Massive antepartum haemorrhage at insertion of Foley balloon catheter for induction of labour.

Induction of labour using a balloon catheter is common practice throughout the world, often used in high-risk pregnancies due to the improved safety profile for the fetus compared with pharmacological methods. This report outlines the case of a 2500 mL antepartum haemorrhage on placement of a Foley catheter through the cervix at a secondary obstetric unit in New Zealand. An emergency caesarean section was carried out 20 min after the bleeding onset. No obvious cause for the bleeding was identified at caesarean. The mother required a blood transfusion, but otherwise, did well clinically; the infant required resuscitation at birth and went on to suffer a left middle cerebral artery stroke. At 6 months, he is assumed to have recovered with no long-term sequelae. A literature review has highlighted this was an unprecedented event. We hope to raise awareness of this rare catastrophic adverse outcome given the prevalence of balloon catheter induction.

Dephosphorylation of caseins in milk protein concentrate alters their interactions with sodium hexametaphosphate.

This study investigated the effects of dephosphorylation and sodium hexametaphosphate (SHMP) salt addition on the viscosity of milk protein concentrate (MPC) solutions. Dephosphorylation (DP) of casein was performed using bovine alkaline phosphatase. Nuclear magnetic resonance (NMR) spectra showed that dephosphorylation depleted the casein-bound phosphate region (CNP). SHMP addition (5 mM) had no impact on the 31P NMR spectra of DP-MPC; addition of 5 mM SHMP to control MPC (C-MPC) resulted in a shift in peaks associated with the CNP region, possibly caused by SHMP sequestering calcium, leading to swelling of micelles. DP-MPC exhibited a lower viscosity compared to C-MPC, with SHMP addition at 12.5 and 25 mM causing gelation of C-MPC and DP-MPC solutions. This work confirmed the role that phosphate residues have in maintaining micelle structural stability and provides new insights into controlling viscosity of MPC solutions.

Food protein hydrolysates as a source of dipeptidyl peptidase IV inhibitory peptides for the management of type 2 diabetes.

The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure-activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM.