CD107a
- Known as:
- CD107a
- Catalog number:
- 10-521-C100
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Exbio
- Gene target:
- CD107a
Related genes to: CD107a
- Gene:
- LAMP1 NIH gene
- Name:
- lysosomal associated membrane protein 1
- Previous symbol:
- -
- Synonyms:
- CD107a
- Chromosome:
- 13q34
- Locus Type:
- gene with protein product
- Date approved:
- 1990-07-15
- Date modifiied:
- 2016-01-14
Related products to: CD107a
Related articles to: CD107a
- Ivermectin suppresses tumor growth in various cancers. However, the mechanism of action in cancer remains unclear. This study aimed to investigate the anticancer activity of ivermectin against gastric cancer cell lines and patient-derived organoids. - Source: PubMed
Publication date: 2026/04/26
Lee SunwoongJung Deuk KjuKim DohyangLim Hee JeongNam Su Youn - The emergence of Decapod iridescent virus 1 (DIV1) has seriously threatened Macrobrachium rosenbergii aquaculture in recent years. While the viral envelope protein 168 L has been identified, its host receptors remain incompletely characterized. Lysosome-associated membrane protein 1 (LAMP1) is frequently exploited by various pathogens for cellular entry and immune evasion. To explore the function of MrLAMP1 in virus infection of M. rosenbergii, we cloned a LAMP1 gene from M. rosenbergii featuring a 978-bp ORF encoding a 325-aa protein. Tissue distribution analysis revealed widespread expression of MrLAMP1, with the highest transcript levels detected in the eyestalk. Following DIV1 challenge, MrLAMP1 expression in different tissues increased significantly from 0 to 72 h post-infection (hpi), followed by a decline at 96 hpi. Functional studies using RNAi-mediated knockdown and in vitro mRNA overexpression demonstrated that DIV1 replication was significantly suppressed in the knockdown group, accompanied by markedly improved survival of infected prawns. In contrast, overexpression of MrLAMP1 led to the opposite outcome. Furthermore, co-immunoprecipitation assays confirmed the interaction between MrLAMP1 and 168 L in HEK293T cells. Cellular localization assays showed that 168 L co-localized with MrLAMP1 on the plasma membrane of transfected cells. These results demonstrate that MrLAMP1 promotes virus replication, suggesting that targeting LAMP1 may represent a potential antiviral strategy. - Source: PubMed
Publication date: 2026/07/10
Qian QieqiXie YumengXu YuxuanZhou LiyingZhu XinhaiGao XiaojianZhang Xiaojun - Post-ovulatory ageing (POA) severely compromises oocyte quality. However, the upstream events linking POA to mitochondrial, endoplasmic reticulum (ER) and autophagic defects remain unclear. Here, we tested whether stabilising the plasma membrane potential can protect porcine metaphase II (MII) oocytes from POA-induced damage. NS309, a pharmacological activator of small-and intermediate-conductance Ca activated K (KCa2/KCa3.1) channels, reduced abnormal morphology, reactive oxygen species (ROS) accumulation and partially restored mitochondrial membrane potential, mtDNA copy number and mitochondrial Ca in POA oocytes, indicating improved mitochondrial fitness. NS309 also preserved ER structure, normalised ER and cytosolic Ca levels, re-balanced unfolded protein response (UPR) markers and remodeled enlarged, clustered lysosomal associated membrane protein 1 (LAMP1)-positive structures into a more homogeneous pattern without markedly increasing total LAMP1 or microtubule-associated protein 1 light chain 3 beta (LC3B), consistent with enhanced ER Ca control and lysosomal/autophagic organisation. These data support a model in which NS309 protects POA oocytes primarily by stabilising the plasma membrane potential, which is upstream of Ca entry, thereby secondarily improving mitochondrial, ER and autophagic homeostasis. Pharmacological manipulation of calcium-activated potassium currents may thus offer a tractable strategy to modulate ion-channel-controlled ageing pathways in mammalian oocytes. - Source: PubMed
Publication date: 2026/07/08
Jin Ying-YanZhan Cheng-LinLee Song-HeeLee Ji-YeonCui Xiang-Shun - Brucella spp. are Gram-negative facultative intracellular pathogens responsible for brucellosis, a widespread zoonosis. Among them, B. melitensis and B. abortus are the most epidemiologically relevant species, primarily infecting sheep and goats, and cattle, respectively. Upon infection, brucellae multiply within phagocytes and develop placental tropism, particularly targeting trophoblasts. Most studies of Brucella pathogenesis and vaccine development have relied on murine or human-derived epithelial and macrophagic cell lines, which may not fully reproduce the natural ruminant host. Here, we investigated whether the intracellular behaviour described for Brucella in non-natural-host