| Topic | Mechanism/claim | Key quantitative/statistical detail | System/disease context | Source (year; DOI/URL) |
|---|---|---|---|---|
| Identity, structure, receptors | THBS1/TSP1 is a secreted extracellular matricellular glycoprotein of the Group A thrombospondins that forms a trimer; key regions include N-terminal domain, procollagen-like region, type I/TSR repeats, EGF-like/type II domains, type III repeats, and a C-terminal domain with a CD47-binding site. TSRs bind latent TGF-β and CD36; N-terminus and EGF-like domains engage integrins. | Quantitative performance data not reported in the excerpt; structural summary is qualitative. | Core functional annotation / extracellular matrix signaling | Pan et al., 2024, Front Cardiovasc Med, doi:10.3389/fcvm.2024.1337586, https://doi.org/10.3389/fcvm.2024.1337586 (pqac-00000001, pqac-00000006, pqac-00000013) |
| CD47–NO/cGMP axis, hemostasis, stress response | THBS1 engages CD47 to inhibit nitric oxide/cGMP signaling, reducing vasodilation and supporting platelet activation/thrombus formation; CD36 also contributes to thrombus formation on collagen. Authors interpret THBS1 as important for surviving environmental stress, especially cardiovascular and immune challenges. | No explicit effect size given in the evidence snippet; mechanism emphasized as central to stress physiology. | Vascular homeostasis, ischemic stress, hemostasis | Kaur & Roberts, 2023, J Cell Commun Signal, doi:10.1007/s12079-023-00722-5, https://doi.org/10.1007/s12079-023-00722-5 (pqac-00000002, pqac-00000003, pqac-00000014, pqac-00000021) |
| Latent TGF-β activation / fibrosis signaling | THBS1 is a major activator of latent TGF-β in vivo; this links THBS1 to downstream Smad2/3 signaling, fibroblast activation, ECM remodeling, and fibrosis. | No single pooled statistic reported in the review excerpts. | Fibrosis, cardiovascular remodeling, immune regulation | Pan et al., 2024, Front Cardiovasc Med, doi:10.3389/fcvm.2024.1337586, https://doi.org/10.3389/fcvm.2024.1337586; Kaur & Roberts, 2023, doi:10.1007/s12079-023-00722-5, https://doi.org/10.1007/s12079-023-00722-5 (pqac-00000005, pqac-00000014) |
| Epithelial wound repair pathway | Exogenous THBS1 enhances intestinal epithelial migration in a CD47- and TGF-β1-dependent manner; the study assayed SMAD2/3 and RhoA/Rac1 signaling, supporting a mechanism involving focal adhesion and cytoskeletal remodeling during restitution. | Quantitative effect sizes were not included in the gathered snippets, but epithelial-specific loss of THBS1 impaired wound healing in vivo. | Intestinal mucosal wound repair | Wilson et al., 2024, JCI Insight, doi:10.1172/jci.insight.180608, https://doi.org/10.1172/jci.insight.180608 (pqac-00000015, pqac-00000020) |
| TGFβ receptor/integrin migratory complex | In prostate cancer cells, THBS1 is a major TGFβ-induced secreted ECM protein that interacts with ITGAV and TGFβ receptor I (TβRI); THBS1/ITGAV/TβRI colocalize at the leading edge and support migration, invasion, and metastasis. | No numerical hazard ratio or AUROC reported in the gathered snippets; qualitative mechanistic evidence from CRISPR/knockdown and xenograft experiments. | Prostate cancer metastasis | Mu et al., 2024, Oncogene, doi:10.1038/s41388-024-03165-3, https://doi.org/10.1038/s41388-024-03165-3 (pqac-00000004, pqac-00000007, pqac-00000008) |
| Biomarker performance in ACLF | THBS1 was the top significantly upregulated PBMC transcript in HBV-related ACLF and tracked disease severity, inflammation, and hepatocellular apoptosis; plasma THBS1 showed prognostic utility for short-term mortality. | Transcriptome subset: ACLF=20, LC=10, CHB=10, NC=15 within 330 COSSH participants. qPCR validation: ACLF=110, LC=60, CHB=60, NC=45. AUROC 0.8438 (28 d) and 0.7778 (90 d) for qPCR; plasma ELISA cohort ACLF=198, LC=50, CHB=50, NC=50 with AUROC 0.7445 (28 d) and 0.7175 (90 d); optimal plasma cutoff <28 µg/ml; correlation with ALT and γ-GT, P=0.01. | Acute-on-chronic liver failure (HBV-related) | Hassan et al., 2024, BMC Med, doi:10.1186/s12916-024-03318-x, https://doi.org/10.1186/s12916-024-03318-x (pqac-00000010, pqac-00000012) |
| Functional causality in liver failure model | Hepatocyte-specific THBS1 knockout improved survival and reduced inflammatory cytokines and hepatocyte apoptosis in experimental liver failure, supporting a pathogenic role for THBS1 in ACLF. | Survival study n=18/group over 48 h; serum/time-point analyses n=10 per time point; reported significance included ****P<0.0001 vs WT in the excerpt. | Experimental acute liver failure / ACLF mechanism | Hassan et al., 2024, BMC Med, doi:10.1186/s12916-024-03318-x, https://doi.org/10.1186/s12916-024-03318-x (pqac-00000010) |
| CKD-associated cardiac remodeling | THBS1 drives cardiac remodeling in CKD; murine CKD increased myocardial THBS1 with left ventricular hypertrophy, fibrosis, and dysfunction, while TSP1 knockout was protective. | Quantitative cohort or AUROC values were not provided in the gathered excerpt. | Chronic kidney disease–associated cardiovascular disease | Julovi et al., 2024, JACC Basic Transl Sci, doi:10.1016/j.jacbts.2024.01.010, https://doi.org/10.1016/j.jacbts.2024.01.010 (pqac-00000009) |
| Obesity/fibro-adipogenic remodeling | THBS1 promotes fibro-adipogenic progenitor expansion and contractile dysfunction of the diaphragm in obesity through TGF-β-associated stromal remodeling; Thbs1 loss is protective. | No numeric effect size in the excerpt; authors describe THBS1 as a necessary mediator and potential therapeutic target. | Obesity-associated respiratory muscle dysfunction | Buras et al., 2024, JCI Insight, doi:10.1172/jci.insight.175047, https://doi.org/10.1172/jci.insight.175047 (pqac-00000019) |


*Table: This table summarizes verified THBS1 mechanisms, receptors, and signaling pathways alongside the main 2024 quantitative findings available in the gathered evidence. It is useful as a compact evidence map linking annotation-relevant biology to translational and disease-focused data.*