Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. / Couchman, J R; Caterson, B; Christner, J E; Baker, J R.

In: Nature, Vol. 307, No. 5952, 1984, p. 650-2.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Couchman, JR, Caterson, B, Christner, JE & Baker, JR 1984, 'Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues.', Nature, vol. 307, no. 5952, pp. 650-2.

APA

Couchman, J. R., Caterson, B., Christner, J. E., & Baker, J. R. (1984). Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. Nature, 307(5952), 650-2.

Vancouver

Couchman JR, Caterson B, Christner JE, Baker JR. Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. Nature. 1984;307(5952):650-2.

Author

Couchman, J R ; Caterson, B ; Christner, J E ; Baker, J R. / Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. In: Nature. 1984 ; Vol. 307, No. 5952. pp. 650-2.

Bibtex

@article{462259a0598d11dd8d9f000ea68e967b,
title = "Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues.",
abstract = "Chondroitin sulphate proteoglycans are widespread connective tissue components and chemical analysis of cartilage and other proteoglycans has demonstrated molecular speciation involving the degree and position of sulphation of the carbohydrate chains. This may, in turn, affect the properties of the glycosaminoglycan (GAG), particularly with respect to self-association and interactions with other extracellular matrix components. Interactions with specific molecules from different connective tissue types, such as the collagens and their associated glycoproteins, could be favoured by particular charge organizations on the GAG molecule endowed by the sulphate groups. So far, it has not been possible to identify and map chondroitins of differing sulphation in tissues, but we have now raised three monoclonal antibodies which specifically recognize unsulphated, 4-sulphated and 6-sulphated chondroitin and dermatan sulphate. These provide novel opportunities to study the in vivo distribution of chondroitin sulphate proteoglycans. We demonstrate that chondroitin sulphates exhibit remarkable connective tissue specificity and furthermore provide evidence that some proteoglycans may predominantly carry only one type of chondroitin sulphate chain.",
author = "Couchman, {J R} and B Caterson and Christner, {J E} and Baker, {J R}",
note = "Keywords: Animals; Antibodies, Monoclonal; Antibody Specificity; Chondroitin; Chondroitin Sulfates; Connective Tissue; Glycosaminoglycans; Proteoglycans; Rats; Tissue Distribution",
year = "1984",
language = "English",
volume = "307",
pages = "650--2",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",
number = "5952",

}

RIS

TY - JOUR

T1 - Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues.

AU - Couchman, J R

AU - Caterson, B

AU - Christner, J E

AU - Baker, J R

N1 - Keywords: Animals; Antibodies, Monoclonal; Antibody Specificity; Chondroitin; Chondroitin Sulfates; Connective Tissue; Glycosaminoglycans; Proteoglycans; Rats; Tissue Distribution

PY - 1984

Y1 - 1984

N2 - Chondroitin sulphate proteoglycans are widespread connective tissue components and chemical analysis of cartilage and other proteoglycans has demonstrated molecular speciation involving the degree and position of sulphation of the carbohydrate chains. This may, in turn, affect the properties of the glycosaminoglycan (GAG), particularly with respect to self-association and interactions with other extracellular matrix components. Interactions with specific molecules from different connective tissue types, such as the collagens and their associated glycoproteins, could be favoured by particular charge organizations on the GAG molecule endowed by the sulphate groups. So far, it has not been possible to identify and map chondroitins of differing sulphation in tissues, but we have now raised three monoclonal antibodies which specifically recognize unsulphated, 4-sulphated and 6-sulphated chondroitin and dermatan sulphate. These provide novel opportunities to study the in vivo distribution of chondroitin sulphate proteoglycans. We demonstrate that chondroitin sulphates exhibit remarkable connective tissue specificity and furthermore provide evidence that some proteoglycans may predominantly carry only one type of chondroitin sulphate chain.

AB - Chondroitin sulphate proteoglycans are widespread connective tissue components and chemical analysis of cartilage and other proteoglycans has demonstrated molecular speciation involving the degree and position of sulphation of the carbohydrate chains. This may, in turn, affect the properties of the glycosaminoglycan (GAG), particularly with respect to self-association and interactions with other extracellular matrix components. Interactions with specific molecules from different connective tissue types, such as the collagens and their associated glycoproteins, could be favoured by particular charge organizations on the GAG molecule endowed by the sulphate groups. So far, it has not been possible to identify and map chondroitins of differing sulphation in tissues, but we have now raised three monoclonal antibodies which specifically recognize unsulphated, 4-sulphated and 6-sulphated chondroitin and dermatan sulphate. These provide novel opportunities to study the in vivo distribution of chondroitin sulphate proteoglycans. We demonstrate that chondroitin sulphates exhibit remarkable connective tissue specificity and furthermore provide evidence that some proteoglycans may predominantly carry only one type of chondroitin sulphate chain.

M3 - Journal article

C2 - 6420711

VL - 307

SP - 650

EP - 652

JO - Nature

JF - Nature

SN - 0028-0836

IS - 5952

ER -

ID: 5167735