TLDR Hair follicles have unique proteins that vary by species and are influenced by nutrition.
The document discussed unique keratin proteins found in hair and wool, specifically high-glycine/tyrosine (HGT) proteins, ultra-high-sulphur (UHS) proteins, and trichohyalin protein. These proteins serve as matrices associated with intermediate filaments and vary between species, with nutritional status affecting their abundance in sheep. HGT proteins were not found in human hair, suggesting modulation in their expression. UHS proteins, with high cysteine content, increase in expression with more available cysteine. A human UHS gene was isolated for further study. Trichohyalin protein, found in the inner root sheath, undergoes significant changes during cell differentiation. The study also noted arginyl-tRNA transferase activity in hair follicles, which may play a role in protein processing.
116 citations
,
April 1986 in “The journal of cell biology/The Journal of cell biology” Trichohyalin is a protein in hair follicles that helps form hair filaments.
45 citations
,
January 1986 8 citations
,
November 1976 in “Journal of Investigative Dermatology” 125 citations
,
February 1971 in “Biochemistry” Specific cross-linkages help make hair proteins stable and strong.
50 citations
,
July 2008 in “British Journal of Dermatology” 138 citations
,
March 2007 in “Experimental cell research” Only a few hair-specific keratins are linked to inherited hair disorders.
276 citations
,
January 2005 in “International review of cytology” More research is needed to understand how hair keratins work and their role in hair disorders.
199 citations
,
January 2004 in “The International Journal of Developmental Biology” Hair follicle growth and development are controlled by specific genes and molecular signals.
29 citations
,
April 2003 in “Experimental dermatology” Human hair follicles grown in vitro maintain normal keratin patterns and structure.
