Arterial chondroitin sulfate proteoglycan: localization with a monoclonal antibody.

We generated a monoclonal antibody (Mab) against a large chondroitin sulfate proteoglycan (CSPG) isolated from bovine aorta. This Mab (941) immunoprecipitates a CSPG synthesized by cultured monkey arterial smooth muscle cells. The immunoprecipitated CSPG is totally susceptible to chondroitinase ABC digestion and possesses a core glycoprotein of Mr approximately 400-500 KD. By use of immunofluorescence light microscopy and immunogold electron microscopy, the PG recognized by this Mab was shown to be deposited in the extracellular matrix of monkey arterial smooth muscle cell cultures in clusters which were not part of other fibrous matrix components and not associated with the cell's plasma membrane. With similar immunolocalization techniques, the CSPG antigen was found enriched in the intima and present in the medial portions of normal blood vessels, as well as in the interstitial matrix of thickened intimal lesions of atherosclerotic vessels. Immunoelectron microscopy revealed that this CSPG was confined principally to the space within the extracellular matrix not occupied by other matrix components, such as collagen and elastic fibers. These results indicate that this particular proteoglycan has a specific but restricted distribution in the extracellular matrix of arterial tissue.

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Characterization of a Chondroitin Sulfate Proteoglycan Synthesized by Monkey Arterial Smooth Muscle Cellsin Vitro

Connective Tissue Research ◽

10.3109/03008209209007001 ◽

1992 ◽

Vol 27 (4) ◽

pp. 265-277 ◽

Cited By ~ 6

Author(s):

Tet-Kin Yeo ◽

Stephen Macfarlane ◽

Thomas N. Wight

Keyword(s):

Smooth Muscle ◽

Chondroitin Sulfate ◽

Chondroitin Sulfate Proteoglycan ◽

Sulfate Proteoglycan ◽

Arterial Smooth Muscle

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Amphibian neural crest cell migration on purified extracellular matrix components: a chondroitin sulfate proteoglycan inhibits locomotion on fibronectin substrates.

The Journal of Cell Biology ◽

10.1083/jcb.105.6.2511 ◽

1987 ◽

Vol 105 (6) ◽

pp. 2511-2521 ◽

Cited By ~ 94

Author(s):

R Perris ◽

S Johansson

Keyword(s):

Extracellular Matrix ◽

Cell Migration ◽

Neural Crest ◽

Chondroitin Sulfate ◽

Neural Crest Cell ◽

Chondroitin Sulfate Proteoglycan ◽

Dependent Manner ◽

Sulfate Proteoglycan ◽

Extracellular Matrix Components ◽

Matrix Components

The ability of purified extracellular matrix components to promote the initial migration of amphibian neural crest (NC) cells was quantitatively investigated in vitro. NC cells migrated avidly on fibronectin (FN), displaying progressively more extensive dispersion at increasing amounts of material incorporated in the substrate. In contrast, dispersion on laminin substrates was optimal at low protein concentrations but strongly reduced at high concentrations. NC cells were unable to migrate on substrates containing a high molecular mass chondroitin sulfate proteoglycan (ChSP). When proteolytic peptides, representing isolated functional domains of the FN molecule, were tested as potential migration substrates, the cell binding region of the molecule (105 kD) was found to be as active as the intact FN. A 31-kD heparin-binding fragment also stimulated NC cell migration, whereas NC cells dispersed to a markedly lower extent on the isolated collagen-binding domain (40 kD), or the latter domain linked to the NH2-terminal part of the FN molecule. Migration on the intact FN was partially inhibited by antibodies directed against the 105- and 31-kD fragments, respectively; dispersion was further decreased when the antibodies were used in combination. Addition of the ChSP to the culture medium dramatically perturbed NC cell migration on substrates of FN, as well as of 105- or 31-kD fragments. However, preincubation of isolated cells or substrates with ChSP followed by washing did not affect NC cell movement. The use of substrates consisting of different relative amounts of ChSP and the 105-kD peptide revealed that ChSP counteracted the motility-promoting activity of the 105-kD FN fragment in a concentration-dependent manner also when bound to the substrate. Our results indicate that NC cell migration on FN involves two separate domains of the molecule, and that ChSP can modulate the migratory behavior of NC cells moving along FN-rich pathways and may therefore influence directionally and subsequent localization of NC cells in the embryo.

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Detection of chondroitin sulfates and decorin in developing fetal and neonatal rat lung

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.00160.2001 ◽

2002 ◽

Vol 282 (3) ◽

pp. L484-L490 ◽

Cited By ~ 18

Author(s):

Yiqiong Wang ◽

Kaori Sakamoto ◽

Jody Khosla ◽

Philip L. Sannes

Keyword(s):

Extracellular Matrix ◽

Chondroitin Sulfate ◽

Wide Distribution ◽

Neonatal Rat ◽

Chondroitin Sulfate Proteoglycan ◽

Sulfate Proteoglycan ◽

Rat Lung ◽

Adult Rats ◽

Chondroitin Sulfates ◽

Monospecific Antibodies

Chondroitin sulfates and their related proteoglycans are components of extracellular matrix that act as key determinants of growth and differentiation characteristics of developing lungs. Changes in their immunohistochemical distribution during progressive organ maturation were examined with monospecific antibodies to chondroitin sulfate, a nonbasement membrane chondroitin sulfate proteoglycan, and the specific chondroitin sulfate-containing proteoglycan decorin in whole fetuses and lungs from newborn and adult rats. Alveolar and airway extracellular matrix immunostained heavily in the prenatal rat for both chondroitin sulfate and chondroitin sulfate proteoglycan, whereas decorin was confined to developing airways and vessels. These sites retained their respective levels of reactivity with all antibodies through 1–10 days postnatal but thereafter became progressively more diminished and focal in alveolar regions. The heavy staining seen early in development was interpreted to reflect a significant and wide distribution of chondroitin sulfates, chondroitin sulfate proteoglycans, and decorin in rapidly growing tissues, whereas the reduced and more focal reactivity observed at later time points coincided with known focal patterns of localization of fibrillar elements of the extracellular matrix and a more differentiated state.

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