Diss. (sammanfattning) Stockholm : Karol. inst., 2001. / Härtill 5 uppsatser.

Thesis (Ph. D.)--University of Washington, 1990. / Vita. Includes bibliographical references (leaves [260]-274).

Thesis (Ph. D.)--University of Wisconsin--Madison, 1962. / Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references.

Thesis (Ph. D.)--Virginia Commonwealth University, 2009. / Prepared for: Dept. of Microbiology and Immunology. Bibliography: leaves 69-85. Also available online via the Internet.

Thesis (Ph.D.)--Kent State University, 2008. / Title from PDF t.p. (viewed May 26, 2009). Advisor: Douglas W. Kline. Keywords: oocyte, egg, ovum, PADI6, PAD6, 14-3-3, peptidylarginine deiminase, phosphorylation, mouse, oocyte maturation, gamete biology. Includes bibliographical references (p. 91-97).

Thesis (Ph. D.)--University of Lund, 1995. / Published dissertation.

Thesis (Ph. D.)--University of Lund, 1995. / Published dissertation.

No description available.

Various alkaline proteases derived from skeletal muscle have been described by a number of researchers and have been purified to varying degrees. Such alkaline proteases may play an important role in the metabolism of myofibrillar and other muscle proteins and as such deserve to be fully characterised. In this study, a major myofibrillar alkaline protease was purified from rat skeletal muscle. The enzyme degraded both denatured casein and azocasein and had a pH optimum of 9,0. The molecular mass was 32 250 ± 650. The presence of a second, minor alkaline protease was demonstrated using three different separation techniques as well as by inhibitor studies. The major protease was insensitive to inhibition by pepstatin and leupeptin, whilst 90 % of the activity was expressed in the presence of 2 mM EGTA. A moderate degree of inhibition was observed in the presence of soybean trypsin inhibitor and the protease was markedly sensitive to chymostatin. A similar alkaline protease was partially purified from rat cardiac muscle using the same purification procedure. Incubation of washed myofibrils in the presence of sodium pyrophosphate released a factor into the supernatant, the removal of which facilitated the separation of myofibrillar alkaline protease from the myofibrils. The factor appeared to be necessary for binding of the alkaline protease to the myofibrillar proteins but its removal did not disrupt the binding of proteolytic activity already attached to the myofibrillar proteins. An inhibitor of myofibrillar alkaline protease was demonstrated which is, in principle, capable of playing an important regulatory role in controlling the activity of these enzymes and thereby of myofibrillar protein catabolism.

Indiana University-Purdue University Indianapolis (IUPUI) / Rap1a and Rap1b are two closely related members of the Ras family of small GTPases. Despite their high sequence similarity, the two proteins serve non-redundant functions in cells and organs. Rap1a plays critical roles during mouse development, and both Rap1a and Rap1b are required for angiogenesis. In glioblastoma cells, however, Rap1b plays a more unique role in tumor cell invasion. Loss of rap1a in mice resulted in 40% embryonic lethality, and caused cardiac defects in mouse embryos and cardiac hypertrophy in adult mice. These phenotypes, distinct from those of the rap1b knockout mice, suggest differential roles of the two GTPases during mouse development. Angiogenesis, the formation of new blood vessels by endothelial cells, is impaired by the loss of rap1. Blood vessel growth into FGF2-containing Matrigel plugs was absent from rap1a-/- mice and aortic rings derived from rap1a-/- mice failed to sprout primitive endothelial tubes in response to FGF2 when embedded in Matrigel. Knocking down of either rap1a or rap1b in human micro-vascular endothelial cells (HMVECs) confirmed that Rap1 plays key roles in endothelial cell function. The knockdown of rap1a or 1b resulted in decreased adhesion to extracellular matrices and impaired cell migration. Rap1 deficient endothelial cells failed to form 3-D tubular structures when plated on Matrigel in vitro. The activation of ERK, p38, and Rac, important signaling molecules in angiogenesis, were all reduced in response to FGF2 when either Rap1 protein was depleted. In U373 human glioblastoma multiforme cells, depletion of rap1b, but not rap1a drastically reduced tumor cell invasion by decreasing the activity of secreted matrix metalloproteinase 2 (MMP2). The adhesion of cells to the extracellular matrices collagen or fibronectin, but not to vitronectin, was decreased upon rap1b depletion. However, a mild increase in proliferation associated with elevation in ERK1/2, p38, Akt and ribosomal S6 protein activation was observed in cells depleted of either rap1a or rap1b. When an MEK1/2 inhibitor U0126 was used, the phosphorylation of p38, Akt and S6 were decreased, however, to various levels, suggesting complex regulatory pathways mediate Rap1 action in glioblastoma cells.