Last update 01 Nov 2024

COL17A1

Last update 01 Nov 2024

Basic Info

Synonyms

120 kDa linear IgA dermatosis antigen, 120 kDa linear IgA disease antigen, 180 kDa bullous pemphigoid antigen 2

+ [14]

Introduction

May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane. The 120 kDa linear IgA disease antigen is an anchoring filament component involved in dermal-epidermal cohesion. Is the target of linear IgA bullous dermatosis autoantibodies.

Drugs associated with COL17A1

WO2023092314

Patent Mining

Target

COL17A1

Mechanism-

Active Org.

Skin Diseases Hospital, China Academy of Medical Science [+1]

Originator Org.

Suzhou Institute of Systems Medicine [+2]

Active Indication

Immune System Diseases

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with COL17A1

100 Translational Medicine associated with COL17A1

0 Patents (Medical) associated with COL17A1

1,244

Literatures (Medical) associated with COL17A1

01 Oct 2024·Journal of Investigative Dermatology

Strategy for the Optimization of Read-Through Therapy for Junctional Epidermolysis Bullosa with COL17A1 Nonsense Mutation

Article

Author: Has, Cristina ; Sayar, Saliha Beyza

Read-through therapy suppresses premature termination codons and induces read-through activity, consequently restoring missing proteins. Aminoglycosides are widely studied as read-through drugs in different human genetic disorders, including hereditary skin diseases. Our previous work revealed that aminoglycosides affect COL17A1 nonsense mutations and represent a therapeutic option to alleviate disease severity. However, the amount of restored type XVII collagen (C17) in C17-deficient junctional epidermolysis bullosa keratinocytes was <1% relative to that in normal keratinocytes and was achieved only after high-dose gentamicin treatment, which induced deep transcriptional changes. Therefore, in this study, we designed a strategy combining aminoglycosides with compounds known to reduce their side effects. We developed translational read-through-inducing drug cocktail, version 5 containing low dosage of aminoglycosides, CC-90009, NMDI-14, melatonin, and apocynin that was able to induce about 20% of missing C17 without cell toxicity or an effect on in vitro wound closure. Translational read-through-inducing drugs cocktail, version 5 significantly induced COL17A1 expression and reverted the proinflammatory phenotype of C17-deficient junctional epidermolysis bullosa keratinocytes. Evaluation of this drug cocktail regarding its stability, penetration, and efficacy as a topical treatment remains to be determined. Translational read-through-inducing drug cocktail, version 5 might represent an improved therapeutic strategy for junctional epidermolysis bullosa and for other genetic skin disorders.

01 Oct 2024·Laboratory Investigation

Junctional Epidermolysis Bullosa in Sprague Dawley Rats Caused by a Frameshift Mutation of Col17a1 Gene

Article

Author: Nishioka, Yasushi ; Ohnuma-Koyama, Aya ; Shimizu-Endo, Naoko ; Katoh, Yoshitaka ; Shiga, Atsushi ; Ito, Tsuyoshi ; Yoshida, Toshinori ; Aoyama, Hiroaki ; Takahashi, Naofumi ; Sato, Akira

Junctional epidermolysis bullosa is an intractable cutaneous disorder in humans causing skin fragility and blistering due to mutations in genes encoding essential molecules adhering epidermis and dermis including collagen XVII. However, the pathogenesis still remains to be not fully understood perhaps because of a lack of appropriate animal models. In this study, we report novel mutant rats experiencing junctional epidermolysis bullosa, which was confirmed to be caused by a frameshift mutation of Col17a1 gene, as a rat model for investigating the underlying mechanism of pathogenesis. The mutant rats completely lacked the expression of collagen XVII and had blisters leading to infantile deaths as a homozygous condition, although their skin was apparently normal at birth by light microscopic evaluation except that immunohistochemical examination could not detect collagen XVII in any organs. These observations suggest that collagen XVII is not essential for the development of skin during the prenatal period but is indispensable for keeping epidermal-dermal connections stable after birth. Subsequent electron microscopic examinations further revealed an absence of hemidesmosomal inner plaques being composed of BP230, a binding partner of collagen XVII, and plectin in Col17a1-null newborns, albeit mRNA expressions of these molecules seemed to be unaffected at least during the fetal period. These results suggest that the lack of collagen XVII induces attenuation of hemidesmosomal inner plaques, which in turn destabilizes the epidermis-dermis connection and results in deterioration of epidermal physiology with formation of blisters after birth.

01 Oct 2024·Journal of Medical Genetics

Heterozygous COL17A1 variants are a frequent cause of amelogenesis imperfecta

Article

Author: Weiss, Jayne E ; Kivelä, Tero T ; Lisch, Walter

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COL17A1

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