Absence of the cotton dust/bract antigen in house dust,clean cotton fibers and cottonseed hulls and proteins

Aqueous extracts of cotton dust and cotton bract induced the formation of antibodies in rabbits. The antisera cross-reacted with both extracts as well as with extracts of stem, leaf, baled cotton, and gin trash. No reaction was obtained with extracts of cottonseed hulls, cottonseed proteins, noncontaminated cotton fibers, or house dust. None of the anitgens reacted with normal rabbit serum. One of the facilities of the Southern Region, Science and Education Administration, U.S. Department of Agriculture.     

Changes in lipid composition of germinating barley embryo

Barley seeds,Hordeum vulgare, var. Kenia, were dissected before and after 5 days of germination, to distinguish between the scutellum, the coleoptile half of the embryo and the coleorhiza half of the embryo. Total lipids were extracted from each fraction and analyzed by thin layer chromatography and gas liquid chromatography. In tissues from the coleoptile and coleorhiza halves of the embryo there was a concurrent disappearance of triglycerides with a marked increase of esterified sterols and esterified sterol glucosides. In the scutellum there was also a change in triglycerides, but the variations in contents of esterified sterols and esterified sterol glucosides were much smaller. Mono- and digalactolipids were virtually absent from embryonic tissue. The amounts of linoleic and linolenic acids in esterified sterol glucosides were increased after 5 days of germination in all the embryonic tissues, especially in the coleoptile half. In sterol esters, linoleic acid comprised nearly half of the total fatty acids, and the desaturation after 5 days of germination was much less pronounced.     

Peanut proteins as food supplements: A compositional study of selected Virginia and Spanish peanuts

Three peanut cultivars (Virginia, red-skinned, and white-skinned Spanish) were analyzed and compared as potential protein supplements for food uses. The seeds were solvent-extracted in the laboratory to yield defatted flours with 9–10% nitrogen contents. Protein isolates were prepared from the flours by subsequent extraction with dilute salt solutions buffered at pH 7.0. Various parameters were compared, such as total protein contents, soluble proteins, amino acid compositions of flours and protein isolates, free amino acids and free sugars of defatted flours, and certain trace minerals in flours and soluble proteins. The application of these results to the selection of certain types of peanuts for potential uses as protein supplements in food products is discussed. Presented in the Symposium, Oilseed Proteins, 66th Annual AOCS Meeting, Dallas, Texas, April 27–30, 1975.     

Lipolysis in castor seeds: A reinvestigation of the neutral lipase

Attempts to study the neutral lipase reported in germinating castor seeds and to compare this enzyme to the acid lipase of dormant seeds were unsuccessful because of the inability to repeat the work described earlier (1). Activity of the proposed neutral lipase could not be detected, nor could appearance of the enzyme be hastened or affected by treating the germinating seeds with gibberellic acid or Actinomycin-D. Possible explanations for the discrepancy between these findings and the early report are presented. So. Utiliz. Res. Dev. Div., ARS, USDA.     

Acid lipase of the castor bean

The acid lipase of the castor bean is present in the dormant seed. It is extracted from the fat pad obtained by centrifuging a macerate of the seed in pH 7.0 buffer containing cysteine and ethylene diaminetetraacetic acid. The pH optimum of the enzyme is 4.2; it is rather heat-stable, and is inhibited by mercurials and sulfhydryl reagents. Maximum hydrolysis of saturated triglycerides occurs with fatty acids of chain length C₄ to C₈; unsaturated C₁₈ triglycerides are hydrolyzed at a slightly lower rate. This lipase is a three-component system consisting of the apoenzyme, a lipid cofactor (a cyclic tetramer of ricinoleic acid), and a protein activator (a small, heat-stable glycoprotein which appears to be related to some of the castor allergens). Maximum lipolysis requires all three components. Lipase activity is associated with the spherosomes, the subcellular site of oil storage in the endosperm. Presented at the AOCS-AACC Joint Meeting, Washington, D.C., April 1968. So. Utiliz. Res. Dev. Div., ARS, USDA.     

Comparison of transsynaptic viral labeling of central nervous system structures from the uterine horn in virgin, pregnant, and lactating rats

Using the transneuronal viral tracing method, the central nervous system (CNS) connections of the uterine horn were studied in virgin, pregnant, and in lactating rats. The frequency of viral labeling in the brain and the distribution of virus-infected neurons from the uterine horn were compared among groups. There was a marked difference in the frequency of viral labeling in the brain stem. In virgin rats more than half of the brain stems (5 out of 9) were labeled. In contrast, in pregnant animals viral-labeled neurons were detected in only a few cases (3 out of 16) and almost each brain stem of the lactating group was labeled (12 out of 13). A similar, less marked difference was observed in the hypothalamus. The pattern of distribution of infected neurons was similar in each group. In the brain stem, the nucleus of the solitary tract, dorsal motor nucleus of the vagus, area postrema, gigantocellular and paragigantocellular nucleus, ventrolateral medulla, A5 cell group, and caudal raphe nuclei were the most frequently labeled structures. In the diencephalon, viral-infected neurons were detected primarily in the hypothalamic paraventricular nucleus. The telencephalon was devoid of infected cells. Data suggest that the CNS control of the uterine horn varies depending on reproductive status. The low frequency of brain labeling in pregnant rats may be related to the almost complete lack of sympathetic fibers in the uterus prior to parturition and the very high frequency of labeling in lactating animals to the postpartum hyperinnervation of the uterus.     

Blocking the PCNA/NKp44 Checkpoint to Stimulate NK Cell Responses to Multiple Myeloma

Simple SummaryMembrane-associated PCNA is expressed on the surface of human MM cell lines and primary MM cells. Mab 14-25-9 interacts with membrane-associated PCNA and blocks its binding to NK-expressed NKp44, thus activating NK function. We showed that mAb 14-25-9 can serve as an immune checkpoint blocker, enhancing the function of NK cells on target human MM cell lines and primary cells.AbstractMultiple Myeloma (MM) is a devastating malignancy that evades immune destruction using multiple mechanisms. The NKp44 receptor interacts with PCNA (Proliferating Cell Nuclear Antigen) and may inhibit NK cells’ functions. Here we studied in vitro the expression and function of PCNA on MM cells. First, we show that PCNA is present on the cell membrane of five out of six MM cell lines, using novel anti-PCNA mAb developed to recognize membrane-associated PCNA. Next, we stained primary bone marrow (BM) mononuclear cells from MM patients and showed significant staining of membrane-associated PCNA in the fraction of CD38⁺CD138⁺ BM cells that contain the MM cells. Importantly, blocking of the membrane PCNA on MM cells enhanced the activity of NK cells, including IFN-γ-secretion and degranulation. Our results highlight the possible blocking of the NKp44-PCNA immune checkpoint by the mAb 14-25-9 antibody to enhance NK cell responses against MM, providing a novel treatment option.