Characterization of the sugar chain expression of normal term human placental villi using lectin histochemistry combined with immunohistochemistry

Lectin histochemistry was used to perform in situ characterization of the glycoconjugates present in boar testis and epididymis. Thirteen horseradish peroxidase- or digoxigenin-labelled lectins were used in samples obtained from healthy fertile boars. The acrosomes of the spermatids were stained intensely by lectins with affinity for galactose and N-acetyl-galactosamine residues, these being soybean, peanut and Ricinus communis agglutinins. Sertoli cells were stained selectively by Maackia ammurensis agglutinin. The lamina propria of seminiferous tubules showed the most intense staining with fucose-binding lectins. The Golgi area and the apical part of the principal cells of the epididymis were stained intensely with many lectins and their distribution was similar in the three zones of the epididymis. On the basis of lectin affinity, both testis and epididymis appear to have N- and O-linked glycoconjugates. Spermatozoa from different epididymal regions showed different expression of terminal galactose and N-acetyl-galactosamine. Sialic acid (specifically alpha2,3 neuraminic-5 acid) was probably incorporated into spermatozoa along the extratesticular ducts. These findings indicate that the development and maturation of boar spermatozoa are accompanied by changes in glycoconjugates. As some lectins stain cellular or extracellular compartments specifically, these lectins could be useful markers in histopathological evaluation of diseases of boar testis and epididymis.

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Characterization of glycoconjugates in the intestinal mucosa of vertebrates by means of lectin histochemistry.

ACTA HISTOCHEMICA ET CYTOCHEMICA ◽

10.1267/ahc.22.1 ◽

1989 ◽

Vol 22 (1) ◽

pp. 1-14 ◽

Cited By ~ 23

Author(s):

J. F. MADRID ◽

J. BALLESTA ◽

M. T. CASTELLS ◽

J. A. MARIN ◽

L. M. PASTOR

Keyword(s):

Intestinal Mucosa ◽

Lectin Histochemistry

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Molecular Cloning and Characterization of Bifidobacterium bifidum 1,2-α-l-Fucosidase (AfcA), a Novel Inverting Glycosidase (Glycoside Hydrolase Family 95)

Journal of Bacteriology ◽

10.1128/jb.186.15.4885-4893.2004 ◽

2004 ◽

Vol 186 (15) ◽

pp. 4885-4893 ◽

Cited By ~ 154

Author(s):

Takane Katayama ◽

Akiko Sakuma ◽

Takatoshi Kimura ◽

Yutaka Makimura ◽

Jun Hiratake ◽

...

Keyword(s):

Amino Acid ◽

Genomic Library ◽

Bifidobacterium Bifidum ◽

Glycoside Hydrolases ◽

Glycoside Hydrolase Family ◽

Amino Acid Residues ◽

Gene Encoding ◽

Sugar Chain ◽

Hydrolysis Of

ABSTRACT A genomic library of Bifidobacterium bifidum constructed in Escherichia coli was screened for the ability to hydrolyze the α-(1→2) linkage of 2′-fucosyllactose, and a gene encoding 1,2-α-l-fucosidase (AfcA) was isolated. The afcA gene was found to comprise 1,959 amino acid residues with a predicted molecular mass of 205 kDa and containing a signal peptide and a membrane anchor at the N and C termini, respectively. A domain responsible for fucosidase activity (the Fuc domain; amino acid residues 577 to 1474) was localized by deletion analysis and then purified as a hexahistidine-tagged protein. The recombinant Fuc domain specifically hydrolyzed the terminal α-(1→2)-fucosidic linkages of various oligosaccharides and a sugar chain of a glycoprotein. The stereochemical course of the hydrolysis of 2′-fucosyllactose was determined to be inversion by using 1H nuclear magnetic resonance. The primary structure of the Fuc domain exhibited no similarity to those of any glycoside hydrolases (GHs) but showed high similarity to those of several hypothetical proteins in a database. Thus, it was revealed that the AfcA protein constitutes a novel inverting GH family (GH family 95).

