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Related Concept Videos

Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Introduction to Actin01:26

Introduction to Actin

Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across different species.
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

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Related Experiment Video

Updated: Jun 13, 2026

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

Structural and functional characterization of human kallistatin.

Stephanie T D Pham1, Kristian W Nielsen2, Jonas H Graversen1

  • 1Inflammation Research Unit, Department of Molecular Medicine, University of Southern Denmark, Odense, Denmark.

Biochemistry and Biophysics Reports
|June 12, 2026
PubMed
Summary

Kallistatin, a serine protease inhibitor, is stabilized by glycosylation, which prevents polymerization and maintains its function. Deglycosylation increases polymerization but not inhibitory activity, highlighting glycosylation

Keywords:
Abdominal aortic aneurysmELISAGlycosylationKallistatinMass spectrometryPolymerization

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The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
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Identification of Functional Protein Regions Through Chimeric Protein Construction

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Related Experiment Videos

Last Updated: Jun 13, 2026

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis
19:16

The Importance of Correct Protein Concentration for Kinetics and Affinity Determination in Structure-function Analysis

Published on: March 17, 2010

Identification of Functional Protein Regions Through Chimeric Protein Construction
11:39

Identification of Functional Protein Regions Through Chimeric Protein Construction

Published on: January 8, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Vascular Biology

Background:

  • Kallistatin is a serine protease inhibitor (serpin) that inhibits tissue kallikrein, crucial for vascular homeostasis.
  • The structural properties, glycosylation, and polymerization potential of human kallistatin are not well understood.

Purpose of the Study:

  • To characterize the structural features, glycosylation, and polymerization of human kallistatin.
  • To develop tools for quantifying kallistatin in biological samples.
  • To investigate the role of glycosylation in kallistatin stability and function.

Main Methods:

  • Generation of kallistatin-specific monoclonal antibodies.
  • Development of a sandwich ELISA for kallistatin quantification.
  • Mass spectrometry to identify glycosylation sites.
  • Biochemical assays to assess polymerization and inhibitory activity.
  • Analysis of vascular tissue from patients with abdominal aortic aneurysm.

Main Results:

  • Established monoclonal antibodies and a sensitive ELISA for kallistatin quantification.
  • Confirmed glycosylation at Asn 33 and characterized other glycosylation sites.
  • Demonstrated that kallistatin can polymerize, and deglycosylation enhances this process.
  • Showed that glycosylation stabilizes kallistatin against polymerization, while deglycosylation retains inhibitory function.

Conclusions:

  • Glycosylation plays a critical role in stabilizing kallistatin structure and preventing polymerization.
  • Glycosylation primarily impacts structural stability rather than directly modulating inhibitory capacity.
  • The developed tools and findings provide a foundation for further research into kallistatin's physiological and pathological roles.