Last update 01 Nov 2024

PTX3

Last update 01 Nov 2024

Basic Info

Synonyms

Pentaxin-related protein PTX3, pentraxin 3, Pentraxin-related protein PTX3

+ [7]

Introduction

Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility.

Drugs associated with PTX3

HC-HA/PTX3

Target

PTX3

Mechanism

PTX3 stimulators

Active Org.

BioTissue Holdings, Inc.

Originator Org.

BioTissue Holdings, Inc.

Active Indication

Retinal Diseases

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

CN116102634

Patent Mining

Target

PTX3

Mechanism-

Active Org.

Yantai University

Originator Org.

Yantai University

Active Indication

Infectious Diseases

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Pentraxin 3

Target

PTX3

Mechanism

PTX3 stimulators

Active Org.-

Originator Org.

Sigma-Tau Industrie Farmaceutiche Riunite SpA

Active Indication-

Inactive Indication

Aspergillosis [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with PTX3

100 Translational Medicine associated with PTX3

0 Patents (Medical) associated with PTX3

2,385

Literatures (Medical) associated with PTX3

01 Dec 2024·Tissue and Cell

Presence of heavy chain-hyaluronan/pentraxin 3 (HC-HA/PTX3) complex in human umbilical cord

Article

Author: Zhang, Suzhen ; Tseng, Scheffer C G ; Tseng, Scheffer C.G.

The heavy chain (HC)-hyaluronan (HA)/pentraxin 3 (HC-HA/PTX3) complex is formed by tumor necrosis factor-stimulated gene-6 (TSG-6) catalyzing the covalent (ester bond) transfer of HC1 from inter-α-trypsin inhibitor (IαI) to HA followed by tight binding of PTX3. The presence of such a complex has been found in human amniotic membrane (AM) and is considered to be a major matrix component responsible for its anti‑inflammatory and anti‑scarring properties to promote regenerative healing. Because the therapeutic potentials of AM and umbilical cord (UC) are similar, we herein evaluated whether human UC also contains HC-HA/PTX3. Immunostaining of UC cross-sections showed abundant PTX3, HC1, HA, TSG-6, and bikunin. Western blot analysis suggested the presence of HC1 complex bound via a NaOH-sensitive bond and tightly bound to PTX3 multimer in UC and AM extracts but not in chorion and placenta extracts. HC-HA/PTX3 was purified from UC extract by successive runs of density gradient ultracentrifugation and verified the presence of HC1 but not HC2 or HC3 based on western blot analysis. These results suggest the presence of HC-HA/PTX3 complex in UC is similar to AM.

01 Nov 2024·Animal Reproduction Science

MiR-29b inhibits COC expansion and oocyte in vitro maturation via induction of ROS by targeting CYCS

Article

Author: Qi, Nanshan ; Zhan, Xiaoshu ; Toms, Derek ; Li, Julang ; Fletcher, Lauren ; Wang, Bingyun ; Freiburger, Renee

Cumulus-oocyte complex (COC) expansion and oocyte maturation are crucial processes for embryo development and fertility across species. Although miR-29b has been detected in porcine ovarian granulosa cells, its specific role in regulating oocyte maturation remains largely unknown. In this study, using the pig as a model, we report that over-expression of miR-29b lead to a decrease of COC expansion area and inhibits oocyte maturation (P<0.05). This suppression correlated with a decrease expression of COC-expansion-associated genes, including SHAS2, ADAMTS1, ADAMTS2, ADAMTS17 and PTX 3 in both mural granulosa cells (mGCs) and cumulus granulosa cells (cGCs). Further investigation revealed that miR-29b over-expression induces reactive oxygen species (ROS) accumulation in both mGCs and cGCs, conversely, knock-down of miR-29b reverses all these effects. Treatment with the antioxidant β-mercaptoethanol alleviates ROS accumulation, rescues COC expansion and restores oocyte polar body formation impaired by miR-29b mimics. Computational analysis predicted CYCS, the gene encoding cytochrome C, as a potential target of miR-29b. Subsequent examination demonstrated that miR-29b downregulates CYCS at both mRNA and protein levels. Dual-luciferase reporter assays further confirmed that miR-29b interacts with the 3'-untranslated region (3'UTR) of CYCS. Over-expression of CYCS decreases ROS accumulation and promotes COC expansion (P<0.05). These results indicate that miR-29b regulates COC expansion and oocyte maturation in vitro by inducing ROS, likely through targeting of CYCS. This study sheds light on the role of miR-29b in oocyte maturation and provides insight into the regulatory function of miRNAs in ovarian physiology.

01 Nov 2024·Genomics

Characterization of small RNAs in the spleen of MASH in a non-human primate model

Article

Author: Zhang, Liwei ; Wang, Bo ; Liu, Enqi ; Cao, Wenbin ; Zhang, Yanru ; Li, Yandong ; Zhao, Yuelei ; Qin, Hongyu ; Ding, Ruike ; Ye, Yun ; Qu, Pengxiang ; Hu, Liangshuo ; Duan, Chenjing ; Zhao, Juan ; Leng, Haoze

Metabolic dysfunction-associated steatotic liver disease (MASLD) and its advanced stage, metabolic dysfunction-associated steatohepatitis (MASH), are increasingly recognized as a global health issue. This study examines the role of small RNAs in the spleen of MASH using a non-human primate model. We performed high-throughput small RNA sequencing on spleen tissues from MASH-primates, revealing significant alterations in the expression of small non-coding RNAs, especially miRNAs. Notably, miR-96, miR-182, miR-183, and miR-122 showed differential expression in MASH spleens. Predictive and validation studies have identified potential target genes, such as PTX3 and NFIX, that were significantly dysregulated in spleens of MASH. These findings characterized small RNAs in spleen of MASH and offer a novel insight for further research for MASH.

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PTX3

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