Histochemical evaluation of secretory glycoproteins in human salivary glands with lectin-horseradish peroxidase conjugates.

Paraffin sections of submandibular, sublingual, minor salivary, and parotid glands from ten human autopsy cases were stained with a battery of ten lectins conjugated to horseradish peroxidase. Variable affinity for one or another lectin between mucous cells in a gland evidenced cellular heterogeneity in mucin production. Mucous cells of a given type of gland varied among individuals, but for a single individual appeared markedly but not completely similar from one type of salivary gland to another. The individual variation related, in part, to the ABO blood group and secretor status of the individual. For mucous cells in secretors of blood group A and B all antigens stained strongly for the presence of terminal alpha-N-acetylgalactosamine or alpha-galactose, respectively. Mucous cells in AB secretors contained both antigens, whereas those of O (H) secretors lacked both. Mucous cells of three presumed nonsecretors, two of whom were immature infants and possibly too young to produce ABO antigen, failed to stain. Mucous cells in glands from the presumed nonsecretors, however, revealed a staining pattern consistent with the presence of Lea antigen. Mucous cells of nonsecretors stained with Lotus tetragonolobus agglutinin but not with Ulex europeus I agglutinin, whereas mucous cells of ABO secretors stained with both lectins. This difference in lectin binding indicated that sites reactive only with Lotus tetragonolobus agglutinin contain 1----4 linked fucosyl residues and sites stained by both lectins contain fucose linked 1----2 to the oligosaccharide. Staining of mucous cells of nonsecretors with Pisum sativum agglutinin indicate that either the lectin binds to internal N-acetylglucosamine of Lea substance or the mucous cells contain an N-glycosidic glycoprotein of the type thought to bind this lectin. Serous cells stained less strongly than mucous cells and differed in lectin affinities from one type of gland to another in an individual. Staining of serous cells of a given gland varied markedly among different subjects. This individual variability did not relate to blood group as terminal sugars demonstrative of A or B blood group antigens were not detected in any serous cells. Serous cells in the submandibular glands from the two immature infants were unreactive with all lectin conjugates. Secretions in parotid and submandibular serous cells generally contained a higher content of fucose than those in sublingual serous cells, which contained higher levels of a terminal galactose-sialic acid dimer. Some but not other cells of striated and interlobular ducts of submandibular glands of one subject stained for alpha-N-acetylgalactosamine.

Download Full-text

Histochemical reactivity of the Geodia cydonium agglutinin (GCA) in human tissues.

Journal of Histochemistry & Cytochemistry ◽

10.1177/39.4.2005375 ◽

1991 ◽

Vol 39 (4) ◽

pp. 491-505 ◽

Cited By ~ 3

Author(s):

M Vierbuchen ◽

G Uhlenbruck ◽

F G Hanisch ◽

W E Müller ◽

M Ortmann ◽

...

Keyword(s):

Binding Site ◽

Blood Group ◽

Lectin Binding ◽

Blood Group Antigens ◽

Group Status ◽

Geodia Cydonium ◽

Group A ◽

Complex Carbohydrates ◽

Group B ◽

Inhibition Studies

We applied a peroxidase-antiperoxidase technique to study the distribution pattern and binding characteristics of the lectin from the marine sponge Geodia cydonium (Geodia cydonium agglutinin; GCA) in various human tissues. This lectin has been shown to possess a broad reactivity, but there was a distinct distribution of binding sites within the different organs. In the histochemical system GCA displayed no blood group specificity and labeled red blood cells, the vascular endothelium, and epithelial cells showing blood group antigen expression independent of the ABH blood group status. However, inhibition of GCA reactivity by simple sugars and complex carbohydrates demonstrated tissue-specific differences of lectin binding related to the ABH blood group status of the tissue and revealed information on the structural requirements of the histological lectin binding site. Tissues that totally lacked blood group antigens or that expressed only the H-antigen disclosed a GCA reactivity which was completely inhibited by lactose. In contrast, tissues that expressed blood group A- or blood group B-antigen exhibited a lactose-resistant lectin binding which was inhibited only by water-soluble blood group substance A from peptone A and by bovine glycophorin but not by other complex carbohydrates, including human glycophorin and human asialoglycophorin. Competitive inhibition studies in situ revealed that GCA binding was not inhibited by blood group type I/II carbohydrate sequence-specific lectins or by lectins with other sugar specificities. Inhibition by lactose of GCA binding to some histological sites indicates that the binding site consists of a beta-linked galactose-containing disaccharide. However, periodate oxidation of tissue sections had no effect on lectin binding, pointing to a subterminal location of the relevant sequence. The results obtained from inhibition studies with simple saccharides and complex carbohydrates in relation to the expression of ABH blood group antigens suggest a complex lectin combining site(s) in histological specimens. The lectin may possess either one binding site with a range of affinities for different carbohydrates (besides beta-linked disaccharides the GCA binding site accommodates to carbohydrate determinants carrying the blood group A or blood group B determinant), or may possess two different binding sites. Besides an acceptor site for beta-linked disaccharides, an additional binding site may exist accommodating to extended carbohydrate sequences related to A or B blood group structures. In conclusion, GCA represents a blood group-nonspecific lectin whose binding affinities are determined by the ABH blood group status of the tissue.

