scholarly journals Leu-7 immunoreactivity in human, monkey, and pig bronchopulmonary neuroepithelial bodies and neuroendocrine cells.

1987 ◽  
Vol 35 (6) ◽  
pp. 687-691 ◽  
Author(s):  
J M Lauweryns ◽  
L Van Ranst
Keyword(s):  
Monoclonal Antibody ◽  
Nerve Fibers ◽  
Neuroendocrine Cells ◽  
Immunoperoxidase Method ◽  
Neuroepithelial Bodies ◽  
Immune Systems ◽  
Myelin Sheaths ◽  
Human Natural Killer Cells ◽  
Indirect Immunoperoxidase ◽  
Leu 7

Anti-Leu 7 is a monoclonal antibody recognizing a surface antigen on human natural killer cells. By applying the indirect immunoperoxidase method, we demonstrated Leu-7 immunoreactivity in the cytoplasm of neuroepithelial bodies (NEB) and neuroendocrine cells (NEC) of human, monkey, and pig respiratory mucosa. In addition, the anti-Leu-7 monoclonal antibody stained the myelin sheaths of nerve fibers in all tissues investigated. Our findings support the hypothesis that shared antigens exist between the nervous, endocrine, and immune systems.

scholarly journals Immunocytochemical localization of aromatic L-amino acid decarboxylase in human, rat, and mouse bronchopulmonary and gastrointestinal endocrine cells.

1988 ◽  
Vol 36 (9) ◽  
pp. 1181-1186 ◽  
Author(s):  
J M Lauweryns ◽  
L Van Ranst
Keyword(s):  
Amino Acid ◽  
Aromatic Amino Acids ◽  
Nerve Fibers ◽  
Neuroendocrine Cells ◽  
Adrenergic Nerve ◽  
Acid Decarboxylase ◽  
Immunoperoxidase Method ◽  
Amino Acid Decarboxylase ◽  
Additional Tool ◽  
Mouse Tissues

Aromatic L-amino acid decarboxylase (AADC) catalyzes the cellular decarboxylation of L-aromatic amino acids and is therefore involved in the synthesis of several biogenic amines. Application of the indirect immunoperoxidase method on human, rat, and mouse tissues using specific antibodies to AADC revealed all AADC-containing cells. Besides mast cells and adrenergic nerve fibers, the following cells were immunostained: neuroendocrine cells in the tracheobronchial epithelium; neuroepithelial bodies in the bronchopulmonary epithelium; Kultschitzky cells in the small intestine and appendix as well as adrenal chromaffin cells. All the latter cells belong to the so-called APUD system, the "D" in the acronym standing for the activity of the enzyme aromatic L-amino acid decarboxylase. Immunocytochemistry for AADC may become an additional tool not only to highlight APUD cells in tissue sections but also to differentiate the sites of cellular amine synthesis from those of amine storage.

scholarly journals Chromogranin in bronchopulmonary neuroendocrine cells. Immunocytochemical detection in human, monkey, and pig respiratory mucosa.

1987 ◽  
Vol 35 (1) ◽  
pp. 113-118 ◽  
Author(s):  
J M Lauweryns ◽  
L van Ranst ◽  
R V Lloyd ◽  
D T O'Connor
Keyword(s):  
Monoclonal Antibody ◽  
Silver Staining ◽  
Chromogranin A ◽  
Neuroendocrine Cells ◽  
Neuroepithelial Bodies ◽  
Apud Cells ◽  
Respiratory Mucosa ◽  
Immunocytochemical Detection

Immunoreactive chromogranin A was demonstrated by immunocytochemistry in the cytoplasm of neuroendocrine cells (NEC) and neuroepithelial bodies (NEB) in human, monkey, and pig respiratory mucosa. Three different antisera (one monoclonal and one polyclonal to human chromogranin A, and one polyclonal to bovine chromogranin A) were applied in this study. Chromogranin immunopositivity varied in extent and intensity according to the antiserum applied and the tissue investigated. The monoclonal antibody revealed the strongest immunoreaction. Good correlation between chromogranin immunoreactivity and Grimelius silver staining was observed by comparing adjacent sections, although more cells seemed to reveal chromogranin immunoreactivity than argyrophylia. Chromogranin appears to be a useful histological marker for APUD cells in the respiratory mucosa of several species.

scholarly journals Immunocytochemical localization of tissue kallikrein in brain ventricular epithelium and hypothalamic cell bodies.

1985 ◽  
Vol 33 (9) ◽  
pp. 951-953 ◽  
Author(s):  
J A Simson ◽  
R Dom ◽  
J Chao ◽  
C Woodley ◽  
L Chao ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Epithelial Cells ◽  
Third Ventricle ◽  
Immunoperoxidase Staining ◽  
Tissue Kallikrein ◽  
Immunocytochemical Localization ◽  
Specific Monoclonal Antibody ◽  
The Third ◽  
Indirect Immunoperoxidase ◽  
Rat Tissue

A specific monoclonal antibody against rat tissue kallikrein was used as the primary antibody for indirect immunoperoxidase staining of rat hypothalamus. Kallikrein was localized in the epithelial cells (ependyma) lining the third ventricle as well as in cell bodies of arcuate, supraoptic, paraventricular, and ventromedial nuclei.

