FGA

Case Study 1: Hui Li, 2022

Angiogenesis is the key condition for the development of endometriosis (EM). This study was aimed to elucidate the role of FGA in endometrial stromal cells involved in angiogenesis in EM. The conditioned medium (CM) of human primary eutopic endometrial stromal cells (EuESC) and immortalized endometrial stromal cell line hEM15A with FGA knockdown were collected and used to treat human umbilical vein endothelial cells (HUVECs). Then, tube formation assay, EdU assay, wound assay, transwell assay and flow cytometry assays were performed to assess the function of HUEVCs in vitro. Functionally, CM of endometrial stromal cells with FGA knockdown could inhibit HUEVCs migration and tube formation in vitro and in vivo, while having no significant effect on HUVECs proliferation, apoptosis and cell cycle. Mechanically, the expression of VEGFA, PDGF, FGF-B, VEGF, MMP-2 and MMP-9 was reduced in hEM15A cells with FGA knockdown.

Fig1. Edu assay showing the proliferation of HUEVCs treated with CM from hEM15A shNC and hEM15A shFGA cells.

Fig2. The protein expression of VEGFA, VEGF, MMP-2 and MMP-9 in hEM15A with FGA knockdown was detected by western blotting.

Case Study 2: Guangli Liu, 2022

This study aims to investigate the expression levels of fibrinogen α chain (FGA) in human gastric cancer (GC) tissues and cell lines, clarify its role in gastric cancer progression, and explore its underlying mechanism. Luciferase and CHIP assays were performed to confirm the transcriptional regulation of FGA on ITGA5. Immunoblot assays and double-label RFP-GFP-LC3 immunofluorescence analysis were conducted to detect its effects on gastric cancer cell autophagy and FAK/ERK pathway, and in vivo tumor growth assays were further performed. The low expression of FGA in human gastric cancer tissues and cell lines. FGA suppressed gastric cancer cell proliferation, motility, and EMT process, and stimulated cell autophagy. Further, FGA suppressed the expression of Integrin-α5 (ITGA5) and inhibited the FAK/ERK pathway, therefore suppressing the progression of gastric cancer. The in vivo assays further confirmed that FGA suppressed tumor growth of gastric cancer cells in the BALB/c nude mice (18-22 g, female, 8-week-old) through suppressing ITGA5-mediated FAK/ERK pathway in mice.

Fig3. Immunoblot assays showed the expression of FGA in 3 representative gastric cancer tissues and normal tissues.

Fig4. FGA suppresses ITGA5 expression and activates FAK/ERK pathway.

FGA involved in several pathways and played different roles in them. We selected most pathways FGA participated on our site, such as Complement and coagulation cascades, Platelet activation, which may be useful for your reference. Also, other proteins which involved in the same pathway with FGA were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

FGA has several biochemical functions, for example, contributes_to cell adhesion molecule binding, protein binding, protein binding, bridging. Some of the functions are cooperated with other proteins, some of the functions could acted by FGA itself. We selected most functions FGA had, and list some proteins which have the same functions with FGA. You can find most of the proteins on our site.

FGA 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 FGA here. Most of them are supplied by our site. Hope this information will be useful for your research of FGA.

FGB; FGG; APOA1; KLK6; PASK; F2; MIS12; KRT18; p29991-pro_0000037941; p29991-pro_0000037946; PRRC2A; d-mannose; crlkekhc; IGHG1; IGHA1; ALB

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