HSPA1A

Case study 1: Dexun Hao, 2021

Chronic obstructive pulmonary disease (COPD) is characterized by airway obstruction and progressive lung inflammation. As the primary ingredient of a traditional Chinese medical herb, Baicalin has been previously shown to possess anti-inflammatory abilities. Thus, the current study aimed to elucidate the mechanism by which baicalin alleviates COPD.

Baicalin was adopted to treat cigarette smoke in extract-exposed MLE-12 cells after which cell viability and apoptosis were determined. A COPD mouse model was constructed via exposure to cigarette smoke and lipopolysaccharide, baicalin treatment. The effect of HSP72 and JNK on COPD following treatment with baicalin was assessed both in vivo and in vitro by conducting loss- and gain- function experiments. Baicalin treatment increased HSP72 expression, while its depletion reversed the effect of baicalin on COPD. HSP72 inhibited the activation of JNK, while JNK activation was found to inhibit the effect of baicalin on COPD.

Fig1. The expression of HSP72 normalized to GAPDH was analyzed using immunoblotting after MLE-12 cells were treated with baicalin for 24 h and stimulated by CSE for 2 h.

Fig2. MLE-12 cells were transfected with si-HSP72 and the expression of HSP72 and JNK phosphorylation normalized to GAPDH was analyzed by immunoblotting.

Case study 2: Chieh-Ting Fang, 2020

The heat shock protein 70 (HSP70) is a conserved molecular chaperone and proteostasis regulator that protects cells from pharmacological stress and promotes drug resistance in cancer cells. In this study, the researchers found that HSP70 may promote resistance to anticancer drugs that target the mitotic kinesin, Eg5, which is essential for assembly and maintenance of the mitotic spindle and cell proliferation. The data show that loss of HSP70 activity enhances Eg5 inhibitor-induced cytotoxicity and spindle abnormalities. Furthermore, HSP70 colocalizes with Eg5 in the mitotic spindle, and inhibition of HSP70 disrupts this colocalization. Using ground state depletion microscopy followed by individual molecule return (GSDIM), they found that HSP70 inhibition reduces the size of Eg5 ensembles and prevents their localization to the inter-polar region of the spindle. In addition, bis(maleimido)hexane-mediated protein-protein crosslinking and proximity ligation assays revealed that HSP70 inhibition deregulates the interaction between Eg5 tetramers and TPX2 at the spindle pole, leading to their accumulation in high-molecular-weight complexes.

Fig3. HSP70 chaperone activity attenuates cell sensitivity to Eg5 inhibitors. HSP70 inhibitors enhanced the cytotoxicity of SB743921.

Fig4. Representative images show the Eg5 distribution within the spindle of the control (h. pLKO.1) and HSP70-depleted (i, shHSP70) prometaphase and metaphase cells.

Fig1. Aqueous CSE stimulation promotes the activation of the JNK pathway thereby promoting the development of COPD, while baicalin can up-regulate the expression of HSP72, which in turn inhibits the activity of the JNK pathway and impedes the development of COPD. (Dexun Hao, 2021)

Fig2. Schematic representation of the model of Hsp70 anti-metastatic function on cancer cells. (Panagiota Kasioumi, 2019)

HSPA1A involved in several pathways and played different roles in them. We selected most pathways HSPA1A participated on our site, such as Spliceosome, MAPK signaling pathway, Protein processing in endoplasmic reticulum, which may be useful for your reference. Also, other proteins which involved in the same pathway with HSPA1A were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

HSPA1A has several biochemical functions, for example, ATP binding, ATPase activity, ATPase activity, coupled. Some of the functions are cooperated with other proteins, some of the functions could acted by HSPA1A itself. We selected most functions HSPA1A had, and list some proteins which have the same functions with HSPA1A. You can find most of the proteins on our site.

HSPA1A has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with HSPA1A here. Most of them are supplied by our site. Hope this information will be useful for your research of HSPA1A.

EGFR; STUB1; SNCA; HSP90AA1