Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.8K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
2.8K
Proteoglycans01:05

Proteoglycans

3.9K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K
Protein Glycosylation01:25

Protein Glycosylation

6.7K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
6.7K
Glucose Transporters01:27

Glucose Transporters

22.4K
Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:
22.4K
Serum Laboratory Studies, Stool Test, Breath Test01:30

Serum Laboratory Studies, Stool Test, Breath Test

299
Gastrointestinal (GI) diagnostic studies are pivotal in confirming, ruling out, diagnosing, or staging various diseases, including cancers. Following diagnosis, allocating time for discussions with the patient and providing informational resources is crucial. Diagnostic assessments of the GI tract often occur in outpatient settings like endoscopy suites or GI labs. Preparation for these tests may include dietary restrictions, fasting, liquid bowel preparations, laxatives, enemas, and the...
299

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Raloxifene inhibits the proliferation of pediatric acute myeloid leukemia by targeting the ANP32B gene and regulating C-MYC expression.

Hematology (Amsterdam, Netherlands)·2026
Same author

GABRD promotes hepatocellular carcinoma progression via the IL-10RA/JAK2-STAT3 signaling axis.

Cell death & disease·2026
Same author

Intrinsic mechanisms underlying urban-rural disparities in physical activity and their changes in China: evidence from China General Social Survey during 2010-2021.

Frontiers in public health·2026
Same author

Selective filtering of relevant sensory signals in parietal cortex.

Research square·2026
Same author

Cytosolic Peptide: N-Glycanase (NGLY1)-from Basic Biology to Genetic Disorder, NGLY1 Deficiency.

Advances in experimental medicine and biology·2026
Same author

Research Progress and Prospects of Modified Biochar in the Adsorption and Degradation of Sulfonamide Antibiotics.

Antibiotics (Basel, Switzerland)·2026

Related Experiment Video

Updated: May 29, 2025

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors
10:17

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

6.2K

Free oligosaccharides in serum.

Chengcheng Huang1, Akinobu Honda2, Tadashi Suzuki2

  • 1Chemical Glycobiology Laboratory, Institute for Glyco-core (iGOCRE), Tokai National Higher Education and Research System Nagoya University, Furo-cho, Nagoya, Aichi 464-8601, Japan.

BBA Advances
|February 3, 2025
PubMed
Summary
This summary is machine-generated.

Free N-glycans (FNGs) in serum have distinct structures and formation mechanisms compared to intracellular FNGs. Their biological roles are currently under investigation, suggesting novel functions for these extracellular sugars.

Keywords:
ENGaseFree oligosaccharidesNgly1OligosaccharyltransferaseSerumfree N-glycans

More Related Videos

OLIgo Mass Profiling OLIMP of Extracellular Polysaccharides
08:43

OLIgo Mass Profiling OLIMP of Extracellular Polysaccharides

Published on: June 20, 2010

13.7K
Automated Modular High Throughput Exopolysaccharide Screening Platform Coupled with Highly Sensitive Carbohydrate Fingerprint Analysis
12:02

Automated Modular High Throughput Exopolysaccharide Screening Platform Coupled with Highly Sensitive Carbohydrate Fingerprint Analysis

Published on: April 11, 2016

11.4K

Related Experiment Videos

Last Updated: May 29, 2025

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors
10:17

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

6.2K
OLIgo Mass Profiling OLIMP of Extracellular Polysaccharides
08:43

OLIgo Mass Profiling OLIMP of Extracellular Polysaccharides

Published on: June 20, 2010

13.7K
Automated Modular High Throughput Exopolysaccharide Screening Platform Coupled with Highly Sensitive Carbohydrate Fingerprint Analysis
12:02

Automated Modular High Throughput Exopolysaccharide Screening Platform Coupled with Highly Sensitive Carbohydrate Fingerprint Analysis

Published on: April 11, 2016

11.4K

Area of Science:

  • Glycobiology
  • Biochemistry
  • Molecular Biology

Background:

  • Glycans, or sugar chains, attached to proteins and lipids significantly alter molecular properties and functions.
  • Intracellular free N-glycans (FNGs) have known processing pathways but unclear biological functions.
  • Extracellular free oligosaccharides are present in animal sera, distinct from intracellular FNGs.

Purpose of the Study:

  • To review current knowledge on the structures and formation mechanisms of serum free oligosaccharides.
  • To explore potential biological functions of extracellular FNGs.
  • To highlight the differences between intracellular and extracellular FNGs.

Main Methods:

  • Literature review of existing studies on free oligosaccharides in serum.
  • Analysis of structural classifications of extracellular FNGs.
  • Comparison of formation mechanisms for intracellular and extracellular FNGs.

Main Results:

  • Extracellular FNGs in serum are classified into sialyl FNGs, oligomannose-type FNGs, and sialyl lactose/N-acetyllactosamine-type glycans.
  • Structural features of extracellular FNGs differ from intracellular FNGs, suggesting distinct origins.
  • The formation mechanisms of serum free oligosaccharides are proposed to be unique.

Conclusions:

  • Serum free oligosaccharides represent a distinct glycan pool with unique structural and formation characteristics.
  • Further research is needed to elucidate the specific biological functions of these extracellular FNGs.
  • Understanding extracellular FNGs may reveal novel roles in physiological processes.