AGBL3

Last update 08 May 2025

Basic Info

Synonyms

AGBL carboxypeptidase 3, AGBL3, ATP/GTP-binding protein-like 3

+ [4]

Introduction

Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK. May catalyze the hydrolysis of aspartate from the carboxy-terminus of target proteins. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of target proteins. Metallocarboxypeptidase that mediates tubulin deglutamylation.

100 Clinical Results associated with AGBL3

100 Translational Medicine associated with AGBL3

0 Patents (Medical) associated with AGBL3

Literatures (Medical) associated with AGBL3

01 Mar 2025·Journal of Biological Chemistry

Complement-activated fragment Ba functions as an antibacterial protein and mediates immune responses in lower vertebrates

Article

Author: Li, Mo-Fei ; Jin, Xiao-Yan ; Wang, Xuan-Yue ; Luo, Hao-Bin ; Zhang, Hong-Qiang ; Sun, Yuan-Yuan ; Liu, Heng ; Li, Xue-Peng ; Feng, Zhe

The complement system plays an important role in antibacterial infection and immune regulation. Ba, an important complement component, is produced and released by the cleavage of complement factor B during complement activation. However, the immune functions of Ba are unclear. In this study, we reported that recombinant Ba exerted direct bactericidal and immune regulatory effects. Recombinant Paralichthys olivaceus Ba (rPoBa) bound bacteria via interaction with the bacterial wall component lipopolysaccharide, resulting in bacterial membrane permeabilization and bacterial death. Furthermore, rPoBa exhibited bactericidal activity against Gram-negative bacteria in a manner that depended on concentration, time, temperature, pH, and metal ions. Structure prediction analysis showed that PoBa contained three distinct complement control protein (CCP) domains. CCP1 was mainly responsible for binding to lipopolysaccharide, and both CCP1 and CCP3 might be required for bacterial membranous permeabilization. The bactericidal effects of Ba were observed only in lower vertebrates, with no such effects observed in mammals. In addition, rPoBa could protect P. olivaceus against Vibrio harveyi infection both in vitro and in vivo by significantly improving the immune activity of peripheral blood leukocytes and reducing tissue bacterial loads. Consistently, when PoCFB expression in P. olivaceus was knocked down, the PoBa production and complement activity were decreased, and bacterial replication was significantly enhanced. In conclusion, this study revealed that the complement-activated recombinant Ba fragment improved the immune defense against bacterial infection and provided a potential strategy to control disease in lower vertebrates.

01 Sep 2024·ACR Open Rheumatology

Multi‐Autoantibody Testing Identifies Expansion of Reactivity to Targeted Antigens Before a Diagnosis of Rheumatoid Arthritis

Article

Author: Martinez‐Prat, Laura ; Feser, Marie L. ; Edison, Jess D. ; Aure, Mary Ann R. ; Holers, V. Michael ; Mikuls, Ted R. ; Mahler, Michael ; Moss, LauraKay ; Deane, Kevin D. ; Goff, Salina H. ; Bergstedt, Dylan T.

ObjectiveRheumatoid arthritis (RA) has a “pre‐RA” period in which multiple autoantibodies, including antibodies to citrullinated (cit) proteins (ACPA), rheumatoid factor (RF), anti–peptidyl arginine deiminase (anti‐PAD), among others, have been described; however, few studies have tested all autoantibodies in a single pre‐RA cohort. This study aims to evaluate the prevalence of multiple autoantibodies in pre‐RA and potentially identify an autoantibody profile in pre‐RA that indicates imminent onset of clinical RA.MethodsWe evaluated 148 individuals with two pre‐ and one post‐RA diagnosis samples available from the Department of Defense Serum Repository and matched controls. Samples were tested for immuglobulin (Ig) G anti–cyclic cit peptide‐3 (anti‐CCP3), five ACPA fine specificities, five anti‐PAD isoforms, as well as RF IgA and RF IgM using commercial platforms; cutoffs were determined using levels present in <1% of controls.ResultsPositivity of anti‐CCP3, RF IgA and RF IgM, anti‐PAD1, anti–cit‐vimentin 2, anti–cit‐fibrinogen, and anti–cit‐histone 1 increased over time in pre‐RA, although anti‐PAD and ACPA fine specificities were predominately present within anti‐CCP3–positive individuals. Within anti‐CCP3–positive samples from the pre‐RA period, positivity for RFs as well as anti‐PAD and ACPA fine specificities classified samples as being closer to the time of RA diagnosis.ConclusionMultiple autoantibodies are present in pre‐RA and increase in positivity as the time of RA diagnosis approaches. These results confirm previous findings predicting imminent RA and provide a pathway using commercial‐grade assays to assess the risk for and timing of development of clinical RA.

01 Aug 2024·Practical Laboratory Medicine

A comparison of anti-cyclic citrullinated peptides (CCP3 and CCP3.1) autoantibody tests in rheumatoid arthritis

Author: Nandakumar, Vijayalakshmi ; Feser, Marie L. ; Novis, Camille L. ; Nelson, Heather A. ; Banerjee, Dipanwita ; Deane, Kevin D.

BackgroundAnti-citrullinated protein antibodies (ACPA) are a specific serological biomarker used in the diagnosis of rheumatoid arthritis (RA). In clinical practice ACPA can be identified using immunoassays targeting synthetic cyclic citrullinated peptides (CCP). The 3rd generation anti-CCP IgG antibody (CCP3) offers improved sensitivity compared to the earlier versions. Recently, CCP3.1, capable of detecting both IgG and IgA antibodies, was introduced to enhance sensitivity, especially in patients with early RA.MethodsWe assessed serum CCP3.1 against CCP3 in 331 subjects undergoing RA panel serology, comprising 136 patients with RA and 195 patients without RA. Sera were tested for anti-CCP IgG (CCP3) and anti-CCP IgG/IgA (CCP3.1) antibodies. Clinical performance of these tests was compared at manufacturer-suggested cutoffs. A separate set of 81 patients with a diagnosis of RA by 2010 criteria and whose samples were obtained from within 1-year of RA diagnosis was similarly assessed to evaluate assay performance in an independent clinical RA cohort.ResultsOverall diagnostic accuracy was similar; CCP3 had an area under the curve (AUC) of 0.88, CCP3.1 had an AUC of 0.89. Sensitivity, specificity, positive predictive value (PPV), and negative predictive value (NPV) for CCP3 were 79 %, 91 %, 86 %, and 86 %, respectively. For CCP3.1, sensitivity was 78 %, specificity 93 %, PPV 89 %, NPV 86 %. Both assays demonstrated excellent agreement; positive percent agreement of 94 % and negative percent agreement of 99 %.ConclusionOur findings indicate comparable diagnostic accuracy between CCP3 and CCP3.1 assays in these clinical cohorts.

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AGBL3

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