In a population-based cohort, PORT use is associated with an increase in survival in patients with N2 nodal disease but not in patients with N1 and N0 nodal disease.

No abstract

Human polymorphonuclear neutrophils exhibit a low level of the microtubule-associated protein kinase (MAPK) activity. This enzymic activity is enhanced up to 3-fold upon cell stimulation with the human haematopoietic hormone granulocyte-macrophage colony-stimulating factor (GM-CSF). This is demonstrated both in whole-cell lysates and in DEAE-anion-exchange semi-purified fractions prepared from GM-CSF-stimulated neutrophils, by assaying the kinase activity against either myelin basic protein or a phosphoacceptor peptide that bears the specific phosphorylation site of the MAPK natural substrate. Similarly, phosphorylation of MAPK in tyrosine residues, as found in immunoblots using anti-phosphotyrosine antibodies, follows similar time- and dose-response curves as the kinase activation. Pretreatment of the cells with the tyrosine kinase inhibitor genistein abrogates the above-mentioned effect, whereas the phosphatase inhibitor okadaic acid enhances both the basal and the GM-CSF-stimulated kinase activities. Likewise, MAPK tyrosine phosphorylation is diminished in genistein-treated neutrophils, and enhanced in okadaic acid-treated cells. We conclude that MAPK activity is present in human neutrophils, and that it is stimulated by GM-CSF. This stimulation of the activity is most likely due to the phosphorylation of MAPK in tyrosine residues triggered upon binding of GM-CSF to its receptors.

Patients can experience successful lactation in the contralateral, untreated breast after breast-conserving therapy. In the treated breast, functional lactation is possible but is significantly diminished in the majority of patients.