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Last update 23 Jan 2025

harmonin

Last update 23 Jan 2025

Basic Info

Synonyms

AIE-75, AIE75, Antigen NY-CO-38/NY-CO-37

+ [13]

Introduction

Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and maintenance of cochlear hair cell bundles (By similarity). As part of the intermicrovillar adhesion complex/IMAC plays a role in brush border differentiation, controlling microvilli organization and length. Probably plays a central regulatory role in the assembly of the complex, recruiting CDHR2, CDHR5 and MYO7B to the microvilli tips (PubMed:24725409, PubMed:26812018).

Drugs associated with harmonin

ASO-29

Target

harmonin

Mechanism

harmonin modulators

Active Org.-

Originator Org.

Louisiana State University

Active Indication-

Inactive Indication

Usher Syndromes

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with harmonin

100 Translational Medicine associated with harmonin

0 Patents (Medical) associated with harmonin

210

Literatures (Medical) associated with harmonin

01 Dec 2024·Laryngoscope Investigative Otolaryngology

Efficiency of gene therapy for sensorineural hearing loss in mouse model: A meta‐analysis

Review

Author: Yilmaz, Nevra Keskin ; Ozen, Dogukan ; Schuster, Artur Koerig ; Ocak, Emre ; da Costa Monsanto, Rafael ; Shimura, Tomotaka ; Cureoglu, Sebahattin

AbstractObjectivesSensorineural hearing loss (SNHL) is a disorder characterized by the loss or impairment of cochlear hair cells or the auditory nerve. In recent years, gene therapy has emerged as a promising approach for SNHL treatment. The objective of this study is to evaluate the impact of gene therapy on the restoration or improvement of auditory function in mouse model with loss or impairment of hearing.MethodsStudies with clear experimental designs, and auditory brainstem response (ABR) analysis as relevant outcome measures were included by searching PubMed, Scopus, and Web of Science databases. The PRISMA guideline was used for abstracting data and assessing data quality and validity. A quantitative synthesis was performed using a random effects model to examine the effect of gene therapy on auditory function in SNHL.ResultsNine articles including 71 studies meeting the inclusion criteria were identified. These studies explored therapies targeting the TMC1, VGLUT3, USH1C, CLRN1, WHRN, and PJVK genes, with genetic material ranging from 1.8 × 1011 and 1.4 × 1014 gc/mL being delivered to the inner ear through round window membrane, cochleostomy, or posterior semicircular canal injection methods. The hearing test results showed a significant mean difference of 26.91 dB (95% CI: 22.01–31.85) in favor of the experimental group.ConclusionsAlthough promising results have been obtained regarding the potential success of gene therapy in SNHL, further investigation is needed to explore the long‐term effects of gene therapy, treatment response rates, and the relationships between different genetic mutation types.

01 Oct 2024·Journal of Histochemistry & Cytochemistry

Intestinal Tuft Cells Are Enriched With Protocadherins

Article

Author: Dooley, Sarah A. ; Edens, Rachel ; Nicholson, Maribeth R. ; Stubler, Rachel ; Engevik, Amy C.

Intestinal tuft cells are rare cells that regulate diverse functions. They harbor chemosensory receptors and signal to the mucosal immune system in response to external stimuli, though their full function and structure remain unclear. Named for their apical “tuft” of long actin-rich microvilli, tuft cells facilitate chemoreception and other physiological responses. In enterocytes, microvilli are stabilized by intermicrovillar adhesion complexes (IMACs) composed of several proteins, including cadherin-related family member-2 (CDHR2) and cadherin-related family member-5 (CDHR5), Myosin 7b, and Usher syndrome type 1 C (USH1C). We hypothesized that IMACs would be enriched in tuft cells to regulate microvillar organization. Immunostaining of murine intestinal tissue revealed that CDHR2 and CDHR5 colocalize with the tuft cell markers, DCLK1, phospho-EGFR, advillin, and cytokeratin 18. CDHR2 was dispersed throughout murine tuft cells, while CDHR5 was concentrated on the apical surface. USH1C and Myosin 7b were present in tuft cells, but at lower levels. Human single-cell RNA sequencing revealed robust CDHR2 and CDHR5 expression in tuft cells in the small intestine and colon. Immunostaining of human intestinal tissue confirmed CDHR2 and CDHR5 localization to the apical surface of tuft cells. Our findings demonstrate that protocadherins are key components of murine and human intestinal tuft cells.

01 Sep 2024·Protein Science

Structural and biochemical characterization of the C‐terminal region of the human RTEL1 helicase

Article

Author: Cortone, Giuseppe ; González‐Magaña, Amaia ; Blanco, Francisco J. ; Hegde, Raghurama ; Chaves‐Arquero, Belén ; Kanade, Manil ; Napolitano, Luisa M. R. ; Graewert, Melissa A. ; Longo, Antonio ; Onesti, Silvia

AbstractRTEL1 is an essential DNA helicase which plays an important role in various aspects of genome stability, from telomere metabolism to DNA replication, repair and recombination. RTEL1 has been implicated in a number of genetic diseases and cancer development, including glioma, breast, lung and gastrointestinal tumors. RTEL1 is a FeS helicase but, in addition to the helicase core, it comprises a long C‐terminal region which includes a number of folded domains connected by intrinsically disordered loops and mediates RTEL1 interaction with factors involved in pivotal cellular pathways. However, information on the architecture and the function of this region is still limited. We expressed and purified a variety of fragments encompassing the folded domains and the unstructured regions. We determined the crystal structure of the second repeat, confirming that it has a fold similar to the harmonin homology domains. SAXS data provide low‐resolution information on all the fragments and suggest that the presence of the RING domain affects the overall architecture of the C‐terminal region, making the structure significantly more compact. NMR data provide experimental information on the interaction between PCNA and the RTEL1 C‐terminal region, revealing a putative low‐affinity additional site of interaction. A biochemical analysis shows that the C‐terminal region, in addition to a preference for telomeric RNA and DNA G‐quadruplexes, has a high affinity for R‐loops and D‐loops, consistent with the role played by the RTEL1 helicase in homologous recombination, telomere maintenance and preventing replication‐transcription conflicts. We further dissected the contribution of each domain in binding different substrates.

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