Inhibitors of epidermal growth factor receptor (EGFR), including tyrosine kinase inhibitors (TKIs), present significant clinical benefits in the treatment of non-small cell lung cancer (NSCLC), particularly in patients with an EGFR mutation. However, TKI treatment also results in unwanted cutaneous toxic side effects, such as a skin rash. Eyelash trichomegaly is rarely reported as a side effect; however, it causes cosmetic issues or eyeball irritation in patients, which may result in the early termination of TKI treatment. Therefore, although TKI-induced eyelash trichomegaly is rare, it should be considered carefully by lung cancer physicians. The present study reported a case of erlotinib-induced eyelash trichomegaly in a 65-year-old Chinese female patient suffering from NSCLC with an EGFR mutation. To the best of our knowledge, this is the first reported case of erlotinib-induced trichomegaly in a Chinese patient.
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http://dx.doi.org/10.3892/ol.2015.3265 | DOI Listing |
Dermatol Ther (Heidelb)
October 2024
Dermatology Unit, IRCCS Azienda Ospedaliero-Universitaria di Bologna, Via Massarenti 5, 40138, Bologna, BO, Italy.
Differentiation
September 2024
Department of Genetics, University of Texas MD Anderson Cancer Center, Houston, TX, 77030, United States. Electronic address:
FGF5 functions as a negative regulator of the hair cycle in mammals. It is expressed in the outer root sheath of hair follicles during the late anagen phase of the hair cycle. It functions as a signaling molecule, mediating the transition of the anagen growth phase to catagen regression phase of the hair cycle.
View Article and Find Full Text PDFInt J Ophthalmol
March 2023
Department of Ophthalmic Center, Kiang Wu Hospital, Macao 999078, China.
J Biomol Struct Dyn
December 2023
Department of Cell Biology and Neuroscience, Rutgers University, Piscataway, New Jersey, USA.
The missense mutation Y174H of FGF5 (FGF5-H174) had been associated with trichomegaly, characterized by abnormally long and pigmented eyelashes. The amino acid tyrosine (Tyr/Y) at position 174 is conserved across many species, proposedly holding important characteristics for the functions of FGF5. Microsecond molecular dynamics simulations along with protein-protein docking and residue interacting network analysis were employed to investigate the structural dynamics and binding mode of both wild-type (FGF5-WT) and its mutated counterpart (FGF5-H174).
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