Short term labeling of proteins, gangliosides and glycoproteins of the optic tract of chickens exposed to light or darkness.

Neurochem Int

Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Ciudad Universitaria, 5016-Córdoba, Argentina.

Published: October 2012

In contrast with previous findings of the labeling of the glycosidic moieties of the gangliosides and glycoproteins in chickens injected with N-[ (3)H ] acetylmannosamine , the labeling of the ganglion cell layer and optic tectum proteins of chicks exposed to light after an intraocular injection of [(3)H]proline showed no differences with those of their counterpart chickens that remained in darkness. The same failure in finding a difference was met when the cytosolic or the particulate proteins or the acid soluble fraction in the retina were compared. Cycloheximide and puromycin inhibited the labeling of retina and optic tectum proteins, gangliosides and glycoproteins in both illumination conditions. Since the labelings in the optic tectum appeared more inhibited than those in the retina ganglion cell layer it was concluded that cycloheximide and puromycin, besides the synthesis of those compounds, also inhibit their axonal transport. On the basis of these contrasting results the working hypothesis is advanced that light stimulation enhances the activity of the Golgi apparatus but not (or less) that of the polyribosomes.

Download full-text PDF

Source
http://dx.doi.org/10.1016/0197-0186(84)90101-3DOI Listing

Publication Analysis

Top Keywords

gangliosides glycoproteins
12
optic tectum
12
proteins gangliosides
8
exposed light
8
ganglion cell
8
cell layer
8
tectum proteins
8
cycloheximide puromycin
8
short term
4
labeling
4

Similar Publications

Most studies on the docking of ivermectin on the spike protein of SARS-CoV-2 concern the receptor binding domain (RBD) and, more precisely, the RBD interface recognized by the ACE2 receptor. The N-terminal domain (NTD), which controls the initial attachment of the virus to lipid raft gangliosides, has not received the attention it deserves. In this study, we combined molecular modeling and physicochemical approaches to analyze the mode of interaction of ivermectin with the interface of the NTD-facing lipid rafts of the host cell membrane.

View Article and Find Full Text PDF

A 40-year-old man presented to our hospital with subacute progressive muscle weakness in the limbs and leukocytosis. Subsequently, the patient was diagnosed with chronic lymphocytic leukemia (CLL) complicated by peripheral motor neuron neuropathy (axonopathy). Serology test for anti-ganglioside GM2 IgG antibody was positive, whereas paraneoplastic syndrome-related and anti-myelin-associated glycoprotein antibodies were not detected.

View Article and Find Full Text PDF

Mechanistic and Therapeutic Implications of Protein and Lipid Sialylation in Human Diseases.

Int J Mol Sci

November 2024

Analytical Research and Development, Biotherapeutics Pharmaceutical Sciences, Pfizer Inc., Andover, MA 01810, USA.

Glycan structures of glycoproteins and glycolipids on the surface glycocalyx and luminal sugar layers of intracellular membrane compartments in human cells constitute a key interface between intracellular biological processes and external environments. Sialic acids, a class of alpha-keto acid sugars with a nine-carbon backbone, are frequently found as the terminal residues of these glycoconjugates, forming the critical components of these sugar layers. Changes in the status and content of cellular sialic acids are closely linked to many human diseases such as cancer, cardiovascular, neurological, inflammatory, infectious, and lysosomal storage diseases.

View Article and Find Full Text PDF

Sjogren's syndrome is an autoimmune disorder that has a prominent involvement of exocrine glands. Systemic involvement of other organs can also happen. Peripheral nervous system involvement is common and may present as axonal sensory/sensorimotor or demyelinating polyneuropathy, mononeuritis multiplex, ganglionopathy, or cranial neuritis.

View Article and Find Full Text PDF

Background And Purpose: Complement factor C2 is a potential therapeutic target in immune-mediated neuropathies. However, literature suggests that classical complement pathway activation may proceed to C3 in the absence of C2, a so-called "C2 bypass." Here, we evaluated a C2 bypass mechanism during complement activation by pathogenic human IgM from patients with immune-mediated neuropathies.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!