteins before and after the oral biotin administration
Hydrophobic membrane-proteins of ultra-high-sulphur keratin-associated protein was detected in the serum of biotin-deficient children with alopecia
Biotin deficiency in children induced the excretion of membrane proteins into the blood, and biotin administration prevented this phenomenon
Summary
In order to clarify the mechanism of hair growth induced by biotin, we compared the serum proteins before and after the oral biotin administration. Serum proteins of this patient are comparatively studied during biotin administration by using protein-direct-microsequencing deciphering (PDMD) method. This proteomics based upon the Edman-degradation [2] is general and quantitative identification method, which is applicable to tissue and cellular proteins [3]. We report that ultra-high-sulphur keratin-associated protein (UHS-KAP) [4] and olfactory receptor (OR) [5] appear in the alopecia children’s sera, and disappear by the biotin administration. We describe a finding that adult sera contain very-large protein-fragments of connectin/titin (mean molecular weight; 2,000,000) [8], which is absent in children’s sera
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