Literature DB >> 410454

The origin of citrulline-containing proteins in the hair follicle and the chemical nature of trichohyalin, an intracellular precursor.

G E Rogers, H W Harding, I J Llewellyn-Smith.   

Abstract

The present studies have demonstrated that the medulla and inner root sheath cells develop within their cytoplasm a protein that is unique in composition and is present in the trichohyalin granules. The protein is rich in arginine residues, some of which undergo a side-chain conversion in situ into citrulline residues. An unusual Ca2+-dependent enzyme activity distinguishable from cross-linking transamidase has been detected in the hair follicle and will act in vitro on trichohyalin protein as the natural substrate. The conversion in vivo must occur during the time that the medullary and inner root sheath cells move up the follicle and their cytoplasm fills with cross-linked protein containing citrulline. The function of citrulline in these proteins is not understood but its formation is a major process during hair growth.

Entities:  

Mesh:

Substances:

Year:  1977        PMID: 410454     DOI: 10.1016/0005-2795(77)90250-1

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  26 in total

1.  Peptidylarginine deiminase in rat and mouse hemopoietic cells.

Authors:  S Nagata; T Senshu
Journal:  Experientia       Date:  1990-01-15

Review 2.  Protein Arginine Deiminases and Associated Citrullination: Physiological Functions and Diseases Associated with Dysregulation.

Authors:  Erin E Witalison; Paul R Thompson; Lorne J Hofseth
Journal:  Curr Drug Targets       Date:  2015       Impact factor: 3.465

Review 3.  Epidermal and hair follicle transglutaminases and crosslinking in skin.

Authors:  L L Peterson; K D Wuepper
Journal:  Mol Cell Biochem       Date:  1984       Impact factor: 3.396

4.  Transglutaminase-mediated cross-linking in mammalian epidermis.

Authors:  J A Rothnagel; G E Rogers
Journal:  Mol Cell Biochem       Date:  1984       Impact factor: 3.396

Review 5.  An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes.

Authors:  Mohammed Alghamdi; Khaled A Al Ghamdi; Rizwan H Khan; Vladimir N Uversky; Elrashdy M Redwan
Journal:  Cell Mol Life Sci       Date:  2019-07-24       Impact factor: 9.261

Review 6.  Rheumatoid arthritis and citrullination.

Authors:  Erika Darrah; Felipe Andrade
Journal:  Curr Opin Rheumatol       Date:  2018-01       Impact factor: 5.006

7.  Functional role of dimerization of human peptidylarginine deiminase 4 (PAD4).

Authors:  Yi-Liang Liu; Yu-Hsiu Chiang; Guang-Yaw Liu; Hui-Chih Hung
Journal:  PLoS One       Date:  2011-06-22       Impact factor: 3.240

Review 8.  Chemical biology of protein citrullination by the protein A arginine deiminases.

Authors:  Santanu Mondal; Paul R Thompson
Journal:  Curr Opin Chem Biol       Date:  2021-03-04       Impact factor: 8.972

Review 9.  Histone citrullination: a new target for tumors.

Authors:  Dongwei Zhu; Yue Zhang; Shengjun Wang
Journal:  Mol Cancer       Date:  2021-06-11       Impact factor: 27.401

Review 10.  Citrullination and PAD Enzyme Biology in Type 1 Diabetes - Regulators of Inflammation, Autoimmunity, and Pathology.

Authors:  Mei-Ling Yang; Fernanda M C Sodré; Mark J Mamula; Lut Overbergh
Journal:  Front Immunol       Date:  2021-06-01       Impact factor: 7.561

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.