Molecular Cloning of Two Novel Types of Peptidylarginine Deiminase cDNAs from Retinoic Acid-Treated Culture of a Newborn Rat Keratinocyte Cell Line

August 1998 in “ FEBS Letters ”

Akihito Ishigami, Masashi Kuramoto, Michiyuki Yamada, Kazutada Watanabe, Tatsuo Senshu

peptidylarginine deiminase PAD retinoic acid keratinocyte epidermal differentiation protein deimination vitamin A acid skin cells skin differentiation

Studysummary In this study, researchers identified two novel peptidylarginine deiminases from treated rat keratinocytes, both showing enzyme activity with PAD‐R11 reflecting a characteristic of epidermal enzymes. Our plain-language summary of this paper — not a Tressless recommendation.

The study investigated the molecular cloning of two novel peptidylarginine deiminase (PAD) cDNAs, PAD-R11 and PAD-R4, from retinoic acid-treated newborn rat keratinocyte cells. These novel PADs showed significant sequence similarity to known PAD types II and III and demonstrated specific enzymatic activities, suggesting their involvement in epidermal differentiation. Northern blot analysis confirmed that retinoic acid induced the expression of these PAD mRNAs, indicating their potential roles in the terminal stages of epidermal differentiation. The study also identified PAD-R11 as encoding PAD type I and PAD-R4 as tentatively classified as type IV, with their expression modulated by retinoic acid, highlighting the need for further research on PAD expression and function in protein deimination during degenerative processes.

View this study on febs.onlinelibrary.wiley.com →

Discuss this study in the Community →

Research cited in this study

4 / 4 results

research Isolation and Molecular Cloning of Epidermal and Hair Follicle-Specific Peptidylarginine Deiminase Type III from Rat

42 citations , May 1997 in “The Journal of Biochemistry”

In this study, researchers purified and cloned rat peptidylarginine deiminase type III, demonstrating its activity and specific expression in the epidermis and hair follicles.

research The Structure of Human Trichohyalin: Potential Multiple Roles as a Functional EF-Hand-Like Calcium-Binding Protein, a Cornified Cell Envelope Precursor, and an Intermediate Filament-Associated (Cross-Linking) Protein

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.

research Analysis of the Sheep Trichohyalin Gene: Potential Structural and Calcium-Binding Roles of Trichohyalin in the Hair Follicle

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.

research The Origin of Citrulline-Containing Proteins in the Hair Follicle and the Chemical Nature of Trichohyalin, an Intracellular Precursor

138 citations , November 1977 in “Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics”