Activity-based protein profiling guided identification of urine proteinase 3 activity in subclinical rejection after renal transplantation.

ABHD14B/CCG1-interacting factor B ABPP/activity-based protein profiling LTF/LactotransferrinPR3 Neurotrypsin/PRSS12 PR3/PRTN3/myeloblastin Renal transplant Serine hydrolase Urine

Journal

Clinical proteomics
ISSN: 1542-6416
Titre abrégé: Clin Proteomics
Pays: England
ID NLM: 101184586

Informations de publication

Date de publication:
2020
Historique:
received: 21 01 2020
accepted: 19 05 2020
entrez: 19 6 2020
pubmed: 19 6 2020
medline: 19 6 2020
Statut: epublish

Résumé

The pathophysiology of subclinical versus clinical rejection remains incompletely understood given their equivalent histological severity but discordant graft function. The goal was to evaluate serine hydrolase enzyme activities to explore if there were any underlying differences in activities during subclinical versus clinical rejection. Serine hydrolase activity-based protein profiling (ABPP) was performed on the urines of a case control cohort of patients with biopsy confirmed subclinical or clinical transplant rejection. In-gel analysis and affinity purification with mass spectrometry were used to demonstrate and identify active serine hydrolase activity. An assay for proteinase 3 (PR3/PRTN3) was adapted for the quantitation of activity in urine. In-gel ABPP profiles suggested increased intensity and diversity of serine hydrolase activities in urine from patients undergoing subclinical versus clinical rejection. Serine hydrolases (n = 30) were identified by mass spectrometry in subclinical and clinical rejection patients with 4 non-overlapping candidates between the two groups (i.e. ABHD14B, LTF, PR3/PRTN3 and PRSS12). Western blot and the use of a specific inhibitor confirmed the presence of active PR3/PRTN3 in samples from patients undergoing subclinical rejection. Analysis of samples from normal donors or from several serial post-transplant urines indicated that although PR3/PRTN3 activity may be highly associated with low-grade subclinical inflammation, the enzyme activity was not restricted to this patient group. There appear to be limited qualitative and quantitative differences in serine hydrolase activity in patients with subclinical versus clinical renal transplant rejection. The majority of enzymes identified were present in samples from both groups implying that in-gel quantitative differences may largely relate to the activity status of shared enzymes. However qualitative compositional differences were also observed indicating differential activities. The PR3/PRTN3 analyses indicate that the activity status of urine in transplant patients is dynamic possibly reflecting changes in the underlying processes in the transplant. These data suggest that differential serine hydrolase pathways may be active in subclinical versus clinical rejection which requires further exploration in larger patient cohorts. Although this study focused on PR3/PRTN3, this does not preclude the possibility that other enzymes may play critical roles in the rejection process.

Sections du résumé

BACKGROUND BACKGROUND
The pathophysiology of subclinical versus clinical rejection remains incompletely understood given their equivalent histological severity but discordant graft function. The goal was to evaluate serine hydrolase enzyme activities to explore if there were any underlying differences in activities during subclinical versus clinical rejection.
METHODS METHODS
Serine hydrolase activity-based protein profiling (ABPP) was performed on the urines of a case control cohort of patients with biopsy confirmed subclinical or clinical transplant rejection. In-gel analysis and affinity purification with mass spectrometry were used to demonstrate and identify active serine hydrolase activity. An assay for proteinase 3 (PR3/PRTN3) was adapted for the quantitation of activity in urine.
RESULTS RESULTS
In-gel ABPP profiles suggested increased intensity and diversity of serine hydrolase activities in urine from patients undergoing subclinical versus clinical rejection. Serine hydrolases (n = 30) were identified by mass spectrometry in subclinical and clinical rejection patients with 4 non-overlapping candidates between the two groups (i.e. ABHD14B, LTF, PR3/PRTN3 and PRSS12). Western blot and the use of a specific inhibitor confirmed the presence of active PR3/PRTN3 in samples from patients undergoing subclinical rejection. Analysis of samples from normal donors or from several serial post-transplant urines indicated that although PR3/PRTN3 activity may be highly associated with low-grade subclinical inflammation, the enzyme activity was not restricted to this patient group.
CONCLUSIONS CONCLUSIONS
There appear to be limited qualitative and quantitative differences in serine hydrolase activity in patients with subclinical versus clinical renal transplant rejection. The majority of enzymes identified were present in samples from both groups implying that in-gel quantitative differences may largely relate to the activity status of shared enzymes. However qualitative compositional differences were also observed indicating differential activities. The PR3/PRTN3 analyses indicate that the activity status of urine in transplant patients is dynamic possibly reflecting changes in the underlying processes in the transplant. These data suggest that differential serine hydrolase pathways may be active in subclinical versus clinical rejection which requires further exploration in larger patient cohorts. Although this study focused on PR3/PRTN3, this does not preclude the possibility that other enzymes may play critical roles in the rejection process.

Identifiants

pubmed: 32549867
doi: 10.1186/s12014-020-09284-9
pii: 9284
pmc: PMC7296916
doi:

Types de publication

Journal Article

Langues

eng

Pagination

23

Informations de copyright

© The Author(s) 2020.

Déclaration de conflit d'intérêts

Competing interestsThe authors declare that they have no competing interests.

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Auteurs

Mario Navarrete (M)

Manitoba Centre for Proteomics and Systems Biology, 799 John Buhler Research Centre, 715 McDermot Ave., Winnipeg, MB R3E3P4 Canada.

Brice Korkmaz (B)

INSERM, UMR 1100, "Centre d'Etude des Pathologies Respiratoires", Université de Tours, 37032 Tours, France.

Carla Guarino (C)

INSERM, UMR 1100, "Centre d'Etude des Pathologies Respiratoires", Université de Tours, 37032 Tours, France.

Adam Lesner (A)

Faculty of Chemistry, University of Gdansk, 80-308 Gdansk, Poland.

Ying Lao (Y)

Manitoba Centre for Proteomics and Systems Biology, 799 John Buhler Research Centre, 715 McDermot Ave., Winnipeg, MB R3E3P4 Canada.

Julie Ho (J)

Manitoba Centre for Proteomics and Systems Biology, 799 John Buhler Research Centre, 715 McDermot Ave., Winnipeg, MB R3E3P4 Canada.
Section Biomedical Proteomics, Dept. Internal Medicine, University of Manitoba, Winnipeg, MB Canada.
Section of Nephrology, Dept. Internal Medicine, University of Manitoba, Winnipeg, MB Canada.
Dept. Immunology, University of Manitoba, Winnipeg, MB Canada.

Peter Nickerson (P)

Manitoba Centre for Proteomics and Systems Biology, 799 John Buhler Research Centre, 715 McDermot Ave., Winnipeg, MB R3E3P4 Canada.
Section Biomedical Proteomics, Dept. Internal Medicine, University of Manitoba, Winnipeg, MB Canada.
Section of Nephrology, Dept. Internal Medicine, University of Manitoba, Winnipeg, MB Canada.
Dept. Immunology, University of Manitoba, Winnipeg, MB Canada.

John A Wilkins (JA)

Manitoba Centre for Proteomics and Systems Biology, 799 John Buhler Research Centre, 715 McDermot Ave., Winnipeg, MB R3E3P4 Canada.
Section Biomedical Proteomics, Dept. Internal Medicine, University of Manitoba, Winnipeg, MB Canada.

Classifications MeSH