Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

Interactions between bovine cornea proteoglycans and collagen

P Speziale, A Bardoni, C Balduini

The Biochemical Journal

|June 1, 1980

Summary

Bovine cornea proteoglycans interact with collagen, primarily through their chondroitin sulfate chains. Proteokeratan sulfate shows no significant collagen binding, indicating specific molecular interactions in corneal structure.

Related Concept Videos

You might also read

Related Articles

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

Sort by

Same author

The proline-rich tyrosine kinase Pyk2 regulates platelet integrin αIIbβ3 outside-in signaling.

Journal of thrombosis and haemostasis : JTH·2012

Same author

Calmodulin regulates the non-amyloidogenic metabolism of amyloid precursor protein in platelets.

Biochimica et biophysica acta·2010

Same author

Lysophosphatidic acid induces protein tyrosine phosphorylation in the absence of phospholipase C activation in human platelets.

Platelets·2010

Same author

Integrin alpha2beta1 induces phosphorylation-dependent and phosphorylation-independent activation of phospholipase Cgamma2 in platelets: role of Src kinase and Rac GTPase.

Journal of thrombosis and haemostasis : JTH·2009

Same author

Photodynamic action of merocyanine 540 on Staphylococcus epidermidis biofilms.

The International journal of artificial organs·2008

Same author

Staphylococcus biofilm components as targets for vaccines and drugs.

The International journal of artificial organs·2007

Area of Science:

Biochemistry
Biomaterials Science
Ocular Biology

Background:

Corneal structure relies on complex interactions between collagen and proteoglycans.
Proteoglycans in bovine cornea exist as an aggregate of proteochondroitin sulfate and proteokeratan sulfate subunits.
Understanding these interactions is crucial for corneal tissue engineering and disease research.

Purpose of the Study:

To investigate the specific interactions between bovine corneal collagen and its constituent proteoglycan subunits.
To determine which proteoglycan component is responsible for binding to collagen.

Main Methods:

Isolation of type-I collagen from bovine cornea.
Coupling collagen to CNBr-activated Sepharose 4B to create an affinity column.
Chromatography of proteochondroitin sulfate, proteokeratan sulfate, and their aggregate on collagen-Sepharose and control columns.
Enzymatic digestion with chondroitinase to assess the role of chondroitin sulfate chains.

Main Results:

The proteochondroitin sulfate subunit and the proteoglycan aggregate showed retarded elution on the collagen-Sepharose column, indicating binding.
The proteokeratan sulfate subunit did not interact with the collagen-Sepharose column.
Chondroitinase digestion abolished the interaction, confirming chondroitin sulfate chains mediate collagen binding.

Conclusions:

Chondroitin sulfate chains of corneal proteoglycans are the primary mediators of interaction with type-I collagen.
Proteokeratan sulfate does not directly bind to corneal collagen.
These findings elucidate specific molecular interactions fundamental to corneal extracellular matrix organization.

Related Experiment Videos