{"title":"Developmental strategies of the angiosperm pollen: a biochemical perspective","authors":"V. Raghavan","doi":"10.1016/0045-6039(87)90476-3","DOIUrl":"10.1016/0045-6039(87)90476-3","url":null,"abstract":"<div><p>The current state of our knowledge of the biochemistry and biochemical cytology of normal pollen development and embryogenic transformation of pollen grains of cultured anthers of angiosperms is reviewed. Recent research shows that normal pollen development is characterized by gene activity for the synthesis of specific mRNAs associated with the gametophytic program. As a result of the trauma of excision and culture of anthers in a mineral salt medium, a small number of the enclosed pollen grains probably synthesize new mRNAs which code for the proteins involved in embryogenic divisions. Since these conclusions are based on the study of a small number of species, the need for sustained investigations on the molecular biology of pollen developmental transformations is emphasized.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 4","pages":"Pages 213-226"},"PeriodicalIF":0.0,"publicationDate":"1987-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90476-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14432865","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Giovanni Bernardini, Marco Ferraguti, Roberto Stipani
{"title":"Fertilization induces endocytosis in Xenopus eggs","authors":"Giovanni Bernardini, Marco Ferraguti, Roberto Stipani","doi":"10.1016/0045-6039(87)90480-5","DOIUrl":"10.1016/0045-6039(87)90480-5","url":null,"abstract":"<div><p>Fertilization-induced endocytosis in <em>Xenopus</em> eggs was shown by direct visualization of fluorescent dye in semithin sections. The eggs were incubated in a medium containing 0.1% Lucifer yellow CH for 20 min before, during and after fertilization and then fixed at different times after fertilization. The eggs incubated during or immediately after fertilization contained fluorescent vesicles in the cortex. These vesicles were mainly distributed in the animal hemisphere.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 4","pages":"Pages 255-260"},"PeriodicalIF":0.0,"publicationDate":"1987-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90480-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14742079","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Proteoglycan biosynthesis in relation to differentiation of cord blood monocytes in vitro","authors":"L. Uhlin-Hansen , S.O. Kolset","doi":"10.1016/0045-6039(87)90455-6","DOIUrl":"10.1016/0045-6039(87)90455-6","url":null,"abstract":"<div><p>Human monocytes were obtained from umbilical cord blood and cultured in vitro. By morphological criteria, the neonatal monocytes developed into macrophage-like cells in the course of 3–5 days in culture. The cells were exposed to [<sup>35</sup>S]sulphate for 24 h, either from day 0–1 or day 9–10 in vitro. The <sup>35</sup>S-labelled macromolecules recovered were mainly associated with the medium fraction (approximately 75%) in both day 1 and day 10 cultures. These secretory macromolecules were demonstrated by the use of chondroitinase ABC-digestions to contain predominately chondroitin sulphate proteoglycan (CSPG). [<sup>35</sup>S]galactosaminoglycan chains from day 10 cultures were more highly sulphated than the corresponding day 1 species due to the appearance of (glucuronosyl-4,6-diS-<em>N</em>-acetylgalactosamine) disulphated disaccharide units. The galactosaminoglycan chains in neonatal CSPG were found to increase in <em>M</em><sub>r</sub> during cultivation in vitro; from mean <em>M</em><sub>r</sub> of 20 400 to 30 200 (<em>n</em> = 5) in day 1 and day 10 medium proteoglycans, respectively. The corresponding <em>M</em><sub>r</sub> values for adult monocyte [<sup>35</sup>S]galactosaminoglycan chains were 21 300 and 22 800. On the basis of the concomitant changes in cellular morphology and glycosaminoglycan structure, it is concluded that neonatal monocytes, like monocytes from adults, differentiate into macrophage-like cells in vitro.