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Last update 08 May 2025

TAFA1

Last update 08 May 2025

Basic Info

Synonyms

Chemokine-like protein TAFA-1, FAM19A1, TAFA chemokine like family member 1

+ [2]

Introduction

Regulatory factor which is ligand for CMKLR2 and is involved in the modulation of neural stem-cell proliferation and differentiation.

Drugs associated with TAFA1

JP2024016199

Patent Mining

Target

TAFA1

Mechanism-

Active Org.

Neuracle Science Co., Ltd.

Originator Org.

Neuracle Science Co., Ltd.

Active Indication

Nervous System Diseases

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with TAFA1

100 Translational Medicine associated with TAFA1

0 Patents (Medical) associated with TAFA1

Literatures (Medical) associated with TAFA1

01 Dec 2020·Journal of Pediatric Genetics

Peruvian Newborn Male with 3p13 Deletion Syndrome Encompassing the FOXP1 Gene: Review of the Literature

Author: Trubnykova, Milana ; Chavesta-Velásquez, Félix ; Barletta-Carrillo, Claudia ; Rondón-Abuhadba, Andrea ; Abarca-Barriga, Hugo H. ; Ordoñez-Linares, Marco

AbstractCopy number variation in loss of 3p13 is an infrequently reported entity characterized by hypertelorism, aniridia, microphthalmia, high palate, neurosensorial deafness, camptodactyly, heart malformation, development delay, autism spectrum disorder, seizures, and choanal atresia. The entity is caused probably by haploinsufficiency for FOXP1, UBA3, FAM19A1, and MITF. We report a newborn male with hypotonia, facial dysmorphism, heart malformation, and without clinical diagnosis; nevertheless, the use of appropriate genetic test, such us the chromosomal microarray analysis allowed identification of a copy number variant in loss of 5.5 Mb at chromosome 3 (p13-p14.1), that included 54 genes, encompassing FOXP1 gene. We compare the findings in our Peruvian patient to those of earlier reported patients; furthermore, add new signs for this entity.

01 Oct 2020·International Forum of Allergy & RhinologyQ1 · MEDICINE

Chronic rhinosinusitis: assessment of changes in nociceptive neurons

Q1 · MEDICINE

Article

Author: Van Crombruggen, Koen ; De Ruyck, Natalie ; Bogaert, Stijn ; Holtappels, Gabriele ; Bachert, Claus ; Park, Jonas Jae‐Hyun ; Suchonos, Nicole

BackgroundPain is a major symptom of chronic rhinosinusitis (CRS). It is mainly associated with CRS without nasal polyps (CRSsNP) and has a major impact in the decision to move on to surgery. Patients with CRS with nasal polyps (CRSwNP) are characterized by trigeminal hypoesthesia and suffer from less pain. The aim of this study was to investigate whether CRS induces alterations in the peripheral nociceptive neurons, mainly focusing on quantitative changes.MethodsSinus mucosa and inferior turbinate (IT) samples were obtained from patients with CRS, and IT tissue of healthy patients served as controls. Reverse transcription quantitative polymerase chain reaction (RT‐qPCR) was performed for neuronal markers including CNTNAP2, FAM19A1, GFRA2, NEFH, NTRK1, PLXNC1, RET, SCN10A, SCN11A, TRPV1, and PGP 9.5; enzyme‐linked immunosorbent assay (ELISA) was performed for KCNK18, SCN10A, MRGPRD, and MAP2. For PGP 9.5, immunohistochemistry was additionally used to analyze tissue slides.ResultsWe included 35 patients with CRSsNP, 47 patients with CRSwNP, and 18 control patients. No differences in expression of the neuronal markers were observed between CRSsNP, CRSwNP, and controls. SCN10A was the only marker exclusively expressed on nociceptive neurons in sinus tissue. No histological difference in nerve fibers was observed between sinus mucosa of both phenotypes.ConclusionOur results indicate that the nociceptive nerve density in CRSwNP is not lower than in CRSsNP, as was assumed previously. The nociceptive neurons in sinonasal mucosa cannot be classified into subtypes due to the lack of specificity of the respective marker genes. Our findings question the generally accepted claim that nasal polyp tissue does not contain any nerves.

07 Sep 2020·Journal of Cell BiologyQ1 · BIOLOGY

Deorphanizing FAM19A proteins as pan-neurexin ligands with an unusual biosynthetic binding mechanism

Q1 · BIOLOGY

Article

Author: Südhof, Thomas C. ; Sterky, Fredrik H. ; Sclip, Alessandra ; Fakler, Bernd ; Khalaj, Anna J. ; Schwenk, Jochen ; Brunger, Axel T.

Neurexins are presynaptic adhesion molecules that organize synapses by binding to diverse trans-synaptic ligands, but how neurexins are regulated is incompletely understood. Here we identify FAM19A/TAFA proteins, “orphan" cytokines, as neurexin regulators that interact with all neurexins, except for neurexin-1γ, via an unusual mechanism. Specifically, we show that FAM19A1-A4 bind to the cysteine-loop domain of neurexins by forming intermolecular disulfide bonds during transport through the secretory pathway. FAM19A-binding required both the cysteines of the cysteine-loop domain and an adjacent sequence of neurexins. Genetic deletion of neurexins suppressed FAM19A1 expression, demonstrating that FAM19As physiologically interact with neurexins. In hippocampal cultures, expression of exogenous FAM19A1 decreased neurexin O-glycosylation and suppressed its heparan sulfate modification, suggesting that FAM19As regulate the post-translational modification of neurexins. Given the selective expression of FAM19As in specific subtypes of neurons and their activity-dependent regulation, these results suggest that FAM19As serve as cell type–specific regulators of neurexin modifications.

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TAFA1

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