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 58,342 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To elucidate the mechanism for the biosynthesis of O-linked mucin oligosaccharides, airway secretory cells of the hamster trachea were embedded in Lowicryl K4M resin, and sections were examined by lectin-gold cytochemistry with special attention focused on the Golgi apparatus. The interrelations between the Golgi cisternae stained with five different lectins were determined by double-staining procedures using various combinations of lectins conjugated with 14-nm and 8-nm colloidal gold. Several cis cisternae were stained only with HPA (Helix pomatia agglutinin specific for terminal alpha-N-acetylgalactosamine). The next medial cisternae were not stained with HPA, but reacted positively with two lectins, GSII (Griffonia simplicifolia agglutinin II specific for terminal alpha- or beta-N-acetylglucosamine) and RCAI (Ricinus communis agglutinin I specific for beta-galactose). The trans cisternae as well as condensing and mature secretory granules were labeled with four lectins, UEAI (Ulex europaeus agglutinin I specific for terminal alpha-L-fucose) and LFA (Limax flavus agglutinin specific for terminal N-acetyl or N-glycolyl neuraminic acid) in addition to HPA and RCAI. The same number of trans cisternae were positive to HPA and UEAI, whereas LFA bound to a few transmost cisternae but fewer than were stained with HPA or UEAI. The observed sequential appearance of different sugar residues in different levels of Golgi cisternae (from cis to trans cisternae) coincides quite well with the sugar sequence of airway mucin oligosaccharide (from reducing to nonreducing ends) proposed by biochemical analysis. It is suggested that airway mucin oligosaccharides elongate during a vectorial movement through the Golgi stack from cis toward trans and that the stack consists of at least three functionally distinct segments, cis, medial, and trans; in these three segments there take place, respectively, the initial O-glycosylation of mucin core peptide, the formation of a core region of oligosaccharide chain, and the completion of chain growth by addition of terminal sugar moieties.
Anat Rec 1988 Jun
PMID:Lectin-gold cytochemistry of mucin oligosaccharide biosynthesis in Golgi apparatus of airway secretory cells of the hamster. 341 85

Testes of sexually mature men were studied histochemically with 20 fluorescein isothiocyanate-labeled lectins. Based on their pattern of reactivity with intratesticular spermatogenic cells, lectins were divided into five groups: 1) lectins reacting with all spermatogenic cells (Suc. ConA, WGA, LCA, PHA-E, PHA-L, STA, MPA, and RCA-II); 2) lectin reacting with spermatocytes, spermatids, and spermatozoa, but not with spermatogonia (RCA-I); 3) lectins reacting with spermatids and spermatozoa only (BPA, PNA, SBA, and VVA); 4) lectins reacting only with spermatozoa (HPA, GSA-I, UEA-II, and GSA-II); and 5) lectins with no distinct staining of spermatogenic cells (DBA, LBA, and UEA-I). All lectins from groups 1-4 were reactive with ejaculated spermatozoa. On the basis of the staining patterns of the head region of ejaculated spermatozoa, four lectin reactivity groups were defined: 1) lectins reacting with the plasma membrane of the whole head (BPA, WGA, LCA, STA, RCA-II, PHA-E, PHA-L, RCA-I, UEA-II, and GSA-II); 2) lectin reacting with the acrosomal cap and postacrosomal region of the plasma membrane (Suc. ConA); 3) lectin reacting with the acrosomal cap region of the plasma membrane (PNA); and 4) lectins reacting with the midregion of the sperm head in a bandlike manner (HPA, VVA, SBA, GSA-I, and MPA). These data provide a map of lectin binding sites on human testicular spermatogenic cells and ejaculated spermatozoa and show that the distribution of glycoconjugate domains of spermatogenic cell changes during differentiation and maturation.
Anat Rec 1985 Jul
PMID:Lectin binding sites on human sperm and spermatogenic cells. 393 81

The cloacal organ of Salamandridae species contains four glands: pelvic, dorsal, ventral, and Kingsbury's glands. Pelvic glands have been studied only by light microscopy with conventional methods, and consist of multiple tubular serous glands with a prismatic epithelium which contains numerous PAS positive secretory granules. The present report is an ultrastructural and lectin cytochemistry characterization of the pelvic glands of Triturus marmoratus marmoratus throughout the reproductive cycle. Our methods consisted of conventional electron microscopy, and colloidal-gold lectin cytochemistry of the following lectins: WGA, ConA, LcA, UEA-I, PNA, SBA, and HPA. In the prereproductive period, the glands showed a tall epithelium which consisted of two cell types, dark and clear cells, surrounded by elongated, myoepithelial cells. Both dark and clear cells showed the ultrastructural characteristics of secretory cells, and exhibited many secretory granules in the apical cytoplasm. Areas showing densely packed, degenerating cell organelles--which were not surrounded by membrane--were observed in the dark cells whereas the clear cells showed large heterolysosomes. In the postreproductive period the number of secretory granules decreased, the rough endoplasmic reticulum was less developed, and areas of degenerating organelles were absent. In addition, small basal cells appeared. The results of the lectin histochemistry study were similar in both reproductive periods. In the epithelial cells, the rough endoplasmic reticulum, the Golgi complex, and secretory granules exclusively labeled to ConA. In all cell types, the nuclei reacted to all lectins while the cytosol only reacted to LcA lectin. The ultrastructural and histochemical characteristics of the pelvic glands of T. marmoratus suggest that these glands could be homologous to the mammalian seminal vesicles and prostate.
Anat Rec 1999 02 01
PMID:Ultrastructure and lectin cytochemistry of the cloacal pelvic glands in the male newt Triturus marmoratus marmoratus. 997 4

The origin of the acrosome is controversial, because of both its lysosomal nature and at the moment of its appearance, which seems to be species-specific. Considering the amazing organization shown by the acrosome of some urodele amphibians, HPA-colloidal gold cytochemistry was used to analyze the biogenesis of the acrosome in the urodele Pleurodeles waltl at electron microscopy level. The results showed that HPA-labeling is useful to label the acrosome and its precursor vesicles and, consequently, HPA-histochemistry could be used as a marker of acrosomal content. Labeling of the Golgi apparatus and precursor vesicles was seen in primary spermatocytes and round (stage I) spermatids, thus contributing solid evidence for the beginning of acrosome biogenesis before meiosis. In both primary spermatocytes and round spermatids, an enigmatic vesicle, probably related to the biosynthesis of the neck piece or the tail, was also labeled. Labeling in elongating spermatids (stage II-IV), showed a homogeneous distribution of colloidal gold particles in the acrosomal cap, but the perforatorium was not positive to the lectin. However, in mature (stage V-VI) spermatids, a regional distribution of labeling in the acrosome was seen, with the apical knob showing a stronger labeling than the lateral barb, and the lateral barb showing a stronger labeling than the principal piece of the acrosomal cap. This regional distribution of the labeling suggests that the acrosome develops several domains with different glycoconjugate compositions.
Anat Rec (Hoboken) 2008 Sep
PMID:Acrosome biosynthesis in spermatocytes and spermatids revealed by HPA lectin cytochemistry. 1852 2