Glycohistochemical investigation of canine and feline zonae pellucidae of preantral and antral oocytes

Parillo, Francesco; Verini-Supplizi, Andrea

doi:10.1016/s0065-1281(99)80013-0

Cited by 18 publications

(34 citation statements)

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“…The absence of DBA-binding sites indicated that galactosamine residues were present in the β-anomeric form, as has been previously reported in domestic species [12][13][14][15][16]25].…”

Section: Discussionsupporting

confidence: 66%

“…The presence in both preantral and antral oocytes of wild boar ZP of the two main families of glycoproteins (having N-or Oglycosidic links) is similar to that in the ZP of domestic species [12][13][14][15][16]25].…”

Section: Discussionmentioning

confidence: 99%

“…Specimens were fixed in Carnoy's fluid. Serial sections of paraffin-embedded tissues were stained with conventional and lectin histochemical methods as described in detail elsewhere [16]. Each stain was performed in duplicate.…”

Section: Tissue Collectionmentioning

confidence: 99%

“…Lectin histochemistry was performed using a modification of the procedure described by Schulte and Spicer [9,21,22]; full details are given elsewhere [16]. The horseradish peroxidase (HRP)-lectin conjugates and their hapten sugars are shown in Table I.…”

Section: Lectin Histochemistrymentioning

confidence: 99%

“…Previous biochemical studies have demonstrated that the glycan portion of the glycoproteins ZPB of the pig [29] and of ZP3 [6,24,28] of the mouse may be the complementary sperm receptors mediating the primary binding between the spermatozoon and the ZP. These findings encouraged the use of plant lectins for the histochemical characterisation of the ZP glycoproteins in rats [3], humans [4] and various domestic mammals [12][13][14][15][16][17]25]. In those studies, lectin-staining was combined with treatments such as neuraminidase, desulphation and saponification to explore the carbohydrate composition and linkage types of the oligosaccharide side chains which constitute the mammalian ZP glycoproteins.…”

Section: Introductionmentioning

confidence: 99%

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Histochemical detection of the lectin-binding carbohydrates in the zona pellucida during oocyte growth in the wild boar (Sus scrofa scrofa)

et al. 2001

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-The changes that occur in the carbohydrate composition of zona pellucida glycoproteins during oocyte maturation in the wild-boar were studied using periodic-acid Schiff (PAS), High Iron Diamine (HID) and Low Iron Diamine (LID). Lectin staining was performed with a panel of 11 HRPlectin conjugates combined with neuraminidase digestion and chemical treatments. There were few internal glucidic residues, such as N-acetylglucosamine, in the wild boar zona pellucida but there were many subterminal β-N-acetylgalactosamine, α-and β-galactose determinants masked by sialic acid. In addition, β-N-acetylgalactosamine, β-galactose-(1-3)-N-acetylgalactosamine and β-galactose-(1-4)-N-acetylglucosamine were detected in the sulphated form in the terminal and/or subterminal position. Some differences in the lectin reactive sites occurred in the zona pellucida, depending on the stage of oocyte maturation. zona pellucida / glycoprotein / lectin-histochemistry / wild-boar Résumé -Détection histochimique des carbohydrates liant les lectines dans la zone pellucide pendant la croissance de l'ovocyte chez le sanglier (Sus scrofa scrofa). Les changements apparaissant dans la composition en carbohydrates des glycoprotéines de la zone pellucide pendant la maturation des oocytes chez le sanglier ont été étudiés en utilisant l'acide périodique Schiff, la diamine riche en fer et la diamine pauvre en fer. La coloration des lectines a été réalisée en utilisant 11 conjugués lectine-péroxydase combinés à une digestion par la neuraminidase et des traitements chimiques. Il y avait peu de résidus glucidiques internes tels que la N-glucosamine, présents dans la zone pellucide du sanglier mais il y avait de nombreux déterminants β-N acétylgalactosamines subterminaux et des déterminants α-et β-galactose masqués par de l'acide sialique. De plus, de la Vet. Res. 32 (2001) [581][582][583][584][585][586][587][588][589][590] 581