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 3","pages":"Pages 189-197"},"PeriodicalIF":0.0,"publicationDate":"1987-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90455-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14772515","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Presence of a unique glycoconjugate on the surface of rat primordial germ cells during migration","authors":"A.R. Fazel , B.A. Schulte , R.P. Thompson , S.S. Spicer","doi":"10.1016/0045-6039(87)90456-8","DOIUrl":"10.1016/0045-6039(87)90456-8","url":null,"abstract":"<div><p>This investigation was undertaken to examine the chemical nature of components on the surface of primordial germ cells (PGCs) possibly related to their directed migration during development. To this end, lectins conjugated to horseradish peroxidase were used as specific histochemical probes to characterize the structure of PGC cell surface glycoconjugates and changes in their composition during and after their migration in the rat embryo. A lectin specific for terminal <em>N</em>-acetylgalactosamine (GalNAc) from <em>Dolichos biflorus</em> intensely stained the cell surface and a perinuclear region assumed to be Golgi zone of PGCs only during their migration. With one exception, no other site in the embryo stained with this lectin as migration proceeded. These observations suggest that the GalNAc-containing glycoconjugates on the surface of PGCs may be of functional importance in regulating the guidance and locomotion of these cells during the course of their extensive migration.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 3","pages":"Pages 199-211"},"PeriodicalIF":0.0,"publicationDate":"1987-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90456-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14772516","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"An immunofluorescence study of chondrogenesis in murine mandibular ectomesenchyme","authors":"Joy M. Richman, Virginia M. Diewert","doi":"10.1016/0045-6039(87)90453-2","DOIUrl":"10.1016/0045-6039(87)90453-2","url":null,"abstract":"<div><p>The temporal and spatial distribution of type I collagen, type II collagen, cartilage-specific proteoglycan (CSPG) and fibronectin in mouse mandible is described. CD-1 mouse embryos of 12-, 15-, and 18-day gestation were used, and matrix molecules were localized using indirect immunofluorescence. On day 12, accumulation of type II collagen, CSPG, and fibronectin within regions of condensed mesenchyme was noted. On day 15, intense staining for type II collagen and CSPG occurred. Fibronectin was less brilliant with its greatest concentration near the perichondrium. On day 18, the cartilage matrix was undergoing osseous replacement concurrent with loss of type II collagen and CSPG. Type I collagen was seen in the perichondrium, membranous bone and sub-basement membrane region in specimens of all ages. Synthesis and expression of extracellular matrix molecules reflect patterns of differentiation in mandibular mesenchyme.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 3","pages":"Pages 161-173"},"PeriodicalIF":0.0,"publicationDate":"1987-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90453-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14436701","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Somite chondrogenesis: the role of the microenvironment","authors":"Nagaswami Sri Vasan","doi":"10.1016/0045-6039(87)90452-0","DOIUrl":"10.1016/0045-6039(87)90452-0","url":null,"abstract":"","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 3","pages":"Pages 147-159"},"PeriodicalIF":0.0,"publicationDate":"1987-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90452-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14436702","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"MB1, a quail leukocyte/vascular endothelium antigen: characterization of the lymphocyte-surface form and identification of its secreted counterpart as α2-macroglobulin","authors":"Bruno Péault","doi":"10.1016/0045-6039(87)90454-4","DOIUrl":"https://doi.org/10.1016/0045-6039(87)90454-4","url":null,"abstract":"<div><p>A monoclonal antibody (α-MB1) binds to a cell surface marker expressed throughout ontogeny and adult life by vascular endothelial and hemopoietic cells of the quail, with the exception of erythrocytes, although it was raised against the heavy chain of quail immunoglobulin M. In addition to an 80 kDa polypeptide accounting for immunoglobulin μ chain, α-MB1 stains intensely a 180-kDa band on Western blots of reduced plasma proteins. We have previously characterized MB1 antigens of quail endothelial cells as glycoproteins of apparent molecular masses ranging from 80 to 200 kDa and provided evidence for the participation of vascular endothelium in the secretion of α-MB1-positive plasma components. We demonstrate here that this circulating material is the proteinase inhibitor <em>α</em><sub>2</sub>-macroglobulin. Furthermore, the MB1 antigens immunoprecipitated from lymphocytes are shown to be essentially similar to their endothelial counterparts, suggesting that the same molecular complex is expressed by all the elements of the hemangioblastic cell lineage. Finally, the cross reactivity of the α-MB1 antibody with immunoglobulin μ chain is confirmed and shown to occur via a carbohydrate epitope.