Download Full-text

The histo-blood group antigens of the host cell may determine the binding of different viruses such as SARS-CoV-2

Future Microbiology ◽

10.2217/fmb-2020-0158 ◽

2021 ◽

Vol 16 (2) ◽

pp. 107-118

Author(s):

Mayra Cuéllar-Cruz

Keyword(s):

Host Cell ◽

Blood Group ◽

Blood Group Antigens ◽

Human Host ◽

Human Organs ◽

Infection Mechanism ◽

The Family ◽

The Individual ◽

Human Viruses

Viruses have caused the death of millions of people worldwide. Specifically, human viruses are grouped into 21 families, including the family of coronaviruses (CoVs). In December 2019, in Wuhan, China, a new human CoV was identified, SARS-CoV-2. The first step of the infection mechanism of the SARS-CoV-2 in the human host is adhesion, which occurs through the S glycoprotein that is found in diverse human organs. Another way through which SARS-CoV-2 could possibly attach to the host’s cells is by means of the histo-blood group antigens. In this work, we have reviewed the mechanisms by which some viruses bind to the histo-blood group antigens, which could be related to the susceptibility of the individual and are dependent on the histo-blood group.

Download Full-text

DIRECT EVIDENCE OF MUTATION AT THE LOCUS FOR GALACTOSE-I-PHOSPHATE URIDYL TRANSFERASE

PEDIATRICS ◽

10.1542/peds.45.4.672 ◽

1970 ◽

Vol 45 (4) ◽

pp. 672-676

Author(s):

William J. Mellman ◽

Fred H. Allen ◽

Lester Baker ◽

Thomas A. Tedesco

Keyword(s):

Genetic Polymorphisms ◽

Blood Group ◽

Genetic Markers ◽

Alternative Explanation ◽

Direct Evidence ◽

Paternity Testing ◽

Mutation Rates ◽

Blood Group Antigens ◽

Heterozygous State ◽

The Individual

An apparent fresh mutation has been identified at the human transferase locus (Gt) that has resulted in an occurrence of the heterozygous state for galactosemia (Gt+/GtG). The individual concerned is the mother of a child with galactosemia, neither of whose parents was found to be heterozygous for galactosemia. Recently discovered human genetic markers and established blood group antigens have been used to test for non-paternity as an alternative explanation to mutation. Paternity was proven in this instance with greater than 98% confidence. This paper illustrates the feasibility of determining biochemically the mutation rates for specific genetic loci and the improved confidence that can be achieved in paternity testing with more recently described human genetic polymorphisms.

Download Full-text

Localization of blood group antigens in human pancreas with lectin-horseradish peroxidase conjugates.

ACTA HISTOCHEMICA ET CYTOCHEMICA ◽

10.1267/ahc.19.205 ◽

1986 ◽

Vol 19 (2) ◽

pp. 205-218 ◽

Cited By ~ 18

Author(s):

NOBUAKI ITO ◽

KATSUJI NISHI ◽

MITSURU NAKAJIMA ◽

YOSHIE MATSUDA ◽

AKIKO ISHITANI ◽

...

Keyword(s):

Horseradish Peroxidase ◽

Blood Group ◽

Blood Group Antigens ◽

Human Pancreas

Download Full-text

Histo-blood group antigens of glycosphingolipids predict susceptibility of human intestinal enteroids to norovirus infection

Journal of Biological Chemistry ◽

10.1074/jbc.ra120.014855 ◽

2020 ◽

Vol 295 (47) ◽

pp. 15974-15987 ◽

Cited By ~ 1

Author(s):

Inga Rimkute ◽

Konrad Thorsteinsson ◽

Marcus Henricsson ◽

Victoria R. Tenge ◽

Xiaoming Yu ◽

...