models also occurs in ruminant trophoblasts (AH-1 and F3 cells) and macrophages (BoMac cells). Using confocal immunofluorescence microscopy and bacteriological assays, we observed similar infection rates for B. abortus and B. melitensis. By 24 hours post-infection (hpi), both species had transitioned to LAMP1-negative Brucella-containing vacuoles, with active replication occurring within calnexin-positive compartments. These results confirm that the Brucella intracellular trafficking previously described in non-natural-host models is conserved in these ruminant cells. Additionally, we characterised for the first time the intracellular behaviour of the Rev1 vaccine strain. Although its initial rate of infection was comparable to B. melitensis 16M, Rev1 exhibited a delay in LAMP1-exclusion from the Brucella-containing vacuole, with most bacteria remaining in LAMP1-positive compartments at 24 hpi, and showed delayed initiation of replication. These findings, together with slower in vitro growth, suggest that the Rev1 attenuation results from both delayed intracellular trafficking and impaired intracellular fitness. Our results advance the understanding of Brucella pathogenesis in natural-host and shed light on Rev1 attenuation, offering key insights to enhance current brucellosis vaccines. - Source: PubMed
Publication date: 2026/07/07
Elizalde-Bielsa AitorLoperena-Barber MaitePfarrer ChristianeSalcedo Suzana PZúñiga-Ripa AmaiaConde-Álvarez Raquel - Retinal degenerative diseases are a leading cause of irreversible blindness. Their pathogenesis is intricately linked to oxidative stress-induced dysfunction of retinal pigment epithelial (RPE) cells and subsequent retinal degeneration. Macroautophagy/autophagy, a critical cellular degradation pathway, plays a vital role in maintaining RPE homeostasis, yet its dysregulation in retinal degenerative diseases remains poorly understood. In this study, we observed that sodium iodate (NaIO), an oxidative stress inducer, triggered lysosomal dysfunction via lysosomal membrane permeabilization (LMP), thereby impairing autophagic flux in RPE cells and exacerbating retinal degeneration. RNA sequencing identified (lysosomal-associated membrane protein 3) as a downregulated gene following NaIO treatment. Functionally, LAMP3 overexpression alleviated NaIO-induced LMP, improved lysosomal function, and alleviated autophagic impairment. Furthermore, upregulation of LAMP3 reduced oxidative stress and apoptosis in RPE cells, while alleviating retinal degeneration in a NaIO-induced mouse model. Mechanistically, our data suggested that NaIO upregulated the transcription factor SNAI1, which acts as a transcriptional repressor of . SNAI1 knockdown increased LAMP3 expression, thereby facilitating the recovery of lysosomal function and the alleviation of autophagic impairment. Collectively, our findings indicate that the SNAI1-LAMP3 axis contributes to the regulation of the autophagy-lysosomal pathway in retinal degeneration, highlighting a potential therapeutic target for delaying disease progression. AMD: age-related macular degeneration; AO: acridine orange; Baf A1: bafilomycin A; BAX: BCL2-associated X protein; BCL2: B cell leukemia/lymphoma 2; BSA: bovine serum albumin; CCK-8: cell counting kit-8; ChIP: chromatin immunoprecipitation; CM-HDCFDA: chloromethyl-2',7'-dichlorodihydrofluorescein diacetate; CTSD: cathepsin D; DAPI: 4',6-diamidino-2-phenylindole; DEGs: differentially expressed genes; DHE: dihydroethidium; EdU: 5-ethynyl-2'-deoxyuridine; ERG: electroretinography; GSEA: gene set enrichment analysis; H&E: hematoxylin and eosin; HsRPE: human primary retinal pigment epithelial; JC-1: 5,5',6,6'-tetrachloro-1,1',3,3'-tetraethylbenzimidazolylcarbocyanine iodide; LAMP1: lysosomal-associated membrane protein 1; LAMP2: lysosomal-associated membrane protein 2; LAMP3: lysosomal-associated membrane protein 3; LGALS3: lectin, galactose binding, soluble 3; LLOMe: leu-leu methyl ester; LMP: lysosomal membrane permeabilization; MAP1LC3B/LC3B: microtubule-associated protein 1 light chain 3 beta; MMP: mitochondrial membrane potential; NAC: N-acetyl-L-cysteine; NaIO: sodium iodte; NC: negative control; OCT: optical coherence tomography; PCA: principal component analysis; PI: propidium iodide; qRT-PCR: quantitative real-time polymerase chain reaction; Rapa: rapamycin; ROS: reactive oxygen species; RP: retinitis pigmentosa; RPE: retinal pigment epithelium; RPE65: retinal pigment epithelium 65; siRNA: small interfering RNA; SNAI1: snail family zinc finger 1; SQSTM1/p62: sequestosome 1; TJP1/ZO-1: tight junction protein 1; ZNF135: zinc finger protein 135. - Source: PubMed
Publication date: 2026/07/10
Ji YukeSun YananHuang XiaoshengLiang JiaFang DongYang WeihuaFeng LujiaZhang Shaochong