UROS

Last update 08 May 2025

Basic Info

Synonyms

Hydroxymethylbilane hydrolyase [cyclizing], UROIIIS, uroporphyrinogen III synthase

+ [3]

Introduction

Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins (PubMed:11689424, PubMed:18004775). Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme).

100 Clinical Results associated with UROS

100 Translational Medicine associated with UROS

0 Patents (Medical) associated with UROS

338

Literatures (Medical) associated with UROS

01 Apr 2025·Molecular and Cellular Endocrinology

p75NTR antagonist THX-B increases mature nerve growth factor secretion by bladder cells through decreased activity of matrix metalloproteinase-9

Article

Author: Hajj, Aya ; Saragovi, H Uri ; Sirmakesyan, Stephanie ; Campeau, Lysanne ; Hamouda, Aalya ; Cammisotto, Philippe G

In urine samples from an aging female cohort with overactive bladder syndrome (OAB), the proteolytic activity of matrix metalloproteinase-9 (MMP-9), an enzyme which degrades mature NGF, was elevated and associated with low levels of nerve growth factor (NGF). Given that a substantial portion of urine constituents originate from bladder cellular processes, we examined the synthesis of NGF and MMP-9 in rat urothelial (UROs) and smooth muscle (SMCs) cells in culture. NGF and proNGF were found expressed and released by both cell types while UROs were the major source of secreted MMP-9. THX-B, a highly specific p75^NTR antagonist, decreased the expression of MMP-9 resulting in increased mature NGF levels in culture medium of UROs while displaying minor effects on SMCs. Likewise, CRISPR-cas9 genomic deletion of MMP-9 potently increased mature NGF levels in both cell types. On the other hand, THX-B decreased the synthesis and release of α2 Macroglobulin (α2M), a protein that stabilizes proNGF in UROs but increased it in SMCs. THX-B also increased the activity of enzymes furin and matrix metalloproteinase-7 (MMP-7), that convert proNGF to mature NGF in UROs, yielding a net increase in mature NGF and a decrease of proNGF. We conclude that p75^NTR is involved in the control of proNGF and mature NGF secretion from bladder cells through modulation of proteolytic activities. Since neurotrophins and binding to their receptors are relevant to pathologies, inhibition of p75^NTR by THX-B may be exploited in a therapeutic strategy.

01 Mar 2025·BMJ Case Reports

Congenital erythropoietic porphyria: the overlooked inherited disorder

Article

Author: Kumar, Mritunjay ; Shukla, Amit ; Mishra, Namita ; Upadhyaya, Amrita ; Prasad, Bimlesh

Congenital erythropoietic porphyria (CEP) also known as Gunther’s disease is a subtype of porphyria. It is an autosomal recessive disorder caused by a mutation in the uroporphyrinogen III gene (URO III) coding for the enzyme UROS synthase, an essential enzyme in the heme synthesis pathway. The condition may present as non-immune hydrops in foetuses, dark-red urine-stained diapers in neonates and skin blistering and mutilation in sun-exposed areas in older children. Enzyme assays and genetic studies are costly and not easily available in low-resource settings; therefore, awareness of the typical phenotype of this rare porphyria is crucial. However, due to the scarcity of reported cases, clinicians remain oblivious to the disease, leading to delays in diagnosis and initiation of treatment, thus contributing to long-term disabilities. We report a case of a male child in early adolescence presenting with classical cutaneous, skeletal and haematological features of CEP.

01 Mar 2025·American Journal of Reproductive Immunology

Finding Potential Drug Targets for Pre‐Eclampsia Using Mendelian Randomisation and Colocalisation Analysis

Article

Author: Zhao, Tingting ; Wu, Chengqian ; Pan, Yingzi ; Ji, Xiaohong ; Xu, Yuexin ; Miao, Jiayan

ABSTRACTIntroductionPre‐eclampsia (PE) is a common complication of pregnancy and there is an urgent need for new drug targets. We performed whole proteome‐wide Mendelian randomisation (MR) and colocalisation analyses to identify potential therapeutic targets for PE.Material and MethodsA two‐sample MR study was conducted using summary‐level statistics of 734 plasma proteins retrieved from large genome‐proteome‐wide association studies. The summary statistics of PE or eclampsia were obtained from the FinnGen consortium. Wald ratio and Inverse variance weighted (IVW) were used to assess the causal association between proteins and PE. Colocalisation analyses were conducted to examine whether the identified proteins and PE shared incidental variants.ResultsGenetically predicted circulating levels of 42 proteins were associated with PE risk after Benjamini‐Hochberg correction. Nineteen of the gene‐predicted proteins showed evidence of increased PE risk (CRELD1, CPA4, AHSG, NFASC, QDPR, NTM, PZP, FAM171B, RTN4R, FLRT2, ADH4, ADM, SPINK5, LGALS4, CKM, SPON2, UROS, CXCL10 and APOBEC3G); 23 proteins reduced the risk of PE (CLIC5, NEO1, SWAP70, KLK8, VWA2, FSTL1, CXCL11, APOB, NPPB, CNTN4, IL12B, ACHE, TCN1, GFRA2, GNMT, HPGDS, DPT, MANBA, SPARCL1, ACE, FUT8, BST1 and ACP1). Bayesian colocalisation indicated that six proteins (VWA2, ACHE, CXCL10, PZP, AHSG and UROS) and PE, which were identified as high evidence of colocalisation with PE.ConclusionsThis study provides evidence of the causal association between genetically predicted 42 proteins associated with PE risk, which might be promising drug targets for PE.

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