Through integrated multi-omics analysis and multi-dimensional experimental validation, this study systematically resolved the core mechanisms by which UPP1 mediates the formation of an immunosuppressive microenvironment and drives tumor progression in LUAD, providing novel theoretical basis for LUAD prognosis assessment and personalized immunotherapy.
Pericytes are key components of the blood-brain barrier (BBB), closely interacting with endothelial cells (ECs) via signaling pathways like PDGF-β. Major pericyte markers include PDGFR-β, α-smooth muscle actin, desmin, CD146, CD13, CD31, and NG2. These markers regulate pericyte-EC communication, cytoskeleton function, and inflammatory responses in the central nervous system.
Platelet-derived growth factor (PDGF) forms dimers that bind PDGF receptors, activating downstream signaling molecules such as PI3K, SHP-2, Akt, and Erk1/2. These pathways regulate cell growth, migration, and differentiation. PDGF signaling is frequently dysregulated in solid tumors, supporting tumor cell proliferation, stromal interaction, and angiogenesis. Targeting PDGF signaling represents a potential therapeutic strategy for cancer.
Parthanatos is a regulated cell death triggered by poly(ADP-ribose) (PAR) accumulation, driven by overactivated PARP-1. Excessive PAR binds AIF, which complexes with MIF, translocates to the nucleus, and cleaves DNA, causing cell death. It is closely linked to neurodegenerative diseases like Alzheimer’s and Parkinson’s.
This text introduces common immunohistochemical markers for pancreatic cells and tumors. Insulin/C‑peptide, glucagon, and NKX6.1 serve as key markers for pancreatic β and α cells, respectively. Pan‑keratin and CD200 help differentiate pancreatic adenocarcinomas and neuroendocrine tumors. Relevant antibodies and their applications are also listed.
The 90 kDa ribosomal S6 kinases (RSK1–4) are a widely expressed family of serine/threonine kinases, featuring two distinct functional kinase domains and a C-terminal docking site for extracellular signal-regulated kinases (ERKs). Key phosphorylation sites, including Ser380, Thr359, Ser363, and Thr573, are critical for RSK activation. RSK1–3 are activated by coordinated phosphorylation mediated by mitogen-activated protein kinases (MAPKs), autophosphorylation, and phosphoinositide-3-OH kinase (PI3K) in response to growth factors, polypeptide hormones, and neurotransmitters. This paper also lists relevant antibodies for RSK detection and provides related research references.
p70 S6 kinase is a mitogen‑activated Ser/Thr protein kinase essential for cell growth and G1 cell cycle progression. It phosphorylates the S6 protein of the 40S ribosomal subunit at key residues (Ser235, Ser236, Ser240, Ser244) and regulates translation of 5′ oligopyrimidine tract mRNAs. In vivo, it phosphorylates eIF4B at the rapamycin‑sensitive Ser422 site; the Ser422Ala mutant of eIF4B exhibits reduced activity in in vitro translation assays. Additionally, phosphorylation of eEF2K by p70 S6 kinase and p90RSK inactivates eEF2K, promoting eEF2 dephosphorylation and facilitating protein translation. This paper summarizes specific antibodies targeting key proteins in this pathway, providing experimental tools for related molecular mechanism studies.
As the most pivotal stromal cells in the tumor microenvironment (TME), cancer-associated fibroblasts (CAFs), also known as activated fibroblasts, engage in multiple critical processes of tumor progression through extensive interactions with tumor cells, immune cells and other stromal cells, including extracellular matrix (ECM) remodeling, the establishment of an immunosuppressive microenvironment, and the regulation of tumor invasion and metastasis. 要不要我把这句英文再**精简一版**，保持学术正式、更适合论文摘要/引言？
The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination .
