Granulocyte function during prophylaxis with doxycycline.

J Belsheim; H Gnarpe; J Löfberg

doi:10.3109/inf.1979.11.issue-4.06

Home/Archive/PubMed

PubMed · 531522

Granulocyte function during prophylaxis with doxycycline.

J Belsheim·H Gnarpe·J Löfberg

View original source ↗Export metadata ↓

Abstract

The influence of doxycycline on granulocyte migration was investigated on patients undergoing fracture surgery. The granulocyte migration of the patients was depressed when doxycycline was administered. Scanning electron microscopy demonstrated a decreased granulocyte adherence to glass as well as a decrease in number of filopods per cell in the presence of doxycycline.

Explore related subjects

Cell Adhesion Chemotaxis, Leukocyte Doxycycline Granulocytes Humans Surgical Wound Infection Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

J Belsheim, H Gnarpe, J Löfberg. 1979. Granulocyte function during prophylaxis with doxycycline.. https://doi.org/10.3109/inf.1979.11.issue-4.06

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1992

Augmentation of retinoic acid-induced granulocytic differentiation in HL-60 leukemia cells by serine/threonine protein phosphatase inhibitors.

To evaluate the involvement of protein phosphatases (PP) in differentiation of human myelogenous leukemia HL-60 cells, we made use of potent inhibitors of PP1 and PP2A, calyculin-A (CAL-A) and okadaic acid (OKA). CAL-A and OKA could augment all-trans retinoic acid (ATRA)-induced granulocytic differentiation, whereas the differentiation toward macrophage lineage by 12-o-tetradecanoylphorbol acetate (TPA) was unchanged in the presence of CAL-A. CAL-A augmented the phosphorylation of 18K, 23K and 30K proteins induced by ATRA. The PP1 and PP2A were identified and were present mainly in the cytosol of HL-60 cells. These results suggest that either PP1 or PP2A or both may be involved in regulating granulocytic differentiation of HL-60 cells.

Cell Adhesion↗

PubMed1992

[Interleukin 4 increases lymphocytic adhesion to allogenic endothelium through a dependent protein kinase A].

Interleukin 4 and tumor necrosis factor alpha increase endothelial cell adhesiveness for lymphocytes by promoting adhesion molecules synthesis. We have shown that intracellular mechanisms, which transduce IL 4--but not TNF alpha--signal, involve a protein kinase A.

Cell Adhesion↗

PubMed1992

Cancer cell binding to E-selectin transfected human endothelia.

Human endothelial cells were transiently transfected with E-Selectin which enabled us to study tumor cell/endothelial interactions following engagement of E-Selectin without the added complications of metabolic stimulation, morphological changes, and/or up regulation of other adhesion molecules due to cytokine induction. Similar results were received from in vitro binding studies and FACS analyses on both Tumor Necrosis Factor-alpha activated and E-Selectin transfected endothelial cells. These data suggest that this methodology is appropriate for dissecting the individual activities of E-selectin while minimizing the participation of other adhesion molecules, thereby allowing us to develop a better understanding of the role of E-Selectin and endothelia in metastatic disease.

Cell Adhesion↗