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D R Garrod

Publications and source records attributed to D R Garrod.

At least 109 records · Page 6Linked to original sources
PubMed1975

Observations on the sorting-out of embryonic cells in monolayer culture.

Two problems are raised concerning the movement of cells during tissue-specific sorting-out of chick embryo cells in mixed aggregates. (i) A possible expectation from the hypothesis of 'contact inhibition' is that cells which are entirely surrounded by other cells in monolayer should be held stationary. Cells within solid aggregates, being totally surrounded by others, might also not be expected to move. How is it then that cell movement takes place within solid aggregates during sorting-out? (ii) Are the movements of cells within sorting aggregates 'passive', being driven by adhesive differentials or 'active', being merely guided by such differentials? In order to study these questions, sorting out experiments with chick embryonic limb bud mesenchyme and liver cells were carried out in monolayer culture, permitting direct observation of cell movements. Cell behavior was observed by time-lapse cinematography. Sorting-out of these cells in monolayer began before and continued after the cells had spread to confluency. During sorting, liver cells showed ruffing activity even when they appeared to be totally surrounded by other cells. Both cell types showed contact inhibition as judged by the criterion of monolayering, for they did not move over each other but remained attached to the substratum. Yet the cells in the confluent monolayer were not immobilized. Because of this, we suggest that the observed restraint against overlapping did not result from an inhibition of movement. Several considerations, detailed in the text, suggest that cell movement during sorting-out involve active locomotion. Previous work suggest that sorting-out configurations are determined by the relative intensities of intercellular adhesive strengths, the more cohesive of 2 cell populations tending to adopt the internal position. While limb bud cells form internal islands surrounded by liver cells in solid aggregates, the reverse was found to be the case in these monolayers. This suggests that, in the monolayer, limb bud cohesiveness is depressed relative to liver cell cohesiveness. This is consistent with the observation that the limb bud cells flattened themselves markedly against the substratum, significantly decreasing their area of mutual apposition.

Animals↗
PubMed1975

Cell locomotion within a contact-inhibited monolayer of chick embryonic liver parenchyma cells.

Using time-lapse filming, the relative movement of cells (nuclei) within a contact-inhibited monolayer of chick embryonic liver parenchyma cells has been studied. Two techniques were employed to determine the amount of relative cell movement during a culture period of 6 h. Firstly, the number of neighbours lost or gained by each nucleus was counted. Secondly, the relative distance moved by each nucleus in relation to other nucleus in the monolayer was measured. (The numerical results obtained from these analyses and details of the methods used are given in the text). A considerable amount of relative movement of nuclei within the monolayer was found during this period of culture. Although some gaps were occasionally seen between the cells in the monolayer, it was observed that cells able both to "ruffle" and to translocate when no gap was detectable; i.e. the cells appeared able to move while entirely surrounded by other cells. Because of this, we suggest that the monolayering of these epitheloid cells on a surface may be due to restriction of overlapping between them rather than to inhibition of movement by mutual contact. We argue that the term "contact inhibition of overlapping" relates to this behaviour better than the term "contact inhibition of movement".

Animals↗
PubMedDate not supplied

Dual role for Dictyostelium contact site B in phagocytosis and developmental size regulation.

Three cohesion molecules have been discovered in the slime mould Dictyostelium discoideum. Two of these molecules are involved in morphogenesis at the aggregation stage of the life cycle and thereafter, and may also provide an essential trigger for late gene expression. The third glycoprotein 126 (gp126) or contact site B, is present on axenically grown vegetative amoebae and persists to the aggregation stage where it is involved in the side-to-side cohesion of cells in aggregation streams. It is puzzling that vegetative amoebae should possess a cohesion molecule because their solitary habit does not necessitate cohesion. However, they do need to adhere to the substratum and adhesion of bacteria to the cells is a prerequisite for phagocytosis. Vogel et al. have proposed that the same receptor is involved in phagocytosis and cohesion. It has also been suggested that contact site B-mediated cohesion is a trigger for development. Using a specific antibody against gp126, we now show that contact site B is a phagocytosis receptor. Furthermore, contact site B is involved in regulating the size of aggregates formed during morphogenesis; it also seems to be involved in cell-substratum adhesion but is not a developmental trigger.

Cell Adhesion↗
PubMedDate not supplied

Cloning, sequence analysis and expression pattern of mouse desmocollin 2 (DSC2), a cadherin-like adhesion molecule.

Desmocollins are cadherin-like adhesion molecules of desmosomes. We have determined the full cDNA sequence of a murine desmocollin, the homologue of human and bovine type 2 desmocollins (DSC2), and studied its tissue distribution and expression in stratified epithelia. An 8.5 day mouse embryo cDNA library was screened yielding overlapping clones which encoded the mouse DSC2. This gene has an open reading frame of 2710 base pairs (bp) encoding a polypeptide of 902 amino acids (aa). The polypeptide comprises a signal peptide, a precursor peptide, and a mature protein of 766 aa having an extracellular domain of 549 aa, a single transmembrane domain and a cytoplasmic domain of 184 aa. Like other desmocollins, murine DSC2 has two products, Dsc2a and Dsc2b, produced by alternative splicing of a 46 bp exon which encodes 11 COOH-terminal aa followed by an in-frame stop codon. Inclusion of this exon forms Dsc2b which is 54 aa shorter than Dsc2a. Mouse Dsc2a shows 75.7% amino acid identity to human and 63.3% identity to bovine Dsc2a. The mouse desmocollin is also homologous to the cadherins; 32.2% to the most closely related typical cadherin, human N-cadherin. DSC2 is ubiquitously expressed in epithelial tissues and the heart of adult mice and from the blastocyst stage of development. In situ hybridization shows that the gene is most strongly expressed suprabasally in stratified epithelia, similar to the expression of bovine DSC2.

Amino Acid Sequence↗