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Characterization of the skin mucus in the common octopus Octopus vulgaris (Cuvier) reared paralarvae

European Journal of Histochemistry ◽

10.4081/ejh.2017.2815 ◽

2017 ◽

Vol 61 (3) ◽

Cited By ~ 4

Author(s):

Gianluca Accogli ◽

Giovanni Scillitani ◽

Donatella Mentino ◽

Salvatore Desantis

Keyword(s):

Surface Layer ◽

Lectin Histochemistry ◽

The Body ◽

Octopus Vulgaris ◽

Mucous Cells ◽

Cell Type ◽

Skin Mucus ◽

The Common ◽

Common Octopus

The Octopus vulgaris farming is impaired by the high mortality of the paralarvae during the first month of life. Several factors have been investigated in this regard, but no data exist on the body surface mucus, which represents the interface with the outside environment. This study included morphometric analysis and glycoconjugates characterization of skin mucus in reared Octopus vulgaris paralarvae during the first month of life. Four types of mucous cells were distinguished: mucous 1 (m1) and mucous 2 (m2) cells were scattered in the mantle epidermis, mucous 3 (m3) and mucous 4 (m4) in the epithelium surrounding the sucker. Except for the presence of fucosylated and neutral glycoconjugates in all mucous cells, each cell type expressed a characteristic glycopattern. m2 and m4 contained also suphate and acid non-sulphate glycans, m3 lacked suphate glycoproteins. Lectin histochemistry showed that mantle mucous cells (m1, m2) expressed GlcNAc and lactosamine terminating glycans. m2 also contained GalNAc terminal or penultimate to sialic acid. m3 was distinguished by mannosylated glycans terminating with lactosamine and m4 by α2,6 sialoglycans. Glycoproteins terminating with lactosamine, Galβ1,3GalNAc, and α1,6-linked fucose were a common feature of paralarvae surface layer. Morphometry revealed a significant decrease of m1 and m2 abundance during the first month of life, afterwards the reared paralarvae died. Since the glycopattern did not change during the investigated period, the mantle mucous cells abundance could be related to the Octopus vulgaris paralarvae survival.

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Heterotopic gastric mucosa of the rectum—Characterization of endocrine and mucin-producing cells by immunocytochemistry and lectin histochemistry

Diseases of the Colon & Rectum ◽

10.1007/bf02553831 ◽

1989 ◽

Vol 32 (2) ◽

pp. 159-164 ◽

Cited By ~ 9

Author(s):

F. Carlei ◽

R. Pietroletti ◽

D. Lomanto ◽

P. Barsotti ◽

A. Crescenzi ◽

...

Keyword(s):

Gastric Mucosa ◽

Lectin Histochemistry ◽

Heterotopic Gastric Mucosa

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Distribution and characterization of anionic sites in trophoblast and capillary basal laminas of human placental villi

The Anatomical Record ◽

10.1002/ar.1092120109 ◽

1985 ◽

Vol 212 (1) ◽

pp. 63-68 ◽

Cited By ~ 3

Author(s):

Barry F. King

Keyword(s):

Anionic Sites ◽

Placental Villi

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Characterization of glycoconjugates in the bovine endometrium and chorion by lectin histochemistry

Reproduction ◽

10.1530/jrf.0.0870509 ◽

1989 ◽

Vol 87 (2) ◽

pp. 509-517 ◽

Cited By ~ 20

Author(s):

L. Munson ◽

J. J. Kao ◽

D. H. Schlafer

Keyword(s):

Lectin Histochemistry

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Tissue factor: identification and characterization of cell types in human placentae

Blood ◽

10.1182/blood.v76.1.86.bloodjournal76186 ◽

1990 ◽

Vol 76 (1) ◽

pp. 86-96 ◽

Cited By ~ 1

Author(s):

WP Faulk ◽

CA Labarrere ◽

SD Carson

Keyword(s):

Connective Tissue ◽

Tissue Factor ◽

Cell Types ◽

Basement Membranes ◽

Factor Vii ◽

Affinity Column ◽

Chorionic Villi ◽

Normal Term ◽

Synthetic Polypeptide

This is an immunohistologic study of tissue factor (TF) in snap frozen, unfixed, human normal-term placentae. Antibodies to TF were a monoclonal to human brain TF purified on a factor VII-agarose affinity column, and a polyclonal to a synthetic polypeptide representing the carboxyl-terminal nine amino acids of human TF. The results detail the localization and distribution of TF and characterize the cells in which it is found. TF was not observed in trophoblast, trophoblastic basement membranes, or noncellular components of connective tissue. TF was identified in some but not all macrophages, most fibroblast-like cells, and occasionally in perivascular cells and endothelium. The most consistent and intense reactions were obtained with vimentin-positive fibroblast-like cells in loose connective tissue. TF usually was not identified in fetal stem vessel endothelial cells, but TF reactivity was found in some of these cells in chorionic villi with histologic evidence of chronic inflammation. Such areas are uncommonly found in normal-term placentae. The vast majority of TF-reactive cells did not react with antibody to factor VII and were not in contact with blood. The biologic purpose of producing relatively great amounts of TF in areas remote from circulating factor VII is not known.

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