Calcium-binding proteins are altered in the cerebellum in schizophrenia.

Francisco Vidal-Domènech, Gemma Riquelme, Raquel Pinacho, Ricard Rodriguez-Mias, América Vera, Alfonso Monje, Isidre Ferrer, Luis F Callado, J Javier Meana, Judit Villén, Belén Ramos

Journal: PloS one 2020;15(7):e0230400

PMID: 32639965

Abstract

Alterations in the cortico-cerebellar-thalamic-cortical circuit might underlie the diversity of symptoms in schizophrenia. However, molecular changes in cerebellar neuronal circuits, part of this network, have not yet been fully determined. Using LC-MS/MS, we screened altered candidates in pooled grey matter of cerebellum from schizophrenia subjects who committed suicide (n = 4) and healthy individuals (n = 4). Further validation by immunoblotting of three selected candidates was performed in two cohorts comprising schizophrenia (n = 20), non-schizophrenia suicide (n = 6) and healthy controls (n = 21). We found 99 significantly altered proteins, 31 of them previously reported in other brain areas by proteomic studies. Transport function was the most enriched category, while cell communication was the most prevalent function. For validation, we selected the vacuolar proton pump subunit 1 (VPP1), from transport, and two EF-hand calcium-binding proteins, calmodulin and parvalbumin, from cell communication. All candidates showed significant changes in schizophrenia (n = 7) compared to controls (n = 7). VPP1 was altered in the non-schizophrenia suicide group and increased levels of parvalbumin were linked to antipsychotics. Further validation in an independent cohort of non-suicidal chronic schizophrenia subjects (n = 13) and non-psychiatric controls (n = 14) showed that parvalbumin was increased, while calmodulin was decreased in schizophrenia. Our findings provide evidence of calcium-binding protein dysregulation in the cerebellum in schizophrenia, suggesting an impact on normal calcium-dependent synaptic functioning of cerebellar circuits. Our study also links VPP1 to suicide behaviours, suggesting a possible impairment in vesicle neurotransmitter refilling and release in these phenotypes.

Address: Psiquiatria Molecular, Institut de Recerca Sant Joan de Déu, Esplugues de Llobregat, Spain.; Dept. de Bioquímica i Biologia Molecular, Facultat de Medicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.; Psiquiatria Molecular, Institut de Recerca Sant Joan de Déu, Esplugues de Llobregat, Spain.; Department of Genome Sciences, School of Medicine, University of Washington, Seattle, Washington, United States of America.; Parc Sanitari Sant Joan de Déu, Sant Boi de Llobregat, Spain.; Departamento de Patologia y Terapeutica Experimental, Universidad de Barcelona, Senior consultant Servicio Anatomia Patológica, Hospital Universitario de Bellvitge-IDIBELL, CIBERNED, Hospital de Llobregat, Barcelona, Spain.; Department of Pharmacology, University of the Basque Country UPV/EHU, Leioa, Bizkaia, Spain.; Centro de Investigación Biomédica en Red de Salud Mental, Madrid, CIBERSAM, Spain.; Biocruces Bizkaia Health Research Institute, Barakaldo, Spain.; Psiquiatria Molecular, Institut de Recerca Sant Joan de Déu, Esplugues de Llobregat, Spain.; Dept. de Bioquímica i Biologia Molecular, Facultat de Medicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.; Parc Sanitari Sant Joan de Déu, Sant Boi de Llobregat, Spain.; Centro de Investigación Biomédica en Red de Salud Mental, Madrid, CIBERSAM, Spain.
Bant logo

© Copyright 2026, Nutrition Evidence

NED wishes to thank the following organisations for their support:

We use cookies to improve your experience and analyze site traffic with Google Analytics. By continuing to use our site, you agree to our use of cookies. Learn more.