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 3","pages":"Pages 175-187"},"PeriodicalIF":0.0,"publicationDate":"1987-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90454-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92062199","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lydie Gualandris , Anne-Marie Duprat , Pierre Rougé
{"title":"Cross-linking of membrane glycoconjugates is not a sufficient condition for neural induction by concanavalin A","authors":"Lydie Gualandris , Anne-Marie Duprat , Pierre Rougé","doi":"10.1016/0045-6039(87)90416-7","DOIUrl":"10.1016/0045-6039(87)90416-7","url":null,"abstract":"<div><p>Tetravalent native concanavalin A (Con A) has a neural inducing effect on amphibian presumptive ectoderm. The divalent dimeric form of this lectin, succinylated Con A (Succ-Con A), is devoid of neuralizing action on this target tissue in <em>Pleurodeles waltlii</em>. These results suggested that cross-linking of Con A receptors on the cell membrane (which is not provoked by the divalent lectin) might be required for neural induction. To test this possibility, Succ-Con A binding sites were experimentally cross-linked after binding of Succ-Con A to the target cell surface, using anti-Con A antibodies. The combination of these two agents mimics the cross-linking of Con A. The results showed that cross-linking alone, either by treatment with Succ-Con A and anti-Con A antibodies, or with the lectins WGA and PHA, which also cross-link cell surface binding sites, was not able to induce neuralization. This suggested that the inductive action of Con A cannot be explained in terms of receptor cross-linking.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 2","pages":"Pages 93-99"},"PeriodicalIF":0.0,"publicationDate":"1987-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90416-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13958927","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The epitope of mouse embryonic antigen(s) recognized by monoclonal antibody TEC-02 is a carbohydrate carried by high-molecular-weight glycoconjugates","authors":"Petr Dráber","doi":"10.1016/0045-6039(87)90419-2","DOIUrl":"10.1016/0045-6039(87)90419-2","url":null,"abstract":"<div><p>The expression and properties of mouse embryonic antigens, recognized by monoclonal antibody TEC-02, were analyzed in teratocarcinoma-derived cell lines. TEC-2 antigens were found in the majority of the parietal endoderm cells PYS-2 and in a fraction of cultured embryonal carcinoma cells but not in other cell lines tested. During the course of retinoic acid-induced differentiation of embryonal carcinoma cells F9, the expression of TEC-2 was transiently increased. Immunolabeling of extracts from F9 and PYS-2 cells separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that TEC-2 antigens are polydisperse glycoconjugates of high molecular weight (mostly > 100 000). The TEC-2 epitope was shown to be carbohydrate which in F9 cells might be attached to the same carrier as another developmentally regulated carbohydrate epitope TEC-1. The TEC-2 antigens, isolated by indirect immunoprecipitation, were degraded by extensive pronase digestion or mild alkaline treatment to mostly large products. Immunostaining of glycolipid standards suggested that TEC-2 epitope involves the GalNAc<em>β</em>1 → 4Gal<em>β</em>1 → 4R sequence. Combined data indicate that TEC-2 is a new developmentally regulated carbohydrate epitope carried in embryonal carcinoma cells predominantly on glycoprotein-bound large carbohydrates.</p></div>","PeriodicalId":75684,"journal":{"name":"Cell differentiation","volume":"21 2","pages":"Pages 119-130"},"PeriodicalIF":0.0,"publicationDate":"1987-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0045-6039(87)90419-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13589298","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}