This protein is a member of the large oligomerization domain (NOD)-like receptor-family of cytoplasmic immune receptors, which upon the detection of certain pathogens or of an internal distress signal, initiates a caspase-1-mediated inflammatory response. HSPA8 interacts with both NLRC4 and mutated NLRC4.

2021年8月6日 · Prior studies have placed substantial emphasis on the role of heat shock protein family A member 8 (HSPA8) on postischemic myocardial inflammation and cardiac dysfunction. However, it has never been determined whether HSPA8 participates in astrocyte activation and thus mediated neuroinflammation associated with SCII.

2024年5月2日 · Geranylgeranylacetone (GGA)-induced HSPA8 overexpression in cecum ligation and puncture (CLP) mice could significantly reduce systemic inflammatory response and mortality, effectively protect lung function, whilst HSPA8 inhibitor VER155008 aggravated this effect.

2023年7月20日 · Heat shock protein family A member 8 (HSPA8) participates in the folding or degradation of misfolded proteins under stress and plays critical roles in cancer. In this study, we investigated the...

2023年8月14日 · Here, we identify heat shock protein family A member 8 (HSPA8) as a new type of enzyme — which we name as ‘amyloidase’ — that directly disassembles RHIM-amyloids to inhibit necroptosis signaling...

2023年5月1日 · HSPA8 promotes inflammation by promoting the expression of LPS-induced inflammatory factors. HSPA8 (Heat shock 70 kDa protein 8) is a molecular chaperone involved in a variety of cellular processes. This gene may affect the proliferation, apoptosis and immune function of chicken macrophages, but the specific mechanism remains unclear.

HSPA8 Is Identified as a Novel Regulator of Hypertensive Disorders in Pregnancy by Modulating the beta-Arrestin1/A1AR Axis. Heat Shock Protein Member 8 (HSPA8) Is Involved in Porcine Reproductive and Respiratory Syndrome Virus Attachment and Internalization.

A small-molecule inducer of HSPA8 or exosomes containing HSPA8 can restore the regulatory activity of HSPA8, thereby curtailing SREBP signaling, ceasing excessive and unregulated lipid production, and mitigating inflammation and fibrosis.

2019年8月7日 · HSPA8 is a crucial molecular regulator of chaperone-mediated autophagy, as a detector of substrates that will be processed by this specialized autophagy pathway. In this review, we shortly summarize its structure and overall functions, dissect its implication in immune disorders, and list the known pharmacological tools that modulate its functions.

In the present study, we described the interaction of HSPA8 (HSC70), the constitutive cytosolic member of the HSP70 family, with lipid membranes. HSPA8 showed high selectivity for negatively charged phospholipids, such as phosphatidylserine and cardiolipin, and low affinity for phosphatidylcholine.