TH van Kuppevelt

Radboud University Nijmegen

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JH Veerkamp

Radboud University Nijmegen

Elly M. M. Versteeg

Radboud University Nijmegen

HA Goedhart

Damien Habert

Inserm

Mohand Ouidir Ouidja

Laboratoire de Recherche sur la Croissance Cellulaire, la Réparation et la Régénération Tissulaires

C.H. Veerkamp

Radboud University Nijmegen

Chris H.A. van de Lest

Utrecht University

Gilles Carpentier

Laboratoire de Recherche sur la Croissance Cellulaire, la Réparation et la Régénération Tissulaires

Carine Dalle

Centre National de la Recherche Scientifique

RW Kranen

Cooperative Institutions

Laboratoire de Recherche sur la Croissance Cellulaire, la Réparation et la Régénération Tissulaires

Centre National de la Recherche Scientifique

Inserm

Université Paris-Est Créteil

Université Paris Cité

Radboud University Nijmegen

Assistance Publique – Hôpitaux de Paris

Sorbonne Université

Paris-Est Sup

Institut du Cerveau

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3-O-sulfated heparan sulfate interactors target synaptic adhesion molecules from neonatal mouse brain and inhibit neural activity and synaptogenesis in vitro

Scientific Reports (2020)

Auriane Maïza Nazha Sidahmed‐Adrar Patrick P. Michel Gilles Carpentier Damien Habert

Abstract Heparan sulfate (HS) chains, covalently linked to heparan sulfate proteoglycans (HSPG), promote synaptic development and functions by connecting various synaptic adhesion proteins (AP). HS binding to AP could vary according to modifications of HS chains by different sulfotransferases. 3- O -sulfotransferases (Hs3sts) produce rare 3- O -sulfated HSs (3S-HSs), of poorly known functions in the nervous system. Here, we showed that a peptide known to block herpes simplex virus by interfering with 3S-HSs in vitro and in vivo (i.e. G2 peptide), specifically inhibited neural activity, reduced evoked glutamate release, and impaired synaptic assembly in hippocampal cell cultures. A role for 3S-HSs in promoting synaptic assembly and neural activity is consistent with the synaptic interactome of G2 peptide, and with the detection of Hs3sts and their products in synapses of cultured neurons and in synaptosomes prepared from developing brains. Our study suggests that 3S-HSs acting as receptors for herpesviruses might be important regulators of neuronal and synaptic development in vertebrates.

Synaptogenesis

10.1038/s41598-020-76030-4

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Digestion of proteoglycans in porcine pancreatic elastase-induced emphysema in rats

European Respiratory Journal (1995)

Chris H.A. van de Lest Elly M. M. Versteeg JH Veerkamp TH van Kuppevelt

Pulmonary emphysema was induced in rats by a single intratracheal instillation of pancreatic elastase. The short-term effects of elastase instillation on basement membrane components were evaluated using immunohistochemical and biochemical methods. Lung alveoli showed a decrease in heparan sulphate proteoglycan content (especially of its heparan sulphate chains) 3 h to 7 days after induction. Type IV collagen, laminin and fibronectin were not affected. The glycosaminoglycan content of the lung was decreased during the first 3 days after induction, while the glycosaminoglycan concentration in urine was increased during the first 4 days by an increase of heparan sulphate and dermatan sulphate. The increase in urinary glycosaminoglycan content was positively correlated with the extent of emphysema developed after 40 days. We conclude that proteoglycans are target molecules for elastase, and may be involved in the pathogenesis of emphysema.

Pancreatic elastase

Pathogenesis

Type IV collagen

Dermatan sulfate

10.1183/09031936.95.08020238

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Hemoglobin and myoglobin content in muscles of broiler chickens

Poultry Science (1999)

RW Kranen TH van Kuppevelt HA Goedhart C.H. Veerkamp E. Lambooy

The two main heme proteins, hemoglobin and myoglobin, are important factors determining meat quality aspects such as color and hemorrhage. The extent of hemorrhage in muscle tissue can probably be determined by measuring the hemoglobin content. The objective of this study was twofold: 1) to develop a specific and reproducible method to quantify the hemoglobin and myoglobin content in muscle tissue of broiler chickens, and 2) to study the effect of hemorrhage on the hemoglobin content in muscle tissue. We tested several methods to determine the total heme, hemoglobin, and myoglobin content in broiler chicken muscles on their specificity, sensitivity, and reproducibility. Methods based on immunological techniques appeared to be very specific and sensitive. The results obtained applying these methods on muscle tissue extracts were, however, not reproducible due to concentration effects. A combination of spectrophotometric analysis of the total heme protein concentration and measurement of the myoglobin concentration, applying size exclusion chromatography, proved to be a reliable and reproducible method to determine the hemoglobin and myoglobin content in chicken muscles. The total heme, hemoglobin, and myoglobin contents were related to muscle type. Extensive hemorrhage increased the hemoglobin content.

Hemeprotein

10.1093/ps/78.3.467

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Citations (105)