GUCA2A

Last update 08 May 2025

Basic Info

Synonyms

GCAP-I, guanylate cyclase activator 2A, Guanylate cyclase-activating protein 1

+ [6]

Introduction

Endogenous activator of intestinal guanylate cyclase. It stimulates this enzyme through the same receptor binding region as the heat-stable enterotoxins.

100 Clinical Results associated with GUCA2A

100 Translational Medicine associated with GUCA2A

0 Patents (Medical) associated with GUCA2A

376

Literatures (Medical) associated with GUCA2A

01 Jan 2025·Journal of Peptide Science

cDNA Display Selection of Interacting Peptide Ligands of the Guanylate Cyclase C Receptor

Article

Author: Ochiai, Eri ; Inokuchi, Shota ; Sumiya, Akie ; Hasegawa, Makoto ; Takahashi, Yuki

ABSTRACTGuanylate cyclase C (GC‐C), a receptor expressed on the apical membrane of intestinal mucosal cells, is activated by heat‐stable enterotoxin (STa) produced by enterotoxigenic Escherichia coli, as well as the endogenous ligands guanylin and uroguanylin. In this study, novel peptides that interact with GC‐C were generated using the cDNA display method, and their binding affinity and biological activity were evaluated. While the linear peptide library did not yield peptides with sufficient affinity for GC‐C, three cyclic peptides (GCC‐P1, GCC‐P2, and GCC‐P3), each containing two cysteine residues within a 15‐residue sequence, were obtained from a cyclic peptide library containing nine‐residue random sequences. GC‐P2 exhibited significant binding affinity in Biacore assays, although the affinity was lower than those reported for known ligands. Notably, GCC‐P2 and GCC‐P3 demonstrated enhanced cGMP activity when used in combination with linaclotide. However, the agonist activity of these peptides was minimal, indicating that further modifications may be necessary to develop them for clinical applications. This study successfully extracted consensus sequences of peptide motifs that bind to GC‐C from a highly diverse nine‐residue random sequence library, which provides fundamental insights for the discovery and optimization of novel GC‐C ligands.

01 Jan 2025·Journal of Peptide Science

Coupling enterotoxigenic Escherichia coli heat‐stable peptide toxin with 8‐arm PEG enhances immunogenicity

Article

Author: Chaukimath, Pooja ; Zegeye, Ephrem Debebe ; Visweswariah, Sandhya S. ; Puntervoll, Pål ; Diaz, Yuleima

Enterotoxigenic Escherichia coli (ETEC) strains, which produce the heat‐stable enterotoxin (ST) either alone or in combination with the heat‐labile enterotoxin, contribute to the bulk of the burden of child diarrheal disease in resource‐limited countries and are associated with mortality. Developing an effective vaccine targeting ST presents challenges due to its potent enterotoxicity, non‐immunogenicity, and the risk of autoimmune reaction stemming from its structural similarity to the human endogenous ligands, guanylin, and uroguanylin. This study aimed to assess a novel synthetic vaccine carrier platform employing a single chemical coupling step for making human ST (STh) immunogenic. Specifically, the method involved cross‐linking STh to an 8‐arm N‐hydroxysuccinimide (NHS) ester‐activated PEG cross‐linker. A conjugate of STh with 8‐arm structure was prepared, and its formation was confirmed through immunoblotting analysis. The impact of conjugation on STh epitopes was assessed using ELISAs with polyclonal and monoclonal antibodies targeting various epitopes of STh. Immunization of mice with the conjugate induced the production of anti‐STh antibodies, exhibiting neutralizing activity against STh.

01 Jun 2024·Environmental Pollution

CXCL1/IGHG1 signaling enhances crosstalk between tumor cells and tumor-associated macrophages to promote MC-LR-induced colorectal cancer progression

Article

Author: Fu, Wenjuan ; Zhang, Guowei ; Wang, Yiqi ; Wang, Lingqiao ; Wu, Zhiling ; Chen, Weiyan ; Cui, Ke ; Qiu, Zhiqun ; Jin, Huidong ; Guo, Chengwei ; Liu, Wenbin ; Zhou, Ziyuan ; Tan, Yao

Microcystin-leucine arginine (MC-LR) is a common cyantotoxin produced by hazardous cyanobacterial blooms, and eutrophication is increasing the contamination level of MC-LR in drinking water supplies and aquatic foods. MC-LR has been linked to colorectal cancer (CRC) progression associated with tumor microenvironment, however, the underlying mechanism is not clearly understood. In present study, by using GEO, KEGG, GESA and ImmPort database, MC-LR related differentially expressed genes (DEGs) and pathway- and gene set-enrichment analysis were performed. Of the three identified DEGs (CXCL1, GUCA2A and GDF15), CXCL1 was shown a positive association with tumor infiltration, and was validated to have a dominantly higher upregulation in MC-LR-treated tumor-associated macrophages (TAMs) rather than in MC-LR-treated CRC cells. Both CRC cell/macrophage co-culture and xenograft mouse models indicated that MC-LR stimulated TAMs to secrete CXCL1 resulting in promoted proliferation, migration, and invasion capability of CRC cells. Furtherly, IP-MS assay found that interaction between TAMs-derived CXCL1 and CRC cell-derived IGHG1 may enhance CRC cell proliferation and migration after MC-LR treatment, and this effect can be attenuated by silencing IGHG1 in CRC cell. In addition, molecular docking analysis, co-immunoprecipitation and immunofluorescence further proved the interactions between CXCL1 and IGHG1. In conclusion, CXCL1 secreted by TAMs can trigger IGHG1 expression in CRC cells, which provides a new clue in elucidating the mechanism of MC-LR-mediated CRC progression.

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GUCA2A

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