Keyword(s):

Blood Group ◽

Lipid Membranes ◽

Molecular Mechanisms ◽

Ex Vivo ◽

Particle Interaction ◽

Lipid Vesicles ◽

Blood Group Antigens ◽

Interaction Kinetics ◽

Glycerolipid Composition ◽

The Individual

The molecular mechanisms behind infection and propagation of human restricted pathogens such as human norovirus (HuNoV) have defied interrogation because they were previously unculturable. However, human intestinal enteroids (HIEs) have emerged to offer unique ex vivo models for targeted studies of intestinal biology, including inflammatory and infectious diseases. Carbohydrate-dependent histo-blood group antigens (HBGAs) are known to be critical for clinical infection. To explore whether HBGAs of glycosphingolipids contribute to HuNoV infection, we obtained HIE cultures established from stem cells isolated from jejunal biopsies of six individuals with different ABO, Lewis, and secretor genotypes. We analyzed their glycerolipid and sphingolipid compositions and quantified interaction kinetics and the affinity of HuNoV virus-like particles (VLPs) to lipid vesicles produced from the individual HIE-lipid extracts. All HIEs had a similar lipid and glycerolipid composition. Sphingolipids included HBGA-related type 1 chain glycosphingolipids (GSLs), with HBGA epitopes corresponding to the geno- and phenotypes of the different HIEs. As revealed by single-particle interaction studies of Sydney GII.4 VLPs with glycosphingolipid-containing HIE membranes, both binding kinetics and affinities explain the patterns of susceptibility toward GII.4 infection for individual HIEs. This is the first time norovirus VLPs have been shown to interact specifically with secretor gene–dependent GSLs embedded in lipid membranes of HIEs that propagate GII.4 HuNoV ex vivo, highlighting the potential of HIEs for advanced future studies of intestinal glycobiology and host-pathogen interactions.

Download Full-text

Expression of Blood Group Antigens and Lectin Binding in Adenocarcinomas of the Endometrium

Pathology International ◽

10.1111/j.1440-1827.1990.tb01593.x ◽

1990 ◽

Vol 40 (7) ◽

pp. 509-516

Author(s):

Rashida S. Memon ◽

Suguru Yonezawa ◽

Kazuhisa Hasui ◽

Eiichi Sato

Keyword(s):

Blood Group ◽

Lectin Binding ◽

Blood Group Antigens

Download Full-text

Faculty Opinions recommendation of Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1099150.555364 ◽

2008 ◽

Author(s):

Richard L Stevens

Keyword(s):

Blood Group ◽

Blood Group Antigens ◽

Differential Recognition

Download Full-text

ADHD with Comorbid Bipolar Disorders: A Systematic Review of Neurobiological, Clinical and Pharmacological Aspects Across the Lifespan

Current Medicinal Chemistry ◽

10.2174/0929867326666190805153610 ◽

2019 ◽

Vol 26 (38) ◽

pp. 6942-6969 ◽

Cited By ~ 1

Author(s):

Federico Mucci ◽

Maria Teresa Avella ◽

Donatella Marazziti

Keyword(s):

Clinical Features ◽

Adult Adhd ◽

Neurodevelopmental Disorder ◽

Bipolar Disorders ◽

Mood Stabilizers ◽

Disruptive Behaviour ◽

Single Individual ◽

Pharmacological Management ◽

Long Time ◽

The Individual

Background: Attention deficit hyperactivity (ADHD) disorder is a neurodevelopmental disorder characterized by inattention, hyperactivity, disruptive behaviour, and impulsivity. Despite considered typical of children for a long time, the persistence of ADHD symptoms in adulthood gained increasing interest during the last decades. Indeed, its diagnosis, albeit controversial, is rarely carried out even because ADHD is often comorbid with several other psychiatric diosrders, in particular with bipolar disorders (BDs), a condition that complicates the clinical picture, assessment and treatment. Aims: The aim of this paper was to systematically review the scientific literature on the neurobiological, clinical features and current pharmacological management of ADHD comorbid with BDs across the entire lifespan, with a major focus on the adulthood. Discussion: The pharmacology of ADHD-BD in adults is still empirical and influenced by the individual experience of the clinicians. Stimulants are endowed of a prompt efficacy and safety, whilst non-stimulants are useful when a substance abuse history is detected, although they require some weeks in order to be fully effective. In any case, an in-depth diagnostic and clinical evaluation of the single individual is mandatory. Conclusions: The comorbidity of ADHD with BD is still a controversial matter, as it is the notion of adult ADHD as a distinct nosological category. Indeed, some findings highlighted the presence of common neurobiological mechanisms and overlapping clinical features, although disagreement does exist. In any case, while expecting to disentangle this crucial question, a correct management of this comorbidity is essential, which requires the co-administration of mood stabilizers. Further controlled clinical studies in large samples of adult ADHD-BD patients appear extremely urgent in order to better define possible therapeutic guidelines, as well as alternative approaches for this potentially invalidating condition.

Download Full-text