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“…The absence of DBA-binding sites indicated that galactosamine residues were present in the β-anomeric form, as has been previously reported in domestic species [12][13][14][15][16]25].…”

Section: Discussionsupporting

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Section: Tissue Collectionmentioning

confidence: 99%

Section: Lectin Histochemistrymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Histochemical detection of the lectin-binding carbohydrates in the zona pellucida during oocyte growth in the wild boar (Sus scrofa scrofa)

et al. 2001

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Pyriform cell differentiation in Podarcis sicula is accompanied by the appearance of surface glycoproteins bearing α‐galNAc terminated chains

et al. 2001

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The present histochemical and cytochemical study using a lectin panel (WGA, GSI-A4, GSI-B4, PSA UEA-I, PNA, LCA, Con-A, DBA, MPA, BPA) has demonstrated that, in Podarcis sicula, the differentiation of small follicle cells into pyriform cells by means of intermediate cells is accompanied by the appearance of glycoproteins bearing alpha-GalNAc terminated O-linked side chains on the cell surface. The distribution of DBA- and MPA-binding sites over the follicular epithelium changed during the different stages of oocyte growth. DBA- and MPA-binding sites first appeared at the beginning of folliculogenesis within the zona pellucida (ZP) and on the surface of small cells, i.e., the stem cells of pyriform cells. Afterward, labeling was evident on the cell surfaces of intermediate cells and, later on, also of pyriform cells. On the other hand, no labeling was detected on the small cells located under the basal lamina, which, reportedly, do not differentiate into pyriform cells (Filosa et al. J. Embryol. Exp. Morphol., 1979; 15:297-316). Once pyriform cells were differentiated, the distribution of DBA- and MPA-binding sites over the follicular epithelium remained unchanged until intermediate and pyriform cells underwent apoptosis (Motta et al. J. Exp. Zool., 1996; 276:233-241) and the follicular epithelium transformed into a monolayer composed of small follicle cells only (Filosa Mon. Zool. Ital., 1973; 7:151-165). During this stage of oocyte growth, DBA and MPA labeling gradually decreased to completely disappear in the follicular epithelium of vitellogenic follicles. It is noteworthy that the observed changes in the distribution of DBA- and MPA-binding sites represent the first evidence recognized by lectins of a gradual modification of surface glycoprotein distribution over the follicular epithelium in the ovarian follicles of nonmammalian vertebrates so far studied. Finally, the zona pellucida (ZP), characterized by the presence of GalNAc, GluNAc, Man, and Gal, was demonstrated to be first synthetized by the oocyte and later on by the follicle cells.

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Looping in on Ndc80 – How does a protein loop at the kinetochore control chromosome segregation?

Nilsson

2012

BioEssays

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Segregation of chromosomes during mitosis requires the interaction of dynamic microtubules with the kinetochore, a large protein structure established on the centromere region of sister chromatids. The core microtubule-binding activity of the kinetochore resides in the KMN network, an outer kinetochore complex. As part of the KMN network, the Ndc80 complex, which is composed of Ndc80, Nuf2, Spc24, and Spc25, is able to bind directly to microtubules and has the ability to track with depolymerizing microtubules to produce chromosome movement. The Ndc80 complex binds directly to microtubules through a calponin homology domain and an unstructured tail in the N terminus of the Ndc80 protein. A recent flurry of papers has highlighted the importance of an internal loop region in Ndc80 in establishing end-on attachment to microtubules. Here I discuss these recent findings that suggest that the Ndc80 internal loop functions as a binding site for proteins required for kinetochore-microtubule interactions.

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Glycohistochemical investigation of canine and feline zonae pellucidae of preantral and antral oocytes

Cited by 18 publications

References 40 publications

Histochemical detection of the lectin-binding carbohydrates in the zona pellucida during oocyte growth in the wild boar (Sus scrofa scrofa)

Histochemical detection of the lectin-binding carbohydrates in the zona pellucida during oocyte growth in the wild boar (Sus scrofa scrofa)

Pyriform cell differentiation in Podarcis sicula is accompanied by the appearance of surface glycoproteins bearing α‐galNAc terminated chains

Looping in on Ndc80 – How does a protein loop at the kinetochore control chromosome segregation?

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