Leu 7 Monoclonal Antibody in Diagnostic Histopathology: its Lack of Neuroendocrine Specificity

1991 ◽  
Vol 187 (8) ◽  
pp. 1028-1030 ◽  
Author(s):  
M. Barbareschi ◽  
S. Girlando ◽  
S. Boi ◽  
F.A. Mauri
Keyword(s):  
Monoclonal Antibody ◽  
Diagnostic Histopathology ◽  
Leu 7

Characterization of a Subset of Human Natural Killer Cells That Express OKM1 But Lack HNK-1 (Leu-7) Antigens

1984 ◽  
Vol 20 (3) ◽  
pp. 261-265 ◽  
Author(s):  
R. MAROLDA ◽  
A. B. TILDEN ◽  
T. ABO ◽  
P. A. DOUGHERTY ◽  
C. M. BALCH
Keyword(s):  
Natural Killer Cells ◽  
Natural Killer ◽  
Killer Cells ◽  
Human Natural Killer Cells ◽  
Leu 7

Recent advances on immunosuppressive drugs and remyelination enhancers for the treatment of multiple sclerosis

2021 ◽  
Vol 27 ◽  
Author(s):  
Jennifer Cadenas-Fernández ◽  
Pablo Ahumada-Pascual ◽  
Luis Sanz Andreu ◽  
Ana Velasco
Keyword(s):  
Multiple Sclerosis ◽  
Intracellular Signaling ◽  
Demyelinating Disease ◽  
Lipid Synthesis ◽  
Immunosuppressive Drugs ◽  
Nerve Fibers ◽  
Myelin Sheaths ◽  
Demyelinating Lesions ◽  
The Central Nervous System ◽  
Lipid Structures

: Mammalian nervous systems depend crucially on myelin sheaths covering the axons. In the central nervous system, myelin sheaths consist of lipid structures which are generated from the membrane of oligodendrocytes (OL). These sheaths allow fast nerve transmission, protect axons and provide them metabolic support. In response to specific traumas or pathologies, these lipid structures can be destabilized and generate demyelinating lesions. Multiple sclerosis (MS) is an example of a demyelinating disease in which the myelin sheaths surrounding the nerve fibers of the brain and spinal cord are damaged. MS is the leading cause of neurological disability in young adults in many countries, and its incidence has been increasing in recent decades. Related to its etiology, it is known that MS is an autoimmune and inflammatory CNS disease. However, there are no effective treatments for this disease and the immunomodulatory therapies that currently exist have proven limited success since they only delay the progress of the disease. Nowadays, one of the main goals in the MS research is to find treatments which allows the recovery of neurological disabilities due to demyelination. To this end, different approaches, such as modulating intracellular signaling or regulating the lipid metabolism of OLs, are being considered. Here, in addition to immunosuppressive or immunomodulatory drugs that reduce the immune response against myelin sheaths, we review a diverse group of drugs that promotes endogenous remyelination in MS patients and whose use may be interesting as potential therapeutic agents in MS disease. To this end, we compile specific treatments against MS that are currently in the market with remyelination strategies which have entered into human clinical trials for future reparative MS therapies. The method used in this study is a systematic literature review on PubMed, Web of Science and Science Direct databases up to May 31, 2020. To narrow down the search results in databases, more specific keywords, such as, “myelin sheath”, “remyelination”, “demyelination”, “oligodendrocyte” and “lipid synthesis” were used to focus the search. We favoured papers published after January, 2015, but did not exclude earlier seminal papers.

Early Reactive Changes at Myelin Sheaths Gaps (nodes of Ranvier) of Nerve Fibers (a supravital study)

2012 ◽  
Vol 42 (7) ◽  
pp. 775-779
Author(s):  
O. S. Sotnikov ◽  
T. N. Kokurina ◽  
I. A. Solovyova ◽  
S. S. Sergeeva
Keyword(s):  
Nerve Fibers ◽  
Nodes Of Ranvier ◽  
Myelin Sheaths ◽  
Reactive Changes

Maternal Smoking and Pulmonary Neuroendocrine Cells in Sudden Infant Death Syndrome

PEDIATRICS ◽  
1996 ◽  
Vol 98 (4) ◽  
pp. 668-672
Author(s):  
Ernest Cutz ◽  
Donald G. Perrin ◽  
Richard Hackman ◽  
Elinor N. Czegledy-Nagy
Keyword(s):  
Sudden Infant Death Syndrome ◽  
Infant Death ◽  
Airway Epithelium ◽  
Maternal Smoking ◽  
Matched Control ◽  
Sudden Infant Death ◽  
Neuroendocrine Cells ◽  
Sudden Infant ◽  
Neuroepithelial Bodies ◽  
Pulmonary Neuroendocrine Cells

Background. Maternal smoking is a well-recognized risk factor for sudden infant death syndrome (SIDS), but the precise mechanism is unknown. We tested a hypothesis that maternal smoking affects pulmonary neuroendocrine cells (PNECs) and neuroepithelial bodies (NEBs), which are innervated PNEC clusters and presumed airway chemoreceptors. Methods. Lung sections from infants who died of SIDS and whose mothers smoked during pregnancy (n = 22), infants who died of SIDS and whose mothers were nonsmokers (n = 17), and age-matched control infants (n = 15) who died of other causes were immunostained for bombesin (a PNEC and NEB marker) and assessed morphometrically. Results. The frequency of PNEC (the percentage of airway epithelium immunoreactive for bombesin) was increased up to twofold in the lungs of infants who died of SIDS (7.7 ± 0.4%) compared with controls (4.9 ± 0.4%), as was the frequency (40 ± 3.5 vs 23 ± 3.7/cm2) and size (748 ± 46.5 vs 491 ± 25.8,µm2) of NEBs. In infants who died of SIDS and who were born to smoking mothers, PNEC frequency was increased significantly compared with that in those born to nonsmoking mothers, but the frequency and size of NEBs were not significantly different between the two groups. Conclusion. Our findings suggest that maternal smoking potentiates hyperplasia of the PNEC system in the lungs of infants who die of SIDS and that a dysfunction of these cells may contribute to the pathophysiology of SIDS.

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