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Last update 23 Jan 2025

Siglec-9

Last update 23 Jan 2025

Basic Info

Synonyms

CD329, CDw329, Protein FOAP-9

+ [4]

Introduction

Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.

Drugs associated with Siglec-9

aSE4-1-Fc

Target

Siglec-9

Mechanism

Siglec-9 inhibitors

Active Org.

University of Science & Technology of China

Originator Org.

University of Science & Technology of China

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

HBM1057

Target

Siglec-7 x Siglec-9

Mechanism

Siglec-7 inhibitors [+1]

Active Org.

Harbour BioMed (Shanghai) Co., Ltd.

Originator Org.

Harbour BioMed (Shanghai) Co., Ltd.

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Siglec-7/9 degrader(The Scripps Research Institute)

Target

Siglec-7 x Siglec-9

Mechanism

Siglec-7 modulators [+1]

Active Org.

The Scripps Research Institute

Originator Org.

The Scripps Research Institute

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with Siglec-9

100 Translational Medicine associated with Siglec-9

0 Patents (Medical) associated with Siglec-9

227

Literatures (Medical) associated with Siglec-9

01 Mar 2025·International Journal of Biological Macromolecules

Identification of potential therapeutic targets for Alzheimer's disease from the proteomes of plasma and cerebrospinal fluid in a multicenter Mendelian randomization study

Article

Author: Wang, Shengnan ; Wang, Jianglong ; Xi, Jianxin ; Zhang, Mengyuan

BACKGROUNDCertain peripheral proteins are believed to be involved in the development of Alzheimer's disease (AD), but the roles of other new protein biomarkers are still unclear. Current treatments aim to manage symptoms, but they are not effective in stopping the progression of the disease. New drug targets are needed to prevent Alzheimer's disease.METHODSWe used Mendelian randomization (MR) to study drug targets for Alzheimer's disease. We analyzed data from the European Alzheimer's and Dementia Biobank consortium and replicated our findings in GWAS data from IGAP and FinnGen cohorts. We identified genetic instruments for plasma and cerebrospinal fluid (CSF) proteins and conducted sensitivity analyses using various methods. Additionally, a comparison and analysis of protein-protein interactions (PPI) were conducted to identify potential causal proteins. The implications of these findings were further explored through an examination of existing AD drugs and their respective targets.RESULTSThrough MR analysis, 10 protein AD pairs were identified as statistically significant at the Bonferroni level (P < 6.35 × 10^-5). The specific findings indicate that elevated levels of plasma cathepsin H (CTSH) (OR = 1.06, 95%CI: 1.03-1.08, p = 6.12 × 10^-6), plasma signal regulatory protein alpha (SIRPA) (OR = 1.03, 95%CI: 1.02-1.05, p = 1.37 × 10^-5), plasma TMEM106B (OR = 1.16, 95%CI: 1.09-1.23, p = 1.92 × 10^-6), and CSF bone sialoprotein (BSP) (OR = 1.33, 95%CI: 1.17-1.51, p = 9.34 × 10^-6), CSF Interleukin-34 (IL-34) (OR = 2.13, 95%CI: 1.51-3.01, p = 1.85 × 10^-5), CSF immunoglobulin-like transcript 2 (ILT-2) (OR = 1.33, 95%CI: 1.17-1.51, p = 9.34 × 10^-6) are associated with an increased risk of AD, while increased levels of plasma progranulin gene (GRN) (OR = 0.79, 95%CI: 0.74-0.84, p = 2.19 × 10^-12), plasma triggering receptor expressed on myeloid cells 2 (TREM2) (OR = 0.67, 95%CI: 0.58-0.78, p = 6.95 × 10^-8), plasma sialic acid-bind immunoglobulin-like lectins (SIGLEC)-9 (OR = 0.67, 95%CI: 0.58-0.78, p = 6.95 × 10^-8), and CSF SIGLEC7 (OR = 0.42, 95%CI: 0.28-0.64, p = 4.30 × 10^-5) are associated with a decreased risk of AD. Bayesian colocalization found that the above protein-related genes shared the same mutation as AD.CONCLUSIONIncreased levels of plasma CTSH, SIRPA, TMEM106B, CSF BSP, CSF IL-34, and CSF ILT-2 have been found to be correlated with an elevated risk of AD, whereas elevated levels of plasma GRN, TREM2, SIGLEC9, and CSF SIGLEC7 are associated with a decreased risk of developing AD. Further investigation through clinical trials is needed.

01 Jan 2025·Advanced Science

Comprehensive Modular Synthesis of Ganglioside Glycans and Evaluation of their Binding Affinities to Siglec‐7 and Siglec‐9

Article

Author: Adak, Avijit K. ; Tseng, Hsin‐Kai ; Lyu, Ke‐Hong ; Lu, Wen ; Lin, Chun‐Cheng ; Chiang, Yu‐Ching ; Kuo, Wen‐Hua ; Lee, Yun‐Sheng ; Chang, Shu‐Yen ; Angata, Takashi

AbstractIn the present work, bacterial glycosyltransferases are utilized to construct ganglioside glycans in a convergent approach via a sugar‒nucleotide regeneration system and one‐pot multienzyme reactions. Starting from β‐lactoside enables the diversification of both the glycan moieties and the linkages in the lower α‐arm and upper β‐arm. Overall, a comprehensive panel of 24 natural a‐series (GM3, GM2, GM1a, GD1a, GT1a, and fucosyl‐GM1), b‐series (GD3, GD2, GD1b, GT1b, and GQ1b), c‐series (GT3, GT2, GT1c, GQ1c, and GP1c), α‐series (GM1α, GD1aα, and GT1aα), and o‐series (GA2, GA1, GM1b, GalNAc‐GM1b, and GD1c) ganglioside glycans are prepared, which are suitable for biological studies and further applications. Moreover, a microarray is constructed with these synthesized ganglioside glycans to investigate their binding specificity with recombinant Fc‐fused Siglec‐7 and Siglec‐9, which are immune checkpoint‐like glycan recognition proteins on natural killer cells. The microarray binding results reveal that GD3 and GT1aα are specific ligands for Siglec‐7 and Siglec‐9, respectively, and this discovery can lead to the identification of appropriate ligands for investigating the roles of these Siglecs in immunomodulation.

16 Dec 2024·Journal of Clinical Investigation

Sialylated glycoproteins suppress immune cell killing by binding to Siglec-7 and Siglec-9 in prostate cancer

Article

Author: Stark, Jessica C. ; Bertozzi, Carolyn R ; Marti, G Edward W ; Brooks, James D. ; Bertozzi, Carolyn R. ; Nolley, Rosalie ; Pitteri, Sharon J ; Wen, Ru M. ; Stark, Jessica C ; Fan, Zenghua ; Totten, Sarah M. ; Totten, Sarah M ; Brooks, James D ; Engleman, Edgar G. ; Garcia Marques, Fernando Jose ; Zhang, Xiangyue ; Bermudez, Abel ; Pitteri, Sharon J. ; Fong, Lawrence ; Engleman, Edgar G ; Riley, Nicholas M ; Lyu, Aram ; Wen, Ru M ; Riley, Nicholas M. ; Marti, G. Edward W. ; Zhao, Hongjuan

Prostate cancer is the second leading cause of male cancer death in the U.S. Current immune checkpoint inhibitor-based immunotherapies have improved survival for many malignancies; however, they have failed to prolong survival for prostate cancer. Siglecs (sialic acid-binding immunoglobulin-like lectins) are expressed on immune cells and regulate their function. Siglec-7 and Siglec-9 contribute to immune evasion in cancer by interacting with sialic acid-containing glycoprotein ligands on cancer cells. However, the role of Siglec-7/9 receptors and their ligands in prostate cancer remains poorly understood. Here, we find that Siglec-7 and Siglec-9 are associated with poor prognosis in patients with prostate cancer and are highly expressed in myeloid cells, including macrophages, in prostate tumor tissues. Siglec-7 and -9 ligands were expressed in prostate cancer cells and human prostate tumor tissues. Blocking the interactions between Siglec-7/9 and sialic acids inhibited prostate cancer xenograft growth and increased immune cell infiltration in humanized mice in vivo. Using a CRISPRi screen and mass spectrometry, we identified CD59 as a candidate Siglec-9 ligand in prostate cancer. The identification of Siglec-7 and -9 as potential therapeutic targets, including the CD59/Siglec-9 axis, opens up opportunities for immune-based interventions in prostate cancer.

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Siglec-9

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