A dual effector theory of growth-hormone action

Abstract. Growth hormone increases tissue formation by acting both directly and indirectly on target cells. The direct action promotes the differentiation of precursor cells; this has been demonstrated for two mesenchymal cell types. Insulin-like growth factor I (IGF-I) is not able to substitute for growth hormone in promoting this differentiation, but it is proposed that its mitogenic action selectively promotes cell multiplication in young differentiated clones. As tissue growth results from both the creation of new differentiated cells and their subsequent clonal expansion, both effectors increase tissue growth, but by different means.     

Visualization of individual DNA molecules in solution by light microscopy: DAPI staining method

A method was developed to visualize individual DNA molecules in solution under a fluorescent microscope connected to a highly sensitive video camera. DNA stained with a fluorescent dye, DAPI, revealed thin extended filaments, thicker filaments and rapidly transforming folded structures dependent upon the solution conditions. Structural transitions were observed and recorded as video images. Our observations indicated the possibility that DNA has the ability of supercoiling itself. This DAPI staining method will have wide possible application in the study of DNA and chromatin.     

Some Improvements in the Preparation of Fresh Frozen Sections

For the histochemical demonstration of sensitive enzymes it is necessary to use fresh unfixed tissue sections. With the following procedure one can constantly obtain such sections 10-20μ thick with relative ease. Schanze's sliding microtome is employed. The microtome knife is deeply cooled by placing blocks of dry ice on its surface, and is provided with a device for preventing the sections from rolling up. The microtome is operated in an ordinary refrigerator maintained at a temperature of 0-3°C. For this purpose, the door of the refrigerator is replaced by a wooden door provided with a glass window, gloved arm holes, and a small door.     

Neutral alpha-glucosidase in granule fractions from guinea pig polymorphonuclear leukocytes: enzymic characterization and comparative studies with monoclonal antibodies

Neutral alpha-glucosidase was partially purified from granular fractions isolated from guinea pig polymorphonuclear leukocytes (PMNL). The native enzyme had a high molecular weight, about 417,000, with a subunit of 43,000. The purified enzyme hydrolysed 4-methylumbelliferyl alpha-glucoside and maltose, but not isomaltose, trehalose, and glycogen. The enzyme was strongly inhibited by bromoconduritol and castanospermine, but only slightly by turanose. Monoclonal antibodies which can bind specifically to the enzyme were prepared by immunizing mice with the partially purified enzyme. Hybridomas producing the monoclonal antibodies were selected by an enzyme-linked immunosorbent assay. The seven monoclonal antibodies were found to react with the enzyme from PMNL, but not with the glycoprotein-processing alpha-glucosidase isolated from liver microsomes nor with the macrophage enzyme. The results indicated that PMNL contain a particulate neutral alpha-glucosidase enzymologically and immunologically distinct from other alpha-glucosidases.