Peptidylarginine Deiminase Isoforms Are Differentially Expressed in Anagen Hair Follicles and Other Human Skin Appendages

June 2005 in “ Journal of Investigative Dermatology ”

Rachida Nachat, Marie‐Claire Méchin, Marie Charvéron, Guy Serre, J. Constans, Michel Simon

peptidylarginine deiminase PAD1 PAD2 PAD3 anagen hair follicles inner root sheath trichohyalin medulla Henle layer hair follicle differentiation sweat glands arrector pili muscles sebaceous glands terminal differentiation hair growth PAD enzymes hair follicle growth hair structure

Studysummary This study demonstrates that PAD1 and PAD3 are involved in hair follicle differentiation, while PAD1 and PAD2 may play a role in the physiology of sweat glands and arrector pili muscles. Our plain-language summary of this paper — not a Tressless recommendation.

The study examined the expression of peptidylarginine deiminase (PAD) isoforms in human anagen hair follicles and other skin appendages. It found that PAD1 and PAD3 were expressed in the inner root sheath of hair follicles, with PAD3 deiminating trichohyalin in the medulla and Henle layer, suggesting their role in hair follicle differentiation. PAD1 and PAD2 were also present in sweat glands and arrector pili muscles, but not in sebaceous glands, indicating potential roles in the physiology of these structures. The research highlighted the importance of PADs in the terminal differentiation of hair follicles and suggested their involvement in hair growth and structure.

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research Trichohyalin Mechanically Strengthens the Hair Follicle

108 citations , October 2003 in “Journal of biological chemistry/The Journal of biological chemistry”

This study documents that trichohyalin acts as a multi-functional cross-bridging protein in the inner root sheath of mouse hair follicles, enhancing mechanical strength by linking keratin filaments to the cell envelope.

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130 citations , April 2003 in “Journal of Investigative Dermatology”

This study reports the cloning and expression details of two new human type II keratins, K6irs3 and K6irs4, in the hair follicle's inner root sheath, suggesting a distinct functional role related to hair structure.

research Selective Expression of Calcium-Binding Proteins S100A8 and S100A9 at Distinct Sites of Hair Follicles

22 citations , September 2001 in “Journal of Investigative Dermatology”

S100A8 and S100A9 proteins help form hair shafts during growth.

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124 citations , November 2000 in “The journal of investigative dermatology/Journal of investigative dermatology”

This study found that human peptidylarginine deiminase type III is the predominant isoform in hair follicles and may modulate structural proteins during hair and hair follicle formation.

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33 citations , August 2000 in “Experimental Cell Research”

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40 citations , April 1999 in “Journal of Histochemistry & Cytochemistry”

In this study, the researchers identified the specific subcellular localization of the protein S100A3 in the endocuticle and cortex of human hair shafts.

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139 citations , December 1998 in “The journal of investigative dermatology/Journal of investigative dermatology”

This study identified a new type II cytokeratin, named K6hf, exclusively expressed in the companion layer of the human hair follicle, distinguishing it from other keratins and suggesting a unique biochemical role.

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135 citations , October 1997 in “Journal of biological chemistry/The Journal of biological chemistry”

This study suggests that trichohyalin is modified by peptidyl-arginine deiminase before being cross-linked by TGase 3, allowing the formation of rigid structures in hair follicle cells.

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161 citations , June 1993 in “Journal of Biological Chemistry”

This study suggests that human trichohyalin may function as a flexible rod linking keratin intermediate filaments and as a scaffold protein in hair follicle and epidermis cell envelopes.

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72 citations , May 1993 in “The Journal of Cell Biology”

This study detailed the structure and amino acid composition of sheep trichohyalin, noting its presence in various tissues and suggesting a possible functional role beyond structural support in hair follicles.

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40 citations , March 1991 in “Journal of Investigative Dermatology”

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116 citations , April 1986 in “The journal of cell biology/The Journal of cell biology”

This study reports that a 190,000 molecular weight protein, identified as trichohyalin, may play a matrix role in the development of inner root sheaths in hair follicles.

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45 citations , January 1977 in “Advances in experimental medicine and biology”

Hair follicles have an enzyme that converts arginine to citrulline in proteins.

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In this study, researchers localized arginine and citrulline in rat hair follicles and found that arginine is abundant in trichohyalin droplets, while citrulline predominantly accumulates in the hardened inner sheath and medulla.