Gene/Protein Disease Symptom Drug Enzyme Compound
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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

In preparation of a clinical phase I/II study in renal cell carcinoma (RCC) patients, we developed a clinically applicable protocol that meets good clinical practice (GCP) criteria regarding the gene transduction and expansion of primary human T lymphocytes. We previously designed a transgene that encodes a single chain (sc) FvG250 antibody chimeric receptor (ch-Rec), specific for a RCC tumor-associated antigen (TAA), and that genetically programs human T lymphocytes with RCC immune specificity. Here we describe the conditions for activation, gene transduction, and proliferation for primary human T lymphocytes to yield: (a) optimal functional expression of the transgene; (b) ch-Rec-mediated cytokine production, and (c) cytolysis of G250-TAA(POS) RCC by the T-lymphocyte transductants. Moreover, these parameters were tested at clinical scale, i.e., yielding up to 5-10 x 10(9) T-cell transductants, defined as the treatment dose according to our clinical protocol. The following parameters were, for the first time, tested in an interactive way: (1) media compositions for production of virus by the stable PG13 packaging cell; (2) T-lymphocyte activation conditions and reagents (anti-CD3 mAb; anti-CD3+anti-CD28 mAbs; and PHA); (3) kinetics of T-lymphocyte activation prior to gene transduction; (4) (i) T-lymphocyte density, and (ii) volume of virus-containing supernatant per surface unit during gene transduction; and (5) medium composition for T-lymphocyte maintenance (i) in-between gene transduction cycles, and (ii) during in vitro T-lymphocyte expansion. Critical to gene transduction of human T lymphocytes at clinical scale appeared to be the use of the fibronectin fragment CH-296 (Retronectin) as well as Lifecell) X-fold cell culture bags. In order to comply with GCP requirements, we used: (a) bovine serum-free human T-lymphocyte transduction system, i.e., media supplemented with autologous patients' plasma, and (b) a closed cell culture system for all lymphocyte processing. This clinical protocol routinely yields 30-65% scFvG250 ch-Rec(POS) T lymphocytes in both healthy donors and RCC patients.
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PMID:Protocol for gene transduction and expansion of human T lymphocytes for clinical immunogene therapy of cancer. 1208 62

The topography and structure of the follicular cells and the follicular cavity of the hypophyseal pars tuberalis (PT) were studied in adult hibernating bats (Pipistrellus pipistrellus and Rhinolophus ferrumequinum) of both sexes, during the annual seasonal cycle and the reproductive cycle. The follicular cells were found to be organized around a central cavity. They showed a polyhedral shape and apical microvilli protruding into central cavities. During hibernation, the follicular cells showed active cytoplasmic organelles, clusters of glycogen particles, and lipid droplets. In the supranuclear cytoplasm, 9+2 type cilia, some dense bodies, microvesicular vacuoles, and thin actin-like filaments (rather scarce during autumn) were detected. The contents of the follicular cavity showed well-defined ultrastructural seasonal characteristics, with a colloid-like aspect during awakening and a strongly granular aspect during autumn oestrus and mating. Positive staining for PAS and paraldehyde fuchsin, and a marked reaction to lectins PHA-L4, MAM, and RCA 60 suggested the presence of sialo-glycoproteins in the follicular cavities. Both follicular and endocrine PT-specific cells appeared to mark the boundary of follicular cavities. This finding suggests that the follicular cavity contents are comprised of both types of cells, rather than by cell fragmentation or degeneration products.
Anat Rec A Discov Mol Cell Evol Biol 2003 Aug
PMID:Ultrastructural aspects of the follicular cells of the pars tuberalis in bats related to the seasonal cycle. 1284 12

During development, different epithelial cells in the mouse cochlea express different cell surface glycoconjugates, which may reflect membrane specialization. Some of the lectins tested in this study (SBA, succ-WGA, and PSA) labeled the sensory cells of the cochlea around birth. Other lectins (WGA, Con A, RCA-II, and PHA-E) labeled surfaces of the sensory cells, particularly the stereocilia, from early stages of development (gestation day (GD) 16) through 21 days after birth. These may be adhesion molecules needed to attach the newly forming tectorial membrane (TM) to the stereocilia. Lectin staining of the developing TM revealed that the substructures of the TM are biochemically distinct. Lectin staining also showed the temporal sequence of the expression of cytoplasmic glycoconjugates of the cochlear epithelium during development. Biochemical changes during development are probably the result of different cells being involved in the production of glycoconjugates, and may have functional significance, specifically with regard to the expression of adhesion and/or signaling molecules.
Anat Rec A Discov Mol Cell Evol Biol 2003 Oct
PMID:Distribution of glycoconjugates during cochlea development in mice: light microscopic lectin study. 1297 16

Glycoconjugates are biopolymers that are broadly distributed in the central nervous system, including the cell surface of neural stem cells or neural precursor cells (NSCs/NPCs). Glycoconjugates can be recognized by carbohydrate-binding proteins, lectins. Two lectins, Phaseolus vulgaris lectin agglutinin E-form (PHA-E4) and wheat germ agglutinin (WGA) have been reported to be useful in isolating NSCs/NPCs by fluorescence-activated cell sorting (FACS) or immunopanning methods. In this study, we analyzed the lectin-binding properties of NSCs/NPCs in two neurogenic regions of the adult mouse brain to determine whether PHA-E4 and WGA exhibit specific binding patterns on sections and whether there are other lectins presenting the binding pattern similar to those of PHA-E4 and WGA in lectin histochemistry. Among nine types of lectins, peanut agglutinin was localized to the white matter and four lectins bound to cells within the subventricular zone (SVZ) of the lateral ventricle. Lectin histochemistry combined with immunohistochemistry demonstrated that one lectin, Ricinus communis agglutinin, specifically detected type A neuronal precursors and that the remaining three lectins, Agaricus bisporus agglutinin (ABA), PHA-E4, and WGA, recognized type B NSCs and type C transient amplifying cells in the SVZ. These three lectins also recognized type 1 quiescent neural progenitors and type 2a amplifying neural progenitors in the subgranular layer of the dentate gyrus. Lectin histochemistry of the neurosphere culture also yielded similar results. These observations suggest that, in addition to PHA-E4 and WGA, ABA lectin may also be applicable in FACS or immunopanning for the isolation of NSCs/NPCs.
Anat Rec (Hoboken) 2011 Feb
PMID:Lectins as a tool for detecting neural stem/progenitor cells in the adult mouse brain. 2123 6