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Related Concept Videos

Detergent Purification of Membrane Proteins01:18

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...

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Revisiting the matricellular concept.

Matrix biology : journal of the International Society for Matrix Biology·2014
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Overexpression of SPARC in human trabecular meshwork increases intraocular pressure and alters extracellular matrix.

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SPARC fusion protein induces cellular adhesive signaling.

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Combinatorial targeting and discovery of ligand-receptors in organelles of mammalian cells.

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Control of excitatory CNS synaptogenesis by astrocyte-secreted proteins Hevin and SPARC.

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Proteolysis of the matricellular protein hevin by matrix metalloproteinase-3 produces a SPARC-like fragment (SLF) associated with neovasculature in a murine glioma model.

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Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
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Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase

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Purification of SPARC/osteonectin.

E Helene Sage1

  • 1The Hope Heart Institute, Seattle, Washington, USA.

Current Protocols in Cell Biology
|January 30, 2008
PubMed
Summary

Secreted protein acidic and rich in cysteine (SPARC) is purified from mammalian cells, E. coli, Sf9 cells, and platelets. Assays evaluate SPARC

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Secreted protein acidic and rich in cysteine (SPARC), also known as osteonectin or BM/40, is a matricellular protein.
  • SPARC plays a critical role in regulating cell adhesion, extracellular matrix production, growth factor activity, and the cell cycle.

Purpose of the Study:

  • To describe the purification methods for SPARC from various sources, including cultured mammalian cells, E. coli, Sf9 cells, and human blood platelets.
  • To detail assays for evaluating SPARC activity, specifically its effects on cell de-adhesion and inhibition of cellular proliferation in vitro.

Main Methods:

  • Purification of native SPARC from cultured mammalian cells.
  • Purification of recombinant SPARC (rSPARC) from prokaryotic (E. coli) and eukaryotic (Sf9) expression systems.

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Purification of Progenitors from Skeletal Muscle

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  • Isolation of SPARC from human blood platelets.
  • In vitro assays to measure SPARC's de-adhesion and anti-proliferative activities.

    • Main Results:

    • Established protocols for obtaining purified SPARC from diverse biological sources.
    • Demonstrated the functional activity of purified SPARC in vitro, including its ability to inhibit cell adhesion and proliferation.
    • Highlighted the expression of SPARC during tissue remodeling and repair processes.

    Conclusions:

    • SPARC can be effectively purified using various methods suitable for different research needs.
    • SPARC exhibits functional activities relevant to cellular processes and tissue repair.
    • The expression pattern of SPARC suggests its potential as a therapeutic target for fibrotic diseases, cancers, and angiogenesis-related disorders.