Shift in Circulating Serum Protein Fraction (SPF) Levels of Pregnant Jennies and Nutritional Related Aspects at Early-, Mid- and Late Gestation

A viable tool for the monitoring of the systemic condition of the pregnant jenny may be the determination of serum protein fraction (SPF) levels, including metabolic profiling. Tissue development and composition of the growing fetus requires the mother to provide adequate nutrients to its body parts and organs. In this regard, body fluid distribution and strategic molecule transportation can be screened using SPF electropherograms and analysis of intermediate metabolites. The nutritional and health status of 12 jennies (age: 5–8 years; BW at the start: 135–138 kg; Body Condition Score, BCS [1 to 5 points] = 2.25–2.50; 4th month of gestation) were monitored throughout gestation (approximate gestation period 350–356 d). All animals were pasture-fed and were offered hay ad libitum. Individual blood samples were collected within the 4th, 7th, and 10th month following conception (ultrasound scanning). Serum biochemistry, in particular, the analysis of 6 fractions of serum proteins was carried out. The significant decrease in circulating albumin in jennies from mid- to late-gestation (p < 0.001) suggests a considerable role of dietary amino acids in the synthesis of protein for fetal tissue formation as well as body fluid distribution and blood pressure control of the jenny in those stages. Moreover, α1-globulin decreased significantly in late gestation (p < 0.047), corresponding to major organ development in the terminal fetus and supported by lipid transportation in the bloodstream of the jenny. Similarly, α2-globulin decreased in late gestation (p < 0.054) as haptoglobin, an important component for the transport of free circulating hemoglobin, is likely used for fetal synthesis. Mid-gestation, appears to be a crucial moment for adequate dietary nutrient supplementation in order to prevent homeostasis perturbation of jennies, as observed in this trial.

The Presence of M Protein Is Strongly Associated with Very Poor Prognosis in Patients with Extranodal Diffuse Large B-Cell Lymphoma

Introduction Several studies concerning extranodal diffuse large B-cell lymphoma (DLBCL) have been reported sporadically. However, no new, valuable prognostic factors have been reported since several risk factors, such as a high international prognostic index (IPI) score, elevated lactate dehydrogenase (LDH) level, poor Eastern Cooperative Oncology Group (ECOG) performance status (PS), advanced stage, and extranodal sites ≥2, were identified. Methods To identify new and valuable prognostic factors, we reviewed the medical records of patients with nodal and extranodal DLBCL who were newly diagnosed at the Cancer Institute Hospital of the Japanese Foundation for Cancer Research from February 2005 to September 2014, and retrospectively analyzed the data of a total of 463 consecutive DLBCL patients. The cases were nodal DLBCL in 237 patients and extranodal DLBCL in 226 patients. We investigated the relationships between overall survival (OS), progression-free survival (PFS), and age, gender, LDH level, beta-2 microglobulin level (b2MG), performance status (PS), stage, extranodal sites ≥2, Ki-67 index, and M protein in serum protein fraction electrophoresis at diagnosis. Univariate and multivariate analyses of estimated risk factors for OS and PFS in extranodal DLBCL patients were performed using the log-rank test and Cox proportional hazard regression analysis. Results In patients with extranodal DLBCL, the median age was 67 years (range, 20-89 years). The median follow-up was 41 months (range, 1-115 months). A serum electrophoresis study detected M protein in 7 patients (3.1%). To adjust the impact of age, gender, LDH level, b2MG, PS, stage, extranodal sites ≥2, Ki-67 index, and the presence of M protein in serum protein fraction electrophoresis at diagnosis for other significant factors for OS, we identified the following risk factors in extranodal DLBCL by univariate analysis: elevated LDH level, elevated b2MG level, stage ≥3, extranodal sites ≥2, and the presence of M protein. Then, we performed multivariate analyses by using all of these factors in the Cox proportional hazard model. M protein (HR 6.78, 95% CI 2.19-20.96, P<0.001) and extranodal sites ≥2 (HR 3.71, 95% CI 1.77-7.80, P<0.001) were identified as independent significant prognostic factors for OS in extranodal DLBCL. Furthermore, we also identified M protein (HR 3.81, 95% CI 1.25-11.60, P=0.019) and extranodal sites ≥2 (HR 2.98, 95% CI 1.45-6.14, P=0.003) as independent significant prognostic factors for PFS by multivariate analysis. Four out of seven patients with M protein died due to lymphoma progression. Median overall survival in patients with extranodal DLBCL with M protein was 12 months (range, 2-114 months) compared with 44 months without M protein (range, 1-115 months, P=0.0038). On the other hand, in patients with nodal DLBCL, M protein (n=10) was not significantly associated with poor OS and PFS. Conclusions These results suggest that the presence of M protein in serum protein fraction electrophoresis is significantly associated with very poor OS and PFS in patients with extranodal DLBCL, but not nodal DLBCL. Extranodal DLBCL with M protein is a rare and very poor prognostic subset of DLBCL. Figure 1. Figure 1. Disclosures Yokoyama: Chugai Pharmaceutical CO., LTD.: Consultancy. Mishima:Chugai Pharmaceutical CO., LTD.: Consultancy. Nishimura:Chugai Pharmaceutical CO., LTD.: Consultancy. Hatake:Chugai Pharmaceutical CO., LTD.: Other: lecture speaking.

Protocol for purification of a rat blood serum protein fraction enriched in gamma-butyrobetaine esterase activity

Protocol for purification of a rat blood serum protein fraction enriched in gamma-butyrobetaine esterase activity Although described some time ago, gamma-butyrobetaine esters and related compounds have not gained much attention from researchers, and their physiological function remains obscure. Formerly we detected GBB-esterase enzymatic activity in rat blood serum. The aim of the present work was to develop a protocol that would enable purification of the protein fraction enriched in GBB esterase activity from rat blood serum. Chromatography on DEAE Sepharose at pH 4.2 enabled to purify a protein fraction enriched in enzymatic activity, but represented by numerous polypeptides. Following separation of this fraction by means of chromatography on DEAE Sepharose at pH 6.5 or heparin Sepharose chromatography at pH 7.0 did not lead to significant decrease of polypeptide number. When the above fraction was further fractionated by means of DEAE Sepharose chromatography at pH 7.4 or Bio Gel P150 chromatography the enzymatic activity was lost. Combination of DEAE Sepharose at pH 4.2 and affinity chromatography with procainamide appears to be the most suitable approach.