ANXA6
- Known as:
- ANXA6
- Catalog number:
- 001696A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ANXA6
Related genes to: ANXA6
- Gene:
- ANXA6 NIH gene
- Name:
- annexin A6
- Previous symbol:
- ANX6
- Synonyms:
- -
- Chromosome:
- 5q33.1
- Locus Type:
- gene with protein product
- Date approved:
- 1990-02-01
- Date modifiied:
- 2014-11-19
Related products to: ANXA6
Related articles to: ANXA6
- Breast cancer is the most common cancer in women worldwide, and early detection remains a significant challenge. Recent studies have identified increased expression of Mammaglobin A (Q13296, Gene: ) mRNA in breast cancer, suggesting its potential as a disease marker, although its function is not fully understood. To elucidate Mammaglobin's role, this study sought to identify co-expressed miRNAs and analyze the biological pathways they regulate. - Source: PubMed
Publication date: 2026/09/01
Abella-Duque Juan FelipeLópez-Kleine LilianaParra-Medina RafaelRamírez-Clavijo SandraPayán-Gómez César - Plasma membrane repair is critical for tissue integrity, especially for elongated contractile muscle cells. Genetically mediated defects in plasma membrane resealing produce persistent leak, leading to a disordered extracellular matrix (ECM). Loss of the membrane repair protein dysferlin slows sarcolemmal resealing and promotes excess leak. Annexin A6 is also implicated in sarcolemmal repair, forming repair caps at the site of membrane disruption. On its own, deletion of the gene for annexin A6, Anxa6, had little effect on muscle health. In contrast, combined loss of dysferlin and annexin A6 (DysfA6) generated muscle fibers with profoundly defective membrane leak. Strikingly, Anxa6 deletion in the context of loss of dystrophin (mdxA6) did not exacerbate muscle defects. The persistent membrane leak in DysfA6 muscle resulted in marked macrophage infiltration with disordered macrophage polarization. Injured muscle fibers were targets of macrophage efferocytosis. Loss of Anxa6 was associated with increased expression of annexins A1 and A2, both of which were heavily deposited into the ECM. In vitro, macrophages exposed to annexins A1 and A2 increased Csf1 expression, consistent with a model where excess leak results in annexins A1 and A2 in the ECM, where this protein composition influences macrophage proliferation and efferocytosis. - Source: PubMed
Publication date: 2026/06/23
Lee GaHyunFitt Alexander JLong Ashlee MVaught Lauren ADeBiasse DorothyKeeble Alexander RKwon Jason MPage Patrick GtDaher Marie-ThereseHadhazy MicheleWillis Alexander BCeja Galindo DavidMcCabe MaxwellLantz ConnorHansen Kirk CCrosbie Rachelle HThorp Edward BDemonbreun Alexis RMcNally Elizabeth M - Annexins are a widely expressed family of multifunctional cytosolic proteins with diverse cellular roles. Recent advances have uncovered new avenues for the involvement of several annexins in membrane dynamics, suggesting a potential link to the coordination of membrane contact site (MCS) formation. Up to date, Annexin A1 (ANXA1), ANXA6 and ANXA11 have been defined as MCS-associated annexins. In a recent study, we demonstrated that ANXA6 critically influences the formation of multiple inter-organelle contact sites. Using electron microscopy, proximity-labelling and proteomic assays, ANXA6 deficiency was shown to substantially reduce the extent and number of MCS between several organelles in a number of cell lines. This correlated with ANXA6 interacting with various tethers and bona fide MCS proteins that can modulate multi-organelle contacts, indicating that the loss of ANXA6-related protein-protein interactions reduced the ability to develop contacts between organelles. Importantly, restoration of ANXA6 expression in ANXA6-deficient cells re-established MCS numbers, suggesting that transient changes in ANXA6 expression levels significantly impact on MCS dynamics. These findings identify ANXA6 as the first example of a cytosolic protein whose expression levels directly modulate the cellular organization of MCS. - Source: PubMed
Publication date: 2026/07/03
Enrich CarlosRentero CarlesGrewal Thomas - Mesenchymal progenitor cells (MPCs) play a significant role in articular cartilage homeostasis and regeneration. Yet, the functional dynamics and molecular characteristics of MPCs may differ significantly across various pathological conditions. Hence, this study comprehensively investigates the biological and molecular characteristics of MPCs isolated from articular cartilage of patients with osteoarthritis (OA) and rheumatoid arthritis (RA), aiming to uncover disease-specific differences that could offer insights into targeted regenerative therapies. Using flow cytometry, gene expression analysis, and in vitro differentiation assays, we assessed the phenotype, growth potential, senescence, cytogenetic instability, and chondrogenic potential to delineate molecular pathways uniquely active in each disease context. Phenotypically, both OA and RA-MPCs retained markers of mesenchymal stem cells (MSCs), but OA-derived MPCs exhibited higher fold expression of progenitor markers (, , , and ), suggesting a more activated state. Functionally, OA-MPCs demonstrated increased growth kinetics (higher proliferation rate and decreased population doubling time) with a significant shift towards adipogenic lineages (increased fold expression of , , and ). However, there were no differences in the osteogenic and chondrogenic potential. Gene expression analysis revealed upregulation of genes involved in extracellular matrix production and cartilage development (, , , , , , , , and ) in 3D cultures compared with 2D or monolayer cultures. Collectively, these findings demonstrate that, while multipotent MPCs are present in both OA and RA articular cartilage, they can exhibit fundamentally altered biological behaviors and molecular signatures reflective of the local disease microenvironment. Understanding these differences is critical for optimizing cell-based therapeutic strategies tailored to each condition and may facilitate the development of novel interventions targeting endogenous progenitor cells for cartilage repair. - Source: PubMed
Publication date: 2026/06/10
Manjappa Akshay BairapuraNitilapura NarendraShetty SiddharthRao ShamaBabu SanthoshShetty JayaprakashaShetty ReshmaBasavarajappa Mohana Kumar - Annexin A6 (ANXA6) regulates cholesterol transfer across membrane contact sites (MCSs) between late endosomes/lysosomes (LE/Lys) and the endoplasmic reticulum (ER) via the late endosomal StAR-related lipid transfer domain-3 (STARD3) transporter. Here, we describe a significant reduction of MCSs in ANXA6-depleted HeLa cells, which could be rescued by restoration of ANXA6 expression. Using AnxA6 as bait in BioID-based assays, we demonstrate that ANXA6 interacts with various tethers and bona fide MCS proteins that can modulate multi-organelle contacts. STARD3 interactors identified in BioID assays include the mitochondrial translocator protein (TSPO) and myosin heavy chain 9 (MYH9). Strikingly, reduced MCS formation in ANXA6-depleted cells was associated with changes in the STARD3 interactome that indicate altered MCS tethering functions of STARD3. Specifically, ANXA6 deficiency correlated with (1) altered positioning of STARD3-positive LE/Lys; (2) a new repertoire of cortical actin-binding proteins, including myosins interacting with STARD3; (3) and decreased microvillar structures and focal adhesions. - Source: PubMed
Publication date: 2026/06/15
Bernaus-Esqué MarcLiu YangjingPrats EvaEstanyol Josep MMartin GemmaCalvo MariaGigourtsi Panagiota AretiNguyen Mai Khanh LinhÁlvarez Alejandra RZanlungo SilvanaAgell NeusLu AlbertTebar FrancescEnrich CarlosGrewal ThomasRentero Carles