LTBP4 antibody
- Known as:
- LTBP4 (anti-)
- Catalog number:
- orb101833
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Biorbyt biorb
- Gene target:
- LTBP4 antibody
Related genes to: LTBP4 antibody
- Gene:
- LTBP4 NIH gene
- Name:
- latent transforming growth factor beta binding protein 4
- Previous symbol:
- -
- Synonyms:
- LTBP-4, LTBP-4L, FLJ46318, FLJ90018
- Chromosome:
- 19q13.1-q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-11-18
- Date modifiied:
- 2017-07-07
Related products to: LTBP4 antibody
Related articles to: LTBP4 antibody
- - Source: PubMed
Publication date: 2026/06/16
Zhang Y QSu Y JXue R YYang Y XLi L - [This corrects the article DOI: 10.1016/j.mbplus.2026.100194.]. - Source: PubMed
Publication date: 2026/05/17
Kemmochi ReikoMiyazaki HarukoTaga YukiTakahashi NaokiWatanabe TakafumiIkemura KentaroSasaki TakakoMizuno KazunoriHirohata SatoshiMatsumoto MitsuakiOohashi Toshitaka - Calcific aortic valve disease (CAVD) is characterized by progressive extracellular matrix (ECM) remodeling that promotes valve fibrosis and calcification. However, its molecular and structural basis remains unclear. In this study, we comprehensively analyzed ECM remodeling in human CAVD valves, focusing on collagen dynamics and key ECM-associated regulatory components. Histopathological analysis revealed fibrous layer thickening, collagen disorganization, and focal loss of the spongiosa in the CAVD group. Polarized picrosirius red staining demonstrated increased yellow-orange birefringence in the fibrotic and calcified regions, indicating altered collagen organization. Quantitative liquid chromatography-mass spectrometry analysis showed region-specific shifts toward an increased type III collagen proportion in fibrotic and calcific regions despite the reduced total collagen content in calcified areas. Collagen with improper triple-helical structure primarily accumulated around the calcified nodules, suggesting abnormal collagen turnover. Transmission electron microscopy revealed thinner and more heterogeneous collagen fibrils in lesioned regions than that in pre-lesional region. In normal valves, immunohistochemistry suggested that the hyaluronan-versican-fibrillin complex contributes to local regulation of Transforming growth factor-beta 1 (TGF-β1) activity via latent TGF-β binding proteins (LTBP); however, this regulatory structure was disrupted in CAVD. Notably, LTBP-4 showed strong, regionally restricted localization in the fibrotic and calcific regions and was positively correlated with collagen yellow-orange birefringence. Collectively, these findings indicate that CAVD is associated with a localized shift toward a structurally heterogeneous, type III collagen-enriched matrix, accompanied by collagen denaturation and abnormal accumulation of LTBP-4, highlighting ECM dysregulation as a key feature of disease progression. - Source: PubMed
Publication date: 2026/05/06
Kemmochi ReikoMiyazaki HarukoTaga YukiTakahashi NaokiWatanabe TakafumiIkemura KentaroSasaki TakakoMizuno KazunoriHirohata SatoshiMatsumoto MitsuakiOohashi Toshitaka - Latent transforming growth factor β-binding protein 4 (LTBP4) has been reported to be associated with heart failure (HF), but its role in HF remains unclear. We observe increased LTBP4 expression in plasma and cardiomyocytes of HF patients, and in a male mouse HF model induced by transverse aortic constriction (TAC). Cardiomyocyte-specific Ltbp4 deficiency attenuates NLRP3 inflammasome activation, cardiac dysfunction, and fibrosis post-TAC. Mechanistically, pressure overload upregulates LTBP4 partially via the transcription factor SP1. Angiotensin II promotes the recruitment of intracellular LTBP4 to the microtubule-organizing center (MTOC) via dynein. Subsequently, LTBP4 facilitates the dynein-mediated NLRP3 translocation to the MTOC and promotes NLRP3-NEK7 interaction, thereby driving NLRP3 inflammasome activation. Additionally, LTBP4 upregulates NLRP3 transcription and correlates positively with NLRP3 and interleukin-1β in HF patients. Here we show that LTBP4 is an important regulator of the NLRP3-NEK7 interaction and NLRP3 inflammasome activation in cardiomyocytes, highlighting its potential as a therapeutic target for HF. - Source: PubMed
Publication date: 2026/05/15
Ma SiyuJiang NanZuo ZhengLian ZhipengWu JianMa JinghuaWei XiangxiangHe YunquanPan QiLin JiayiLi YongboHou YannanZhi XiulingLi XiaoboOsto ElenaDai YuxiangLi JunGuo JieyuMeng Dan - There is a lack of approaches to detect and kill metastatic cells. As an agent for metastasis targeting, a cyclic peptide BLMP6 has been previously characterized. As a step toward translation, we designed AZDye555-labeled BLMP6 and demonstrated its homing to metastases of human MDA-MB-231 cells in mice. We show that Ga-radiolabeled BLMP6 can be used for the detection of MDA-MB-231 metastases. We designed a peptide-drug conjugate consisting of monomethyl auristatin E (MMAE) and BLMP6. We show that MMAE-BLMP6 kills MDA-MB-231 cells in cell culture and . In mouse models of lung metastases, treatment with MMAE-BLMP6 suppressed metastasis growth and improved survival. Based on BLMP6 similarity to latent transforming growth factor β binding protein 4 (LTBP4), we identified fibulin-4 as a BLMP6 target. We show that BLMP6 mimics the LTBP4 domain binding to fibulin-4 and selectively binds to fibulin-4 . Fibulin-4 knockout in cancer cells abrogated BLMP6 homing to lung metastases in mice. Fibulin-4 expression was found to be increased in invasive and metastatic human breast cancer and correlated with the binding of AZDye555-BLMP6 in human tissue sections. Our results suggest that fibulin-4 and BLMP6 may be further developed for the detection and targeting of metastatic human cancers. - Source: PubMed
Publication date: 2026/04/18
Daquinag Alexes CGhosh Sukhen CAghaAmiri SolmazFarmer Stephen MZhang ShengVargas Servando HernandezRamesh Ashwin KAn ZhiqiangAzhdarinia AliKolonin